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<p><span>Polyclonal antibody raised in rabbit against <strong>MeCP2</strong> (<strong>Methyl-CpG-binding domain protein 2</strong>), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><small><strong> Figure 1 ChIP results obtained with the Diagenode antibody directed against MeCP2</strong><br /> ChIP assays were performed using human osteosarcoma (U2OS) cells, the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) and optimized PCR primer sets. Sheared chromatin from 1x10e6 cells and 5 μg of antibody were used per ChIP experiment. IgG (1 μg/IP) was used as a negative IP control. Quantitative PCR was performed with primers for the promoters of the ZMYND10 gene (used as a positive control) and CDC6 gene (used as a negative control). Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<p><span>Polyclonal antibody raised in rabbit against <strong>MeCP2</strong> (<strong>Methyl-CpG-binding domain protein 2</strong>), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410052_fig3.jpg" alt="MeCP2 Antibody for ChIP" /></p>
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<p><small><strong> Figure 1 ChIP results obtained with the Diagenode antibody directed against MeCP2</strong><br /> ChIP assays were performed using human osteosarcoma (U2OS) cells, the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) and optimized PCR primer sets. Sheared chromatin from 1x10e6 cells and 5 μg of antibody were used per ChIP experiment. IgG (1 μg/IP) was used as a negative IP control. Quantitative PCR was performed with primers for the promoters of the ZMYND10 gene (used as a positive control) and CDC6 gene (used as a negative control). Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<td>1:1,000</td>
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<p><span>Polyclonal antibody raised in rabbit against <strong>MeCP2</strong> (<strong>Methyl-CpG-binding domain protein 2</strong>), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<p><small><strong> Figure 1 ChIP results obtained with the Diagenode antibody directed against MeCP2</strong><br /> ChIP assays were performed using human osteosarcoma (U2OS) cells, the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) and optimized PCR primer sets. Sheared chromatin from 1x10e6 cells and 5 μg of antibody were used per ChIP experiment. IgG (1 μg/IP) was used as a negative IP control. Quantitative PCR was performed with primers for the promoters of the ZMYND10 gene (used as a positive control) and CDC6 gene (used as a negative control). Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410052_fig1.jpg" alt="MeCP2 Antibody ELISA validated " /></p>
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<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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'description' => '<p><strong>Western blot</strong> : The quality of antibodies used in this technique is crucial for correct and specific protein identification. Diagenode offers huge selection of highly sensitive and specific western blot-validated antibodies.</p>
<p>Learn more about: <a href="https://www.diagenode.com/applications/western-blot">Loading control, MW marker visualization</a><em>. <br /></em></p>
<p><em></em>Check our selection of antibodies validated in Western blot.</p>',
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<div class="small-10 columns">
<h3>Epigenetic antibodies you can trust!</h3>
<p>Antibody quality is essential for assay success. Diagenode offers antibodies that are actually validated and have been widely used and published by the scientific community. Now we are adding a new level of siRNA knockdown validation to assure the specificity of our non-histone antibodies.</p>
<p><strong>Short interfering RNA (siRNA)</strong> degrades target mRNA, followed by the knock-down of protein production. If the antibody that recognizes the protein of interest is specific, the Western blot of siRNA-treated cells will show a significant reduction of signal vs. untreated cells.</p>
<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
</div>
<div class="small-2 columns">
<p><img src="https://www.diagenode.com/emailing/images/epi-success-guaranteed-icon.png" alt="Epigenetic success guaranteed" /></p>
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<div class="spaced"></div>
<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>',
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
<ul>
<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
<li>Expert technical support</li>
<li>Sample sizes available</li>
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'description' => '<p><span style="font-weight: 400;">All Diagenode’s antibodies are listed below. Please, use our Quick search field to find the antibody of interest by target name, application, purity.</span></p>
<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
<li>Expert technical support</li>
<li>Sample sizes available</li>
<li>100% satisfaction guarantee</li>
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<div class="small-12 columns"><center></center>
<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
<p></p>
</div>
</div>
<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
<div class="row">
<div class="small-12 medium-6 large-6 columns"><img src="https://www.diagenode.com/img/product/antibodies/C15410003-fig1-ChIP.jpg" alt="" width="400" height="315" /> </div>
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<p></p>
<p></p>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'description' => '<p style="text-align: justify;"><span>Epigenetic research tools have evolved over time from endpoint PCR to qPCR to the analyses of large sets of genome-wide sequencing data. ChIP sequencing (ChIP-seq) has now become the gold standard method for chromatin studies, given the accuracy and coverage scale of the approach over other methods. Successful ChIP-seq, however, requires a higher level of experimental accuracy and consistency in all steps of ChIP than ever before. Particularly crucial is the quality of ChIP antibodies. </span></p>',
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'name' => 'Mu opioid receptor expressing neurons in the rostral ventromedial medullaare the source of mechanical hypersensitivity induced by repeated restraintstress.',
'authors' => 'Imbe Hiroki and Ihara Hayato',
'description' => '<p>Repeated exposure to psychophysical stress often causes an increase in sensitivity and response to pain. This phenomenon is commonly called stress-induced hyperalgesia (SIH). Although psychophysical stress is a well-known risk factor for numerous chronic pain syndromes, the neural mechanism underlying SIH has not yet been elucidated. The rostral ventromedial medulla (RVM) is a key output element of the descending pain modulation system. Descending signals from the RVM have a major impact on spinal nociceptive neurotransmission. In the present study, to clarify changes in the descending pain modulatory system in rats with SIH, we examined the expression of Mu opioid receptor (MOR) mRNA, MeCP2 and global DNA methylation in the RVM after repeated restraint stress for 3 weeks. Additionally, we microinjected neurotoxin dermorphin-SAP into the RVM. The repeated restraint stress for 3 weeks induced mechanical hypersensitivity in the hind paw, a significant increase in the expression of MOR mRNA and MeCP2, and a significant decrease in global DNA methylation in the RVM. The MeCP2 binding to MOR gene promoter in the RVM was significantly decreased in rats with repeated restraint stress. Furthermore, microinjection of dermorphin-SAP into the RVM prevented the mechanical hypersensitivity induced by repeated restraint stress. Although, because of the lack of specific antibody to MOR, we could not show a quantitative analysis in the number of MOR-expressing neurons after the microinjection, these results suggest that MOR-expressing neurons in the RVM induce SIH after repeated restraint stress.</p>',
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'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37331575',
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'name' => 'Epigenetic Silencing of OR and TAS2R Genes Expression inHuman Orbitofrontal Cortex At Early Stages of SporadicAlzheimer’s Disease',
'authors' => 'Alves Victoria Cunha et al.',
'description' => '<p>Modulation of brain olfactory (OR) and taste receptors (TASR) expression was recently reported in neurological diseases. We explored the possible expression and regulation of selected OR and TASR genes in human orbitofrontal cortex of sporadic Alzheimer’s disease (AD) and found that these are expressed and markedly downregulated at early stages. The expression pattern did not follow disease progression suggesting regulation through epigenetic mechanisms. We found an increase of global H3K9me3 levels and substantial enrichment of this repressive signature at ORs and TAS2Rs proximal promoter at early stages, ultimately lost at advanced stages. By mass spectrometry-based proteomic and further validation, we found that H3K9me3 interacts with MeCP2 at early stages and that this protein is increased in sporadic AD. Findings suggest MeCP2 might be implicated in OR and TAS2R genes expression regulation through interaction with H3K9me3, and as an early event, it may uncover a novel etiopathogenetic mechanism of sporadic AD.</p>',
'date' => '2021-12-01',
'pmid' => 'https://doi.org/10.21203%2Frs.3.rs-1098461%2Fv1',
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'id' => '4242',
'name' => 'Rett syndrome linked to defects in forming the MeCP2/Rbfox/LASRcomplex in mouse models',
'authors' => 'Jiang Yan et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder and a leading cause of intellectual disability in young females. RTT is mainly caused by mutations found in the X-linked gene encoding methyl-CpG binding protein 2 (MeCP2). Despite extensive studies, the molecular mechanism underlying RTT pathogenesis is still poorly understood. Here, we report MeCP2 as a key subunit of a higher-order multiunit protein complex Rbfox/LASR. Defective MeCP2 in RTT mouse models disrupts the assembly of the MeCP2/Rbfox/LASR complex, leading to reduced binding of Rbfox proteins to target pre-mRNAs and aberrant splicing of Nrxns and Nlgn1 critical for synaptic plasticity. We further show that MeCP2 disease mutants display defective condensate properties and fail to promote phase-separated condensates with Rbfox proteins in vitro and in cultured cells. These data link an impaired function of MeCP2 with disease mutation in splicing control to its defective properties in mediating the higher-order assembly of the MeCP2/Rbfox/LASR complex.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34599184',
'doi' => '10.1038/s41467-021-26084-3',
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'id' => '4324',
'name' => 'Environmental enrichment preserves a young DNA methylation landscape inthe aged mouse hippocampus',
'authors' => 'Zocher S. et al. ',
'description' => '<p>The decline of brain function during aging is associated with epigenetic changes, including DNA methylation. Lifestyle interventions can improve brain function during aging, but their influence on age-related epigenetic changes is unknown. Using genome-wide DNA methylation sequencing, we here show that experiencing a stimulus-rich environment counteracts age-related DNA methylation changes in the hippocampal dentate gyrus of mice. Specifically, environmental enrichment prevented the aging-induced CpG hypomethylation at target sites of the methyl-CpG-binding protein Mecp2, which is critical to neuronal function. The genes at which environmental enrichment counteracted aging effects have described roles in neuronal plasticity, neuronal cell communication and adult hippocampal neurogenesis and are dysregulated with age-related cognitive decline in the human brain. Our results highlight the stimulating effects of environmental enrichment on hippocampal plasticity at the level of DNA methylation and give molecular insights into the specific aspects of brain aging that can be counteracted by lifestyle interventions.</p>',
'date' => '2021-06-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34162876',
'doi' => '10.1038/s41467-021-23993-1',
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'name' => 'MeCP2 controls neural stem cell fate specification throughmiR-199a-mediated inhibition of BMP-Smad signaling.',
'authors' => 'Nakashima H. et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder, with impaired brain development caused by mutations in MECP2; however, the underlying mechanism remains elusive. We know from previous work that MeCP2 facilitates the processing of a specific microRNA, miR-199a, by associating with the Drosha complex to regulate neuronal functions. Here, we show that the MeCP2/miR-199a axis regulates neural stem/precursor cell (NS/PC) differentiation. A shift occurs from neuronal to astrocytic differentiation of MeCP2- and miR-199a-deficient NS/PCs due to the upregulation of a miR-199a target, Smad1, a downstream transcription factor of bone morphogenetic protein (BMP) signaling. Moreover, miR-199a expression and treatment with BMP inhibitors rectify the differentiation of RTT patient-derived NS/PCs and development of brain organoids, respectively, suggesting that facilitation of BMP signaling accounts for the impaired RTT brain development. Our study illuminates the molecular pathology of RTT and reveals the MeCP2/miR-199a/Smad1 axis as a potential therapeutic target for RTT.</p>',
'date' => '2021-05-01',
'pmid' => 'https://doi.org/10.1016%2Fj.celrep.2021.109124',
'doi' => '10.1016/j.celrep.2021.109124',
'modified' => '2022-08-03 16:35:57',
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'id' => '4032',
'name' => 'MeCP2 regulates gene expression through recognition of H3K27me3.',
'authors' => 'Lee, W and Kim, J and Yun, JM and Ohn, T and Gong, Q',
'description' => '<p>MeCP2 plays a multifaceted role in gene expression regulation and chromatin organization. Interaction between MeCP2 and methylated DNA in the regulation of gene expression is well established. However, the widespread distribution of MeCP2 suggests it has additional interactions with chromatin. Here we demonstrate, by both biochemical and genomic analyses, that MeCP2 directly interacts with nucleosomes and its genomic distribution correlates with that of H3K27me3. In particular, the methyl-CpG-binding domain of MeCP2 shows preferential interactions with H3K27me3. We further observe that the impact of MeCP2 on transcriptional changes correlates with histone post-translational modification patterns. Our findings indicate that MeCP2 interacts with genomic loci via binding to DNA as well as histones, and that interaction between MeCP2 and histone proteins plays a key role in gene expression regulation.</p>',
'date' => '2020-07-19',
'pmid' => 'http://www.pubmed.gov/32561780',
'doi' => '10.1038/s41467-020-16907-0',
'modified' => '2020-12-16 18:05:17',
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'id' => '3720',
'name' => 'Genome-wide methylation in alcohol use disorder subjects: implications for an epigenetic regulation of the cortico-limbic glucocorticoid receptors (NR3C1).',
'authors' => 'Gatta E, Grayson DR, Auta J, Saudagar V, Dong E, Chen Y, Krishnan HR, Drnevich J, Pandey SC, Guidotti A',
'description' => '<p>Environmental factors, including substance abuse and stress, cause long-lasting changes in the regulation of gene expression in the brain via epigenetic mechanisms, such as DNA methylation. We examined genome-wide DNA methylation patterns in the prefrontal cortex (PFC, BA10) of 25 pairs of control and individuals with alcohol use disorder (AUD), using the Infinium MethylationEPIC BeadChip. We identified 5254 differentially methylated CpGs (p < 0.005). Bioinformatic analyses highlighted biological processes containing genes related to stress adaptation, including the glucocorticoid receptor (encoded by NR3C1). Considering that alcohol is a stressor, we focused our attention on differentially methylated regions of the NR3C1 gene and validated the differential methylation of several genes in the NR3C1 network. Chronic alcohol drinking results in a significant increased methylation of the NR3C1 exon variant 1, with a particular increase in the levels of 5-hydroxymethylcytosine over 5-methylcytosine. These changes in DNA methylation were associated with reduced NR3C1 mRNA and protein expression levels in PFC, as well as other cortico-limbic regions of AUD subjects when compared with controls. Furthermore, we show that the expression of several stress-responsive genes (e.g., CRF, POMC, and FKBP5) is altered in the PFC of AUD subjects. These stress-response genes were also changed in the hippocampus, a region that is highly susceptible to stress. These data suggest that alcohol-dependent aberrant DNA methylation of NR3C1 and consequent changes in other stress-related genes might be fundamental in the pathophysiology of AUD and lay the groundwork for treatments targeting the epigenetic mechanisms regulating NR3C1 in AUD.</p>',
'date' => '2019-06-25',
'pmid' => 'http://www.pubmed.gov/31239533',
'doi' => '10.1038/s41380-019-0449-6',
'modified' => '2019-07-04 18:07:16',
'created' => '2019-07-04 10:42:34',
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(int) 7 => array(
'id' => '3333',
'name' => 'The L1 adhesion molecule normalizes neuritogenesis in Rett syndrome-derived neural precursor cells',
'authors' => 'Yoo M. et al.',
'description' => '<p>Therapeutic intervention is an important need in ameliorating the severe consequences of Rett Syndrome (RTT), a neurological disorder caused by mutations in the X-linked gene methyl-CpG-binding protein-2 (MeCP2). Following previously observed morphological defects in induced pluripotent stem cell (iPSC)-derived neurons obtained from female RTT patients, we hypothesized that transfection with the L1 cell adhesion molecule (L1) could contribute to normalizing a pathological male cell system bearing a nonsense mutation of MeCP2. We found a decreased expression of L1 in RTT iPSCs-derived neural precursor cells (RTT NPCs) and decreased neuritogenesis. Expression of wild-type MeCP2 in RTTNPCs revealed a positive correlation between the levels of MeCP2 and L1, and normalization of cell survival. Expression of L1 in RTTNPCs enhanced neuritogenesis and soma size. Knock-down of MeCP2 in wild type NPCs reduced neuritogenesis. L1 expression is regulated by the MeCP2 promoter. These results suggest that a deficiency in L1 may partially account for RTT phenotypes.</p>',
'date' => '2017-12-16',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/29050935',
'doi' => '',
'modified' => '2018-02-08 17:13:12',
'created' => '2018-02-08 17:13:12',
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[maximum depth reached]
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(int) 8 => array(
'id' => '3142',
'name' => 'Epigenetic regulation of RELN and GAD1 in the frontal cortex (FC) of autism spectrum disorder (ASD) subjects',
'authors' => 'Zhubi A. et al.',
'description' => '<p>Both Reelin (RELN) and glutamate decarboxylase 67 (GAD1) have been implicated in the pathophysiology of Autism Spectrum Disorders (ASD). We have previously shown that both mRNAs are reduced in the cerebella (CB) of ASD subjects through a mechanism that involves increases in the amounts of MECP2 binding to the corresponding promoters. In the current study, we examined the expression of RELN, GAD1, GAD2, and several other mRNAs implicated in this disorder in the frontal cortices (FC) of ASD and CON subjects. We also focused on the role that epigenetic processes play in the regulation of these genes in ASD brain. Our goal is to better understand the molecular basis for the down-regulation of genes expressed in GABAergic neurons in ASD brains. We measured mRNA levels corresponding to selected GABAergic genes using qRT-PCR in RNA isolated from both ASD and CON groups. We determined the extent of binding of MECP2 and DNMT1 repressor proteins by chromatin immunoprecipitation (ChIP) assays. The amount of 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) present in the promoters of the target genes was quantified by methyl DNA immunoprecipitation (MeDIP) and hydroxyl MeDIP (hMeDIP). We detected significant reductions in the mRNAs associated with RELN and GAD1 and significant increases in mRNAs encoding the Ten-eleven Translocation (TET) enzymes 1, 2, and 3. We also detected increased MECP2 and DNMT1 binding to the corresponding promoter regions of GAD1, RELN, and GAD2. Interestingly, there were decreased amounts of 5mC at both promoters and little change in 5hmC content in these same DNA fragments. Our data demonstrate that RELN, GAD1, and several other genes selectively expressed in GABAergic neurons, are down-regulated in post-mortem ASD FC. In addition, we observed increased DNMT1 and MECP2 binding at the corresponding promoters of these genes. The finding of increased MECP2 binding to the RELN, GAD1 and GAD2 promoters, with reduced amounts of 5mC and unchanged amounts of 5hmC present in these regions, suggests the possibility that DNMT1 interacts with and alters MECP2 binding properties to selected promoters. Comparisons between data obtained from the FC with CB studies showed some common themes between brain regions which are discussed.</p>',
'date' => '2017-02-14',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28229923',
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'name' => 'The heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a novel tumor regulator and a prognostic marker in breast cancer',
'authors' => 'Mao X, Gauche C, Coughtrie MW, Bui C, Gulberti S, Merhi-Soussi F, Ramalanjaona N, Bertin-Jung I, Diot A, Dumas D, De Freitas Caires N, Thompson AM, Bourdon JC, Ouzzine M, Fournel-Gigleux S',
'description' => '<p>Heparan sulfate (HS) proteoglycan chains are key components of the breast tumor microenvironment that critically influence the behavior of cancer cells. It is established that abnormal synthesis and processing of HS play a prominent role in tumorigenesis, albeit mechanisms remain mostly obscure. HS function is mainly controlled by sulfotransferases, and here we report a novel cellular and pathophysiological significance for the 3-O-sulfotransferase 3-OST3A (HS3ST3A), catalyzing the final maturation step of HS, in breast cancer. We show that 3-OST3A is epigenetically repressed in all breast cancer cell lines of a panel representative of distinct molecular subgroups, except in human epidermal growth factor receptor 2-positive (HER2+) sloan-kettering breast cancer (SKBR3) cells. Epigenetic mechanisms involved both DNA methylation and histone modifications, producing different repressive chromatin environments depending on the cell molecular signature. Gain and loss of function experiments by cDNA and siRNA transfection revealed profound effects of 3-OST3A expression on cell behavior including apoptosis, proliferation, response to trastuzumab in vitro and tumor growth in xenografted mice. 3-OST3A exerted dual activities acting as tumor-suppressor in lumA-michigan cancer foundation (MCF)-7 and triple negative-MD Anderson (MDA) metastatic breast (MB)-231 cells, or as an oncogenic factor in HER2+-SKBR3 cells. Mechanistically, fluorescence-resonance energy transfer-fluorescence-lifetime imaging microscopy experiments indicated that the effects of 3-OST3A in MCF-7 cells were mediated by altered interactions between HS and fibroblast growth factor-7 (FGF-7). Further, this interplay between HS and FGF-7 modulated downstream ERK, AKT and p38 cascades, suggesting that altering 3-O-sulfation affects FGFR2IIIb-mediated signaling. Corroborating our cellular data, a clinical study conducted in a cohort of breast cancer patients uncovered that, in HER2+ patients, high level expression of 3-OST3A in tumors was associated with reduced relapse-free survival. Our findings define 3-OST3A as a novel regulator of breast cancer pathogenicity, displaying tumor-suppressive or oncogenic activities in a cell- and tumor-dependent context, and demonstrate the clinical value of the HS-O-sulfotransferase 3-OST3A as a prognostic marker in HER2+ patients.</p>',
'date' => '2016-04-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/27041583',
'doi' => ' 10.1038/onc.2016.44',
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'name' => 'Sequence features accurately predict genome-wide MeCP2 binding in vivo',
'authors' => 'Rube HT, Lee W, Hejna M, Chen H, Yasui DH, Hess JF, LaSalle JM, Song JS, Gong Q',
'description' => '<p>Methyl-CpG binding protein 2 (MeCP2) is critical for proper brain development and expressed at near-histone levels in neurons, but the mechanism of its genomic localization remains poorly understood. Using high-resolution MeCP2-binding data, we show that DNA sequence features alone can predict binding with 88<span class="mb">%</span> accuracy. Integrating MeCP2 binding and DNA methylation in a probabilistic graphical model, we demonstrate that previously reported genome-wide association with methylation is in part due to MeCP2’s affinity to GC-rich chromatin, a result replicated using published data. Furthermore, MeCP2 co-localizes with nucleosomes. Finally, MeCP2 binding downstream of promoters correlates with increased expression in <i>Mecp2</i>-deficient neurons.</p>',
'date' => '2016-03-24',
'pmid' => 'http://www.nature.com/ncomms/2016/160324/ncomms11025/abs/ncomms11025.html',
'doi' => '10.1038/ncomms11025',
'modified' => '2016-04-06 10:42:59',
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'name' => 'Adrenergic Repression of the Epigenetic Reader MeCP2 Facilitates Cardiac Adaptation in Chronic Heart Failure',
'authors' => 'Mayer SC. et al.',
'description' => '<h4>RATIONALE:</h4>
<p><abstracttext label="RATIONALE" nlmcategory="BACKGROUND">In chronic heart failure, increased adrenergic activation contributes to structural remodeling and altered gene expression. Although adrenergic signaling alters histone modifications, it is unknown, whether it also affects other epigenetic processes, including DNA methylation and its recognition.</abstracttext></p>
<h4>OBJECTIVE:</h4>
<p><abstracttext label="OBJECTIVE" nlmcategory="OBJECTIVE">The aim of this study was to identify the mechanism of regulation of the methyl-CpG-binding protein 2 (MeCP2) and its functional significance during cardiac pressure overload and unloading.</abstracttext></p>
<h4>METHODS AND RESULTS:</h4>
<p><abstracttext label="METHODS AND RESULTS" nlmcategory="RESULTS">MeCP2 was identified as a reversibly repressed gene in mouse hearts after transverse aortic constriction and was normalized after removal of the constriction. Similarly, MeCP2 repression in human failing hearts resolved after unloading by a left ventricular assist device. The cluster miR-212/132 was upregulated after transverse aortic constriction or on activation of α1- and β1-adrenoceptors and miR-212/132 led to repression of MeCP2. Prevention of MeCP2 repression by a cardiomyocyte-specific, doxycycline-regulatable transgenic mouse model aggravated cardiac hypertrophy, fibrosis, and contractile dysfunction after transverse aortic constriction. Ablation of MeCP2 in cardiomyocytes facilitated recovery of failing hearts after reversible transverse aortic constriction. Genome-wide expression analysis, chromatin immunoprecipitation experiments, and DNA methylation analysis identified mitochondrial genes and their transcriptional regulators as MeCP2 target genes. Coincident with its repression, MeCP2 was removed from its target genes, whereas DNA methylation of MeCP2 target genes remained stable during pressure overload.</abstracttext></p>
<h4>CONCLUSIONS:</h4>
<p><abstracttext label="CONCLUSIONS" nlmcategory="CONCLUSIONS">These data connect adrenergic activation with a microRNA-MeCP2 epigenetic pathway that is important for cardiac adaptation during the development and recovery from heart failure.</abstracttext></p>',
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'name' => 'Dynamic CCAAT/Enhancer Binding Protein-Associated Changes of DNA Methylation in the Angiotensinogen Gene.',
'authors' => 'Wang F, Demura M, Cheng Y, Zhu A, Karashima S, Yoneda T, Demura Y, Maeda Y, Namiki M, Ono K, Nakamura Y, Sasano H, Akagi T, Yamagishi M, Saijoh K, Takeda Y.',
'description' => 'DNA methylation patterns are maintained in adult somatic cells. Recent findings, however, suggest that all methylation patterns are not preserved. We demonstrate that stimulatory signals can change the DNA methylation status at a CCAAT/enhancer binding protein (CEBP) binding site and a transcription start site and activate expression of the angiotensinogen gene (AGT). A CEBP binding site in the human AGT promoter was hypomethylated in tissues with high expression of AGT, but not in those with low expression. The transcriptional activity of AGT promoter sequences cloned into a reporter plasmid depended on DNA methylation. In cultured human cells, interleukin 6 stimulation caused DNA demethylation around a CEBP binding site and a transcription start site; demethylation was accompanied by increased CEBP-β recruitment and chromatin accessibility of the AGT promoter. DNA methylation activity decreased in the nucleus. Excess circulating aldosterone upregulated AGT expression and was accompanied by DNA hypomethylation around a CEBP binding site and a transcription start site in human visceral adipose tissue. High salt intake led to upregulation of Agt expression, DNA hypomethylation around 2 CEBP binding sites and a transcription start site, and decreased DNA methylation activity in rat visceral adipose tissue. Taken together, CEBP binding initiates chromatin relaxation and transcription, which are followed by DNA demethylation around a CEBP binding site and a transcription start site in the AGT promoter. Decreased DNA methylation activity in the nucleus may play a role in DNA demethylation. DNA demethylation switches the phenotype of AGT expression from an inactive to an active state.',
'date' => '2013-11-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/24191285',
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'name' => 'Survival motor neuron gene 2 silencing by DNA methylation correlates with spinal muscular atrophy disease severity and can be bypassed by histone deacetylase inhibition.',
'authors' => 'Hauke J, Riessland M, Lunke S, Eyüpoglu IY, Blümcke I, El-Osta A, Wirth B, Hahnen E',
'description' => 'Spinal muscular atrophy (SMA), a common neuromuscular disorder, is caused by homozygous absence of the survival motor neuron gene 1 (SMN1), while the disease severity is mainly influenced by the number of SMN2 gene copies. This correlation is not absolute, suggesting the existence of yet unknown factors modulating disease progression. We demonstrate that the SMN2 gene is subject to gene silencing by DNA methylation. SMN2 contains four CpG islands which present highly conserved methylation patterns and little interindividual variations in SMN1-deleted SMA patients. The comprehensive analysis of SMN2 methylation in patients suffering from severe versus mild SMA carrying identical SMN2 copy numbers revealed a correlation of CpG methylation at the positions -290 and -296 with the disease severity and the activity of the first transcriptional start site of SMN2 at position -296. These results provide first evidence that SMN2 alleles are functionally not equivalent due to differences in DNA methylation. We demonstrate that the methyl-CpG-binding protein 2, a transcriptional repressor, binds to the critical SMN2 promoter region in a methylation-dependent manner. However, inhibition of SMN2 gene silencing conferred by DNA methylation might represent a promising strategy for pharmacologic SMA therapy. We identified histone deacetylase (HDAC) inhibitors including vorinostat and romidepsin which are able to bypass SMN2 gene silencing by DNA methylation, while others such as valproic acid and phenylbutyrate do not, due to HDAC isoenzyme specificities. These findings indicate that DNA methylation is functionally important regarding SMA disease progression and pharmacological SMN2 gene activation which might have implications for future SMA therapy regimens.',
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<div class="small-10 columns">
<h3>Epigenetic antibodies you can trust!</h3>
<p>Antibody quality is essential for assay success. Diagenode offers antibodies that are actually validated and have been widely used and published by the scientific community. Now we are adding a new level of siRNA knockdown validation to assure the specificity of our non-histone antibodies.</p>
<p><strong>Short interfering RNA (siRNA)</strong> degrades target mRNA, followed by the knock-down of protein production. If the antibody that recognizes the protein of interest is specific, the Western blot of siRNA-treated cells will show a significant reduction of signal vs. untreated cells.</p>
<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
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<p><img src="https://www.diagenode.com/emailing/images/epi-success-guaranteed-icon.png" alt="Epigenetic success guaranteed" /></p>
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<div class="spaced"></div>
<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>',
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<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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'description' => 'MeCP2 (UniProt/Swiss-Prot entry P51608) is a chromosomal protein with abundant binding sites in the chromatin. It belongs to the family of methyl CpG binding proteins which also comprises MBD1, MBD2, MBD3 and MBD4. MeCP2 can bind specifically to methylated promoters, thereby repressing transcription. This transcriptional repression is mediated through interaction with histone deacetylase and the corepressor SIN3A. MeCP2 also is essential for development. Mutations in MeCP2 are the cause of several types of mental retardation including Rett syndrome, a progressive neurological disorder that causes mental retardation in females and mental retardation syndromic X-linked type 13, and may also be involved in Angelman syndrome and susceptibility to some types of autism.',
'clonality' => '',
'isotype' => '',
'lot' => 'A20-001P',
'concentration' => '1.2 µg/µl',
'reactivity' => 'Human',
'type' => 'Polyclonal',
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'classification' => 'Classic',
'application_table' => '<table>
<thead>
<tr>
<th>Applications</th>
<th>Suggested dilution</th>
<th>References</th>
</tr>
</thead>
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<tr>
<td>ChIP <sup>*</sup></td>
<td>5 μg/IP</td>
<td>Fig 1</td>
</tr>
<tr>
<td>ELISA</td>
<td>1:1,000</td>
<td>Fig 2</td>
</tr>
<tr>
<td>Western Blotting</td>
<td>1:1,000</td>
<td>Fig 3</td>
</tr>
</tbody>
</table>
<p><small><sup>*</sup> Please note that the optimal antibody amount per ChIP should be determined by the end-user. We recommend testing 1-5 μg per IP.</small></p>',
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'name' => 'MeCP2 Antibody ',
'description' => '<p><span>Alternative names: <strong>AUTSX3</strong>, <strong>MRX16</strong>, <strong>MRX79</strong>, <strong>MRXS13</strong>, <strong>MRXSL</strong>, <strong>PPMX</strong>, <strong>RTS</strong>, <strong>RTT</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against <strong>MeCP2</strong> (<strong>Methyl-CpG-binding domain protein 2</strong>), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410052_fig3.jpg" alt="MeCP2 Antibody for ChIP" /></p>
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<p><small><strong> Figure 1 ChIP results obtained with the Diagenode antibody directed against MeCP2</strong><br /> ChIP assays were performed using human osteosarcoma (U2OS) cells, the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) and optimized PCR primer sets. Sheared chromatin from 1x10e6 cells and 5 μg of antibody were used per ChIP experiment. IgG (1 μg/IP) was used as a negative IP control. Quantitative PCR was performed with primers for the promoters of the ZMYND10 gene (used as a positive control) and CDC6 gene (used as a negative control). Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><img src="https://www.diagenode.com/img/product/antibodies/C15410052_fig1.jpg" alt="MeCP2 Antibody ELISA validated " /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410052_fig2.jpg" alt="MeCP2 Antibody validated in Western Blot" /></p>
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<div class="small-8 columns">
<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<div class="row">
<div class="small-4 columns">
<p><img src="https://www.diagenode.com/img/product/antibodies/C15410052_wb_2.png" alt="MeCP2 Antibody validated in Western Blot" /></p>
</div>
<div class="small-8 columns">
<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<p>Learn more about: <a href="https://www.diagenode.com/applications/western-blot">Loading control, MW marker visualization</a><em>. <br /></em></p>
<p><em></em>Check our selection of antibodies validated in Western blot.</p>',
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<h3>Epigenetic antibodies you can trust!</h3>
<p>Antibody quality is essential for assay success. Diagenode offers antibodies that are actually validated and have been widely used and published by the scientific community. Now we are adding a new level of siRNA knockdown validation to assure the specificity of our non-histone antibodies.</p>
<p><strong>Short interfering RNA (siRNA)</strong> degrades target mRNA, followed by the knock-down of protein production. If the antibody that recognizes the protein of interest is specific, the Western blot of siRNA-treated cells will show a significant reduction of signal vs. untreated cells.</p>
<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
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<div class="small-2 columns">
<p><img src="https://www.diagenode.com/emailing/images/epi-success-guaranteed-icon.png" alt="Epigenetic success guaranteed" /></p>
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<div class="spaced"></div>
<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>',
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
<ul>
<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
<li>Expert technical support</li>
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
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<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<div class="small-12 medium-6 large-6 columns"><img src="https://www.diagenode.com/img/product/antibodies/C15410003-fig1-ChIP.jpg" alt="" width="400" height="315" /> </div>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'name' => 'Mu opioid receptor expressing neurons in the rostral ventromedial medullaare the source of mechanical hypersensitivity induced by repeated restraintstress.',
'authors' => 'Imbe Hiroki and Ihara Hayato',
'description' => '<p>Repeated exposure to psychophysical stress often causes an increase in sensitivity and response to pain. This phenomenon is commonly called stress-induced hyperalgesia (SIH). Although psychophysical stress is a well-known risk factor for numerous chronic pain syndromes, the neural mechanism underlying SIH has not yet been elucidated. The rostral ventromedial medulla (RVM) is a key output element of the descending pain modulation system. Descending signals from the RVM have a major impact on spinal nociceptive neurotransmission. In the present study, to clarify changes in the descending pain modulatory system in rats with SIH, we examined the expression of Mu opioid receptor (MOR) mRNA, MeCP2 and global DNA methylation in the RVM after repeated restraint stress for 3 weeks. Additionally, we microinjected neurotoxin dermorphin-SAP into the RVM. The repeated restraint stress for 3 weeks induced mechanical hypersensitivity in the hind paw, a significant increase in the expression of MOR mRNA and MeCP2, and a significant decrease in global DNA methylation in the RVM. The MeCP2 binding to MOR gene promoter in the RVM was significantly decreased in rats with repeated restraint stress. Furthermore, microinjection of dermorphin-SAP into the RVM prevented the mechanical hypersensitivity induced by repeated restraint stress. Although, because of the lack of specific antibody to MOR, we could not show a quantitative analysis in the number of MOR-expressing neurons after the microinjection, these results suggest that MOR-expressing neurons in the RVM induce SIH after repeated restraint stress.</p>',
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'name' => 'Epigenetic Silencing of OR and TAS2R Genes Expression inHuman Orbitofrontal Cortex At Early Stages of SporadicAlzheimer’s Disease',
'authors' => 'Alves Victoria Cunha et al.',
'description' => '<p>Modulation of brain olfactory (OR) and taste receptors (TASR) expression was recently reported in neurological diseases. We explored the possible expression and regulation of selected OR and TASR genes in human orbitofrontal cortex of sporadic Alzheimer’s disease (AD) and found that these are expressed and markedly downregulated at early stages. The expression pattern did not follow disease progression suggesting regulation through epigenetic mechanisms. We found an increase of global H3K9me3 levels and substantial enrichment of this repressive signature at ORs and TAS2Rs proximal promoter at early stages, ultimately lost at advanced stages. By mass spectrometry-based proteomic and further validation, we found that H3K9me3 interacts with MeCP2 at early stages and that this protein is increased in sporadic AD. Findings suggest MeCP2 might be implicated in OR and TAS2R genes expression regulation through interaction with H3K9me3, and as an early event, it may uncover a novel etiopathogenetic mechanism of sporadic AD.</p>',
'date' => '2021-12-01',
'pmid' => 'https://doi.org/10.21203%2Frs.3.rs-1098461%2Fv1',
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'name' => 'Rett syndrome linked to defects in forming the MeCP2/Rbfox/LASRcomplex in mouse models',
'authors' => 'Jiang Yan et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder and a leading cause of intellectual disability in young females. RTT is mainly caused by mutations found in the X-linked gene encoding methyl-CpG binding protein 2 (MeCP2). Despite extensive studies, the molecular mechanism underlying RTT pathogenesis is still poorly understood. Here, we report MeCP2 as a key subunit of a higher-order multiunit protein complex Rbfox/LASR. Defective MeCP2 in RTT mouse models disrupts the assembly of the MeCP2/Rbfox/LASR complex, leading to reduced binding of Rbfox proteins to target pre-mRNAs and aberrant splicing of Nrxns and Nlgn1 critical for synaptic plasticity. We further show that MeCP2 disease mutants display defective condensate properties and fail to promote phase-separated condensates with Rbfox proteins in vitro and in cultured cells. These data link an impaired function of MeCP2 with disease mutation in splicing control to its defective properties in mediating the higher-order assembly of the MeCP2/Rbfox/LASR complex.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34599184',
'doi' => '10.1038/s41467-021-26084-3',
'modified' => '2022-05-20 09:12:57',
'created' => '2022-05-19 10:41:50',
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(int) 3 => array(
'id' => '4324',
'name' => 'Environmental enrichment preserves a young DNA methylation landscape inthe aged mouse hippocampus',
'authors' => 'Zocher S. et al. ',
'description' => '<p>The decline of brain function during aging is associated with epigenetic changes, including DNA methylation. Lifestyle interventions can improve brain function during aging, but their influence on age-related epigenetic changes is unknown. Using genome-wide DNA methylation sequencing, we here show that experiencing a stimulus-rich environment counteracts age-related DNA methylation changes in the hippocampal dentate gyrus of mice. Specifically, environmental enrichment prevented the aging-induced CpG hypomethylation at target sites of the methyl-CpG-binding protein Mecp2, which is critical to neuronal function. The genes at which environmental enrichment counteracted aging effects have described roles in neuronal plasticity, neuronal cell communication and adult hippocampal neurogenesis and are dysregulated with age-related cognitive decline in the human brain. Our results highlight the stimulating effects of environmental enrichment on hippocampal plasticity at the level of DNA methylation and give molecular insights into the specific aspects of brain aging that can be counteracted by lifestyle interventions.</p>',
'date' => '2021-06-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34162876',
'doi' => '10.1038/s41467-021-23993-1',
'modified' => '2022-08-03 15:56:05',
'created' => '2022-05-19 10:41:50',
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[maximum depth reached]
)
),
(int) 4 => array(
'id' => '4347',
'name' => 'MeCP2 controls neural stem cell fate specification throughmiR-199a-mediated inhibition of BMP-Smad signaling.',
'authors' => 'Nakashima H. et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder, with impaired brain development caused by mutations in MECP2; however, the underlying mechanism remains elusive. We know from previous work that MeCP2 facilitates the processing of a specific microRNA, miR-199a, by associating with the Drosha complex to regulate neuronal functions. Here, we show that the MeCP2/miR-199a axis regulates neural stem/precursor cell (NS/PC) differentiation. A shift occurs from neuronal to astrocytic differentiation of MeCP2- and miR-199a-deficient NS/PCs due to the upregulation of a miR-199a target, Smad1, a downstream transcription factor of bone morphogenetic protein (BMP) signaling. Moreover, miR-199a expression and treatment with BMP inhibitors rectify the differentiation of RTT patient-derived NS/PCs and development of brain organoids, respectively, suggesting that facilitation of BMP signaling accounts for the impaired RTT brain development. Our study illuminates the molecular pathology of RTT and reveals the MeCP2/miR-199a/Smad1 axis as a potential therapeutic target for RTT.</p>',
'date' => '2021-05-01',
'pmid' => 'https://doi.org/10.1016%2Fj.celrep.2021.109124',
'doi' => '10.1016/j.celrep.2021.109124',
'modified' => '2022-08-03 16:35:57',
'created' => '2022-05-19 10:41:50',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 5 => array(
'id' => '4032',
'name' => 'MeCP2 regulates gene expression through recognition of H3K27me3.',
'authors' => 'Lee, W and Kim, J and Yun, JM and Ohn, T and Gong, Q',
'description' => '<p>MeCP2 plays a multifaceted role in gene expression regulation and chromatin organization. Interaction between MeCP2 and methylated DNA in the regulation of gene expression is well established. However, the widespread distribution of MeCP2 suggests it has additional interactions with chromatin. Here we demonstrate, by both biochemical and genomic analyses, that MeCP2 directly interacts with nucleosomes and its genomic distribution correlates with that of H3K27me3. In particular, the methyl-CpG-binding domain of MeCP2 shows preferential interactions with H3K27me3. We further observe that the impact of MeCP2 on transcriptional changes correlates with histone post-translational modification patterns. Our findings indicate that MeCP2 interacts with genomic loci via binding to DNA as well as histones, and that interaction between MeCP2 and histone proteins plays a key role in gene expression regulation.</p>',
'date' => '2020-07-19',
'pmid' => 'http://www.pubmed.gov/32561780',
'doi' => '10.1038/s41467-020-16907-0',
'modified' => '2020-12-16 18:05:17',
'created' => '2020-10-12 14:54:59',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 6 => array(
'id' => '3720',
'name' => 'Genome-wide methylation in alcohol use disorder subjects: implications for an epigenetic regulation of the cortico-limbic glucocorticoid receptors (NR3C1).',
'authors' => 'Gatta E, Grayson DR, Auta J, Saudagar V, Dong E, Chen Y, Krishnan HR, Drnevich J, Pandey SC, Guidotti A',
'description' => '<p>Environmental factors, including substance abuse and stress, cause long-lasting changes in the regulation of gene expression in the brain via epigenetic mechanisms, such as DNA methylation. We examined genome-wide DNA methylation patterns in the prefrontal cortex (PFC, BA10) of 25 pairs of control and individuals with alcohol use disorder (AUD), using the Infinium MethylationEPIC BeadChip. We identified 5254 differentially methylated CpGs (p < 0.005). Bioinformatic analyses highlighted biological processes containing genes related to stress adaptation, including the glucocorticoid receptor (encoded by NR3C1). Considering that alcohol is a stressor, we focused our attention on differentially methylated regions of the NR3C1 gene and validated the differential methylation of several genes in the NR3C1 network. Chronic alcohol drinking results in a significant increased methylation of the NR3C1 exon variant 1, with a particular increase in the levels of 5-hydroxymethylcytosine over 5-methylcytosine. These changes in DNA methylation were associated with reduced NR3C1 mRNA and protein expression levels in PFC, as well as other cortico-limbic regions of AUD subjects when compared with controls. Furthermore, we show that the expression of several stress-responsive genes (e.g., CRF, POMC, and FKBP5) is altered in the PFC of AUD subjects. These stress-response genes were also changed in the hippocampus, a region that is highly susceptible to stress. These data suggest that alcohol-dependent aberrant DNA methylation of NR3C1 and consequent changes in other stress-related genes might be fundamental in the pathophysiology of AUD and lay the groundwork for treatments targeting the epigenetic mechanisms regulating NR3C1 in AUD.</p>',
'date' => '2019-06-25',
'pmid' => 'http://www.pubmed.gov/31239533',
'doi' => '10.1038/s41380-019-0449-6',
'modified' => '2019-07-04 18:07:16',
'created' => '2019-07-04 10:42:34',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 7 => array(
'id' => '3333',
'name' => 'The L1 adhesion molecule normalizes neuritogenesis in Rett syndrome-derived neural precursor cells',
'authors' => 'Yoo M. et al.',
'description' => '<p>Therapeutic intervention is an important need in ameliorating the severe consequences of Rett Syndrome (RTT), a neurological disorder caused by mutations in the X-linked gene methyl-CpG-binding protein-2 (MeCP2). Following previously observed morphological defects in induced pluripotent stem cell (iPSC)-derived neurons obtained from female RTT patients, we hypothesized that transfection with the L1 cell adhesion molecule (L1) could contribute to normalizing a pathological male cell system bearing a nonsense mutation of MeCP2. We found a decreased expression of L1 in RTT iPSCs-derived neural precursor cells (RTT NPCs) and decreased neuritogenesis. Expression of wild-type MeCP2 in RTTNPCs revealed a positive correlation between the levels of MeCP2 and L1, and normalization of cell survival. Expression of L1 in RTTNPCs enhanced neuritogenesis and soma size. Knock-down of MeCP2 in wild type NPCs reduced neuritogenesis. L1 expression is regulated by the MeCP2 promoter. These results suggest that a deficiency in L1 may partially account for RTT phenotypes.</p>',
'date' => '2017-12-16',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/29050935',
'doi' => '',
'modified' => '2018-02-08 17:13:12',
'created' => '2018-02-08 17:13:12',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 8 => array(
'id' => '3142',
'name' => 'Epigenetic regulation of RELN and GAD1 in the frontal cortex (FC) of autism spectrum disorder (ASD) subjects',
'authors' => 'Zhubi A. et al.',
'description' => '<p>Both Reelin (RELN) and glutamate decarboxylase 67 (GAD1) have been implicated in the pathophysiology of Autism Spectrum Disorders (ASD). We have previously shown that both mRNAs are reduced in the cerebella (CB) of ASD subjects through a mechanism that involves increases in the amounts of MECP2 binding to the corresponding promoters. In the current study, we examined the expression of RELN, GAD1, GAD2, and several other mRNAs implicated in this disorder in the frontal cortices (FC) of ASD and CON subjects. We also focused on the role that epigenetic processes play in the regulation of these genes in ASD brain. Our goal is to better understand the molecular basis for the down-regulation of genes expressed in GABAergic neurons in ASD brains. We measured mRNA levels corresponding to selected GABAergic genes using qRT-PCR in RNA isolated from both ASD and CON groups. We determined the extent of binding of MECP2 and DNMT1 repressor proteins by chromatin immunoprecipitation (ChIP) assays. The amount of 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) present in the promoters of the target genes was quantified by methyl DNA immunoprecipitation (MeDIP) and hydroxyl MeDIP (hMeDIP). We detected significant reductions in the mRNAs associated with RELN and GAD1 and significant increases in mRNAs encoding the Ten-eleven Translocation (TET) enzymes 1, 2, and 3. We also detected increased MECP2 and DNMT1 binding to the corresponding promoter regions of GAD1, RELN, and GAD2. Interestingly, there were decreased amounts of 5mC at both promoters and little change in 5hmC content in these same DNA fragments. Our data demonstrate that RELN, GAD1, and several other genes selectively expressed in GABAergic neurons, are down-regulated in post-mortem ASD FC. In addition, we observed increased DNMT1 and MECP2 binding at the corresponding promoters of these genes. The finding of increased MECP2 binding to the RELN, GAD1 and GAD2 promoters, with reduced amounts of 5mC and unchanged amounts of 5hmC present in these regions, suggests the possibility that DNMT1 interacts with and alters MECP2 binding properties to selected promoters. Comparisons between data obtained from the FC with CB studies showed some common themes between brain regions which are discussed.</p>',
'date' => '2017-02-14',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28229923',
'doi' => '',
'modified' => '2017-03-23 14:58:21',
'created' => '2017-03-23 14:58:21',
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(int) 9 => array(
'id' => '2907',
'name' => 'The heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a novel tumor regulator and a prognostic marker in breast cancer',
'authors' => 'Mao X, Gauche C, Coughtrie MW, Bui C, Gulberti S, Merhi-Soussi F, Ramalanjaona N, Bertin-Jung I, Diot A, Dumas D, De Freitas Caires N, Thompson AM, Bourdon JC, Ouzzine M, Fournel-Gigleux S',
'description' => '<p>Heparan sulfate (HS) proteoglycan chains are key components of the breast tumor microenvironment that critically influence the behavior of cancer cells. It is established that abnormal synthesis and processing of HS play a prominent role in tumorigenesis, albeit mechanisms remain mostly obscure. HS function is mainly controlled by sulfotransferases, and here we report a novel cellular and pathophysiological significance for the 3-O-sulfotransferase 3-OST3A (HS3ST3A), catalyzing the final maturation step of HS, in breast cancer. We show that 3-OST3A is epigenetically repressed in all breast cancer cell lines of a panel representative of distinct molecular subgroups, except in human epidermal growth factor receptor 2-positive (HER2+) sloan-kettering breast cancer (SKBR3) cells. Epigenetic mechanisms involved both DNA methylation and histone modifications, producing different repressive chromatin environments depending on the cell molecular signature. Gain and loss of function experiments by cDNA and siRNA transfection revealed profound effects of 3-OST3A expression on cell behavior including apoptosis, proliferation, response to trastuzumab in vitro and tumor growth in xenografted mice. 3-OST3A exerted dual activities acting as tumor-suppressor in lumA-michigan cancer foundation (MCF)-7 and triple negative-MD Anderson (MDA) metastatic breast (MB)-231 cells, or as an oncogenic factor in HER2+-SKBR3 cells. Mechanistically, fluorescence-resonance energy transfer-fluorescence-lifetime imaging microscopy experiments indicated that the effects of 3-OST3A in MCF-7 cells were mediated by altered interactions between HS and fibroblast growth factor-7 (FGF-7). Further, this interplay between HS and FGF-7 modulated downstream ERK, AKT and p38 cascades, suggesting that altering 3-O-sulfation affects FGFR2IIIb-mediated signaling. Corroborating our cellular data, a clinical study conducted in a cohort of breast cancer patients uncovered that, in HER2+ patients, high level expression of 3-OST3A in tumors was associated with reduced relapse-free survival. Our findings define 3-OST3A as a novel regulator of breast cancer pathogenicity, displaying tumor-suppressive or oncogenic activities in a cell- and tumor-dependent context, and demonstrate the clinical value of the HS-O-sulfotransferase 3-OST3A as a prognostic marker in HER2+ patients.</p>',
'date' => '2016-04-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/27041583',
'doi' => ' 10.1038/onc.2016.44',
'modified' => '2016-05-09 09:58:38',
'created' => '2016-05-09 09:58:38',
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[maximum depth reached]
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),
(int) 10 => array(
'id' => '2882',
'name' => 'Sequence features accurately predict genome-wide MeCP2 binding in vivo',
'authors' => 'Rube HT, Lee W, Hejna M, Chen H, Yasui DH, Hess JF, LaSalle JM, Song JS, Gong Q',
'description' => '<p>Methyl-CpG binding protein 2 (MeCP2) is critical for proper brain development and expressed at near-histone levels in neurons, but the mechanism of its genomic localization remains poorly understood. Using high-resolution MeCP2-binding data, we show that DNA sequence features alone can predict binding with 88<span class="mb">%</span> accuracy. Integrating MeCP2 binding and DNA methylation in a probabilistic graphical model, we demonstrate that previously reported genome-wide association with methylation is in part due to MeCP2’s affinity to GC-rich chromatin, a result replicated using published data. Furthermore, MeCP2 co-localizes with nucleosomes. Finally, MeCP2 binding downstream of promoters correlates with increased expression in <i>Mecp2</i>-deficient neurons.</p>',
'date' => '2016-03-24',
'pmid' => 'http://www.nature.com/ncomms/2016/160324/ncomms11025/abs/ncomms11025.html',
'doi' => '10.1038/ncomms11025',
'modified' => '2016-04-06 10:42:59',
'created' => '2016-04-06 10:42:59',
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[maximum depth reached]
)
),
(int) 11 => array(
'id' => '2858',
'name' => 'Adrenergic Repression of the Epigenetic Reader MeCP2 Facilitates Cardiac Adaptation in Chronic Heart Failure',
'authors' => 'Mayer SC. et al.',
'description' => '<h4>RATIONALE:</h4>
<p><abstracttext label="RATIONALE" nlmcategory="BACKGROUND">In chronic heart failure, increased adrenergic activation contributes to structural remodeling and altered gene expression. Although adrenergic signaling alters histone modifications, it is unknown, whether it also affects other epigenetic processes, including DNA methylation and its recognition.</abstracttext></p>
<h4>OBJECTIVE:</h4>
<p><abstracttext label="OBJECTIVE" nlmcategory="OBJECTIVE">The aim of this study was to identify the mechanism of regulation of the methyl-CpG-binding protein 2 (MeCP2) and its functional significance during cardiac pressure overload and unloading.</abstracttext></p>
<h4>METHODS AND RESULTS:</h4>
<p><abstracttext label="METHODS AND RESULTS" nlmcategory="RESULTS">MeCP2 was identified as a reversibly repressed gene in mouse hearts after transverse aortic constriction and was normalized after removal of the constriction. Similarly, MeCP2 repression in human failing hearts resolved after unloading by a left ventricular assist device. The cluster miR-212/132 was upregulated after transverse aortic constriction or on activation of α1- and β1-adrenoceptors and miR-212/132 led to repression of MeCP2. Prevention of MeCP2 repression by a cardiomyocyte-specific, doxycycline-regulatable transgenic mouse model aggravated cardiac hypertrophy, fibrosis, and contractile dysfunction after transverse aortic constriction. Ablation of MeCP2 in cardiomyocytes facilitated recovery of failing hearts after reversible transverse aortic constriction. Genome-wide expression analysis, chromatin immunoprecipitation experiments, and DNA methylation analysis identified mitochondrial genes and their transcriptional regulators as MeCP2 target genes. Coincident with its repression, MeCP2 was removed from its target genes, whereas DNA methylation of MeCP2 target genes remained stable during pressure overload.</abstracttext></p>
<h4>CONCLUSIONS:</h4>
<p><abstracttext label="CONCLUSIONS" nlmcategory="CONCLUSIONS">These data connect adrenergic activation with a microRNA-MeCP2 epigenetic pathway that is important for cardiac adaptation during the development and recovery from heart failure.</abstracttext></p>',
'date' => '2015-09-11',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/26195221',
'doi' => '10.1161/CIRCRESAHA.115.306721',
'modified' => '2016-03-15 14:12:52',
'created' => '2016-03-15 14:12:52',
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(int) 12 => array(
'id' => '1742',
'name' => 'Dynamic CCAAT/Enhancer Binding Protein-Associated Changes of DNA Methylation in the Angiotensinogen Gene.',
'authors' => 'Wang F, Demura M, Cheng Y, Zhu A, Karashima S, Yoneda T, Demura Y, Maeda Y, Namiki M, Ono K, Nakamura Y, Sasano H, Akagi T, Yamagishi M, Saijoh K, Takeda Y.',
'description' => 'DNA methylation patterns are maintained in adult somatic cells. Recent findings, however, suggest that all methylation patterns are not preserved. We demonstrate that stimulatory signals can change the DNA methylation status at a CCAAT/enhancer binding protein (CEBP) binding site and a transcription start site and activate expression of the angiotensinogen gene (AGT). A CEBP binding site in the human AGT promoter was hypomethylated in tissues with high expression of AGT, but not in those with low expression. The transcriptional activity of AGT promoter sequences cloned into a reporter plasmid depended on DNA methylation. In cultured human cells, interleukin 6 stimulation caused DNA demethylation around a CEBP binding site and a transcription start site; demethylation was accompanied by increased CEBP-β recruitment and chromatin accessibility of the AGT promoter. DNA methylation activity decreased in the nucleus. Excess circulating aldosterone upregulated AGT expression and was accompanied by DNA hypomethylation around a CEBP binding site and a transcription start site in human visceral adipose tissue. High salt intake led to upregulation of Agt expression, DNA hypomethylation around 2 CEBP binding sites and a transcription start site, and decreased DNA methylation activity in rat visceral adipose tissue. Taken together, CEBP binding initiates chromatin relaxation and transcription, which are followed by DNA demethylation around a CEBP binding site and a transcription start site in the AGT promoter. Decreased DNA methylation activity in the nucleus may play a role in DNA demethylation. DNA demethylation switches the phenotype of AGT expression from an inactive to an active state.',
'date' => '2013-11-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/24191285',
'doi' => '',
'modified' => '2015-07-24 15:39:01',
'created' => '2015-07-24 15:39:01',
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[maximum depth reached]
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(int) 13 => array(
'id' => '81',
'name' => 'Survival motor neuron gene 2 silencing by DNA methylation correlates with spinal muscular atrophy disease severity and can be bypassed by histone deacetylase inhibition.',
'authors' => 'Hauke J, Riessland M, Lunke S, Eyüpoglu IY, Blümcke I, El-Osta A, Wirth B, Hahnen E',
'description' => 'Spinal muscular atrophy (SMA), a common neuromuscular disorder, is caused by homozygous absence of the survival motor neuron gene 1 (SMN1), while the disease severity is mainly influenced by the number of SMN2 gene copies. This correlation is not absolute, suggesting the existence of yet unknown factors modulating disease progression. We demonstrate that the SMN2 gene is subject to gene silencing by DNA methylation. SMN2 contains four CpG islands which present highly conserved methylation patterns and little interindividual variations in SMN1-deleted SMA patients. The comprehensive analysis of SMN2 methylation in patients suffering from severe versus mild SMA carrying identical SMN2 copy numbers revealed a correlation of CpG methylation at the positions -290 and -296 with the disease severity and the activity of the first transcriptional start site of SMN2 at position -296. These results provide first evidence that SMN2 alleles are functionally not equivalent due to differences in DNA methylation. We demonstrate that the methyl-CpG-binding protein 2, a transcriptional repressor, binds to the critical SMN2 promoter region in a methylation-dependent manner. However, inhibition of SMN2 gene silencing conferred by DNA methylation might represent a promising strategy for pharmacologic SMA therapy. We identified histone deacetylase (HDAC) inhibitors including vorinostat and romidepsin which are able to bypass SMN2 gene silencing by DNA methylation, while others such as valproic acid and phenylbutyrate do not, due to HDAC isoenzyme specificities. These findings indicate that DNA methylation is functionally important regarding SMA disease progression and pharmacological SMN2 gene activation which might have implications for future SMA therapy regimens.',
'date' => '2009-01-15',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/18971205',
'doi' => '',
'modified' => '2015-07-24 15:38:56',
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'id' => '2214',
'antibody_id' => '203',
'name' => 'MeCP2 Antibody (sample size)',
'description' => '<p><span>Alternative names: <strong>AUTSX3</strong>, <strong>MRX16</strong>, <strong>MRX79</strong>, <strong>MRXS13</strong>, <strong>MRXSL</strong>, <strong>PPMX</strong>, <strong>RTS</strong>, <strong>RTT</strong></span></p>
<p><span>Polyclonal antibody raised in rabbit against <strong>MeCP2</strong> (Methyl-CpG-binding domain protein 2), using a KLH-conjugated synthetic peptide containing a sequence from the C-terminal part of the protein.</span></p>',
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'format' => '10 µg',
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<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
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<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>',
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<p><small><strong> Figure 1 ChIP results obtained with the Diagenode antibody directed against MeCP2</strong><br /> ChIP assays were performed using human osteosarcoma (U2OS) cells, the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) and optimized PCR primer sets. Sheared chromatin from 1x10e6 cells and 5 μg of antibody were used per ChIP experiment. IgG (1 μg/IP) was used as a negative IP control. Quantitative PCR was performed with primers for the promoters of the ZMYND10 gene (used as a positive control) and CDC6 gene (used as a negative control). Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<p><small><strong> Figure 1 ChIP results obtained with the Diagenode antibody directed against MeCP2</strong><br /> ChIP assays were performed using human osteosarcoma (U2OS) cells, the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) and optimized PCR primer sets. Sheared chromatin from 1x10e6 cells and 5 μg of antibody were used per ChIP experiment. IgG (1 μg/IP) was used as a negative IP control. Quantitative PCR was performed with primers for the promoters of the ZMYND10 gene (used as a positive control) and CDC6 gene (used as a negative control). Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<h3>Epigenetic antibodies you can trust!</h3>
<p>Antibody quality is essential for assay success. Diagenode offers antibodies that are actually validated and have been widely used and published by the scientific community. Now we are adding a new level of siRNA knockdown validation to assure the specificity of our non-histone antibodies.</p>
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<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
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<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>',
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<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'meta_description' => 'Diagenode Offers Extensively Validated ChIP-Grade Antibodies, Confirmed for their Specificity, and high level of Performance in Chromatin Immunoprecipitation ChIP',
'meta_title' => 'Chromatin immunoprecipitation ChIP-grade antibodies | Diagenode',
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'name' => 'Datasheet MeCP2 pAb-052-050',
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'name' => 'Antibodies you can trust',
'description' => '<p style="text-align: justify;"><span>Epigenetic research tools have evolved over time from endpoint PCR to qPCR to the analyses of large sets of genome-wide sequencing data. ChIP sequencing (ChIP-seq) has now become the gold standard method for chromatin studies, given the accuracy and coverage scale of the approach over other methods. Successful ChIP-seq, however, requires a higher level of experimental accuracy and consistency in all steps of ChIP than ever before. Particularly crucial is the quality of ChIP antibodies. </span></p>',
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(int) 2 => array(
'id' => '38',
'name' => 'Epigenetic Antibodies Brochure',
'description' => '<p>More than in any other immuoprecipitation assays, quality antibodies are critical tools in many epigenetics experiments. Since 10 years, Diagenode has developed the most stringent quality production available on the market for antibodies exclusively focused on epigenetic uses. All our antibodies have been qualified to work in epigenetic applications.</p>',
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'type' => 'Brochure',
'url' => 'files/brochures/Epigenetic_Antibodies_Brochure.pdf',
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'name' => 'product/antibodies/ab-chip-icon.png',
'alt' => 'Antibody ChIP icon',
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'created' => '2018-03-15 15:52:35',
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'id' => '4856',
'name' => 'Mu opioid receptor expressing neurons in the rostral ventromedial medullaare the source of mechanical hypersensitivity induced by repeated restraintstress.',
'authors' => 'Imbe Hiroki and Ihara Hayato',
'description' => '<p>Repeated exposure to psychophysical stress often causes an increase in sensitivity and response to pain. This phenomenon is commonly called stress-induced hyperalgesia (SIH). Although psychophysical stress is a well-known risk factor for numerous chronic pain syndromes, the neural mechanism underlying SIH has not yet been elucidated. The rostral ventromedial medulla (RVM) is a key output element of the descending pain modulation system. Descending signals from the RVM have a major impact on spinal nociceptive neurotransmission. In the present study, to clarify changes in the descending pain modulatory system in rats with SIH, we examined the expression of Mu opioid receptor (MOR) mRNA, MeCP2 and global DNA methylation in the RVM after repeated restraint stress for 3 weeks. Additionally, we microinjected neurotoxin dermorphin-SAP into the RVM. The repeated restraint stress for 3 weeks induced mechanical hypersensitivity in the hind paw, a significant increase in the expression of MOR mRNA and MeCP2, and a significant decrease in global DNA methylation in the RVM. The MeCP2 binding to MOR gene promoter in the RVM was significantly decreased in rats with repeated restraint stress. Furthermore, microinjection of dermorphin-SAP into the RVM prevented the mechanical hypersensitivity induced by repeated restraint stress. Although, because of the lack of specific antibody to MOR, we could not show a quantitative analysis in the number of MOR-expressing neurons after the microinjection, these results suggest that MOR-expressing neurons in the RVM induce SIH after repeated restraint stress.</p>',
'date' => '2023-06-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37331575',
'doi' => '10.1016/j.brainres.2023.148465',
'modified' => '2023-08-01 14:43:22',
'created' => '2023-08-01 15:59:38',
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(int) 1 => array(
'id' => '4275',
'name' => 'Epigenetic Silencing of OR and TAS2R Genes Expression inHuman Orbitofrontal Cortex At Early Stages of SporadicAlzheimer’s Disease',
'authors' => 'Alves Victoria Cunha et al.',
'description' => '<p>Modulation of brain olfactory (OR) and taste receptors (TASR) expression was recently reported in neurological diseases. We explored the possible expression and regulation of selected OR and TASR genes in human orbitofrontal cortex of sporadic Alzheimer’s disease (AD) and found that these are expressed and markedly downregulated at early stages. The expression pattern did not follow disease progression suggesting regulation through epigenetic mechanisms. We found an increase of global H3K9me3 levels and substantial enrichment of this repressive signature at ORs and TAS2Rs proximal promoter at early stages, ultimately lost at advanced stages. By mass spectrometry-based proteomic and further validation, we found that H3K9me3 interacts with MeCP2 at early stages and that this protein is increased in sporadic AD. Findings suggest MeCP2 might be implicated in OR and TAS2R genes expression regulation through interaction with H3K9me3, and as an early event, it may uncover a novel etiopathogenetic mechanism of sporadic AD.</p>',
'date' => '2021-12-01',
'pmid' => 'https://doi.org/10.21203%2Frs.3.rs-1098461%2Fv1',
'doi' => '10.21203/rs.3.rs-1098461/v1',
'modified' => '2022-05-23 09:51:36',
'created' => '2022-05-19 10:41:50',
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(int) 2 => array(
'id' => '4242',
'name' => 'Rett syndrome linked to defects in forming the MeCP2/Rbfox/LASRcomplex in mouse models',
'authors' => 'Jiang Yan et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder and a leading cause of intellectual disability in young females. RTT is mainly caused by mutations found in the X-linked gene encoding methyl-CpG binding protein 2 (MeCP2). Despite extensive studies, the molecular mechanism underlying RTT pathogenesis is still poorly understood. Here, we report MeCP2 as a key subunit of a higher-order multiunit protein complex Rbfox/LASR. Defective MeCP2 in RTT mouse models disrupts the assembly of the MeCP2/Rbfox/LASR complex, leading to reduced binding of Rbfox proteins to target pre-mRNAs and aberrant splicing of Nrxns and Nlgn1 critical for synaptic plasticity. We further show that MeCP2 disease mutants display defective condensate properties and fail to promote phase-separated condensates with Rbfox proteins in vitro and in cultured cells. These data link an impaired function of MeCP2 with disease mutation in splicing control to its defective properties in mediating the higher-order assembly of the MeCP2/Rbfox/LASR complex.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34599184',
'doi' => '10.1038/s41467-021-26084-3',
'modified' => '2022-05-20 09:12:57',
'created' => '2022-05-19 10:41:50',
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(int) 3 => array(
'id' => '4324',
'name' => 'Environmental enrichment preserves a young DNA methylation landscape inthe aged mouse hippocampus',
'authors' => 'Zocher S. et al. ',
'description' => '<p>The decline of brain function during aging is associated with epigenetic changes, including DNA methylation. Lifestyle interventions can improve brain function during aging, but their influence on age-related epigenetic changes is unknown. Using genome-wide DNA methylation sequencing, we here show that experiencing a stimulus-rich environment counteracts age-related DNA methylation changes in the hippocampal dentate gyrus of mice. Specifically, environmental enrichment prevented the aging-induced CpG hypomethylation at target sites of the methyl-CpG-binding protein Mecp2, which is critical to neuronal function. The genes at which environmental enrichment counteracted aging effects have described roles in neuronal plasticity, neuronal cell communication and adult hippocampal neurogenesis and are dysregulated with age-related cognitive decline in the human brain. Our results highlight the stimulating effects of environmental enrichment on hippocampal plasticity at the level of DNA methylation and give molecular insights into the specific aspects of brain aging that can be counteracted by lifestyle interventions.</p>',
'date' => '2021-06-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34162876',
'doi' => '10.1038/s41467-021-23993-1',
'modified' => '2022-08-03 15:56:05',
'created' => '2022-05-19 10:41:50',
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(int) 4 => array(
'id' => '4347',
'name' => 'MeCP2 controls neural stem cell fate specification throughmiR-199a-mediated inhibition of BMP-Smad signaling.',
'authors' => 'Nakashima H. et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder, with impaired brain development caused by mutations in MECP2; however, the underlying mechanism remains elusive. We know from previous work that MeCP2 facilitates the processing of a specific microRNA, miR-199a, by associating with the Drosha complex to regulate neuronal functions. Here, we show that the MeCP2/miR-199a axis regulates neural stem/precursor cell (NS/PC) differentiation. A shift occurs from neuronal to astrocytic differentiation of MeCP2- and miR-199a-deficient NS/PCs due to the upregulation of a miR-199a target, Smad1, a downstream transcription factor of bone morphogenetic protein (BMP) signaling. Moreover, miR-199a expression and treatment with BMP inhibitors rectify the differentiation of RTT patient-derived NS/PCs and development of brain organoids, respectively, suggesting that facilitation of BMP signaling accounts for the impaired RTT brain development. Our study illuminates the molecular pathology of RTT and reveals the MeCP2/miR-199a/Smad1 axis as a potential therapeutic target for RTT.</p>',
'date' => '2021-05-01',
'pmid' => 'https://doi.org/10.1016%2Fj.celrep.2021.109124',
'doi' => '10.1016/j.celrep.2021.109124',
'modified' => '2022-08-03 16:35:57',
'created' => '2022-05-19 10:41:50',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 5 => array(
'id' => '4032',
'name' => 'MeCP2 regulates gene expression through recognition of H3K27me3.',
'authors' => 'Lee, W and Kim, J and Yun, JM and Ohn, T and Gong, Q',
'description' => '<p>MeCP2 plays a multifaceted role in gene expression regulation and chromatin organization. Interaction between MeCP2 and methylated DNA in the regulation of gene expression is well established. However, the widespread distribution of MeCP2 suggests it has additional interactions with chromatin. Here we demonstrate, by both biochemical and genomic analyses, that MeCP2 directly interacts with nucleosomes and its genomic distribution correlates with that of H3K27me3. In particular, the methyl-CpG-binding domain of MeCP2 shows preferential interactions with H3K27me3. We further observe that the impact of MeCP2 on transcriptional changes correlates with histone post-translational modification patterns. Our findings indicate that MeCP2 interacts with genomic loci via binding to DNA as well as histones, and that interaction between MeCP2 and histone proteins plays a key role in gene expression regulation.</p>',
'date' => '2020-07-19',
'pmid' => 'http://www.pubmed.gov/32561780',
'doi' => '10.1038/s41467-020-16907-0',
'modified' => '2020-12-16 18:05:17',
'created' => '2020-10-12 14:54:59',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 6 => array(
'id' => '3720',
'name' => 'Genome-wide methylation in alcohol use disorder subjects: implications for an epigenetic regulation of the cortico-limbic glucocorticoid receptors (NR3C1).',
'authors' => 'Gatta E, Grayson DR, Auta J, Saudagar V, Dong E, Chen Y, Krishnan HR, Drnevich J, Pandey SC, Guidotti A',
'description' => '<p>Environmental factors, including substance abuse and stress, cause long-lasting changes in the regulation of gene expression in the brain via epigenetic mechanisms, such as DNA methylation. We examined genome-wide DNA methylation patterns in the prefrontal cortex (PFC, BA10) of 25 pairs of control and individuals with alcohol use disorder (AUD), using the Infinium MethylationEPIC BeadChip. We identified 5254 differentially methylated CpGs (p < 0.005). Bioinformatic analyses highlighted biological processes containing genes related to stress adaptation, including the glucocorticoid receptor (encoded by NR3C1). Considering that alcohol is a stressor, we focused our attention on differentially methylated regions of the NR3C1 gene and validated the differential methylation of several genes in the NR3C1 network. Chronic alcohol drinking results in a significant increased methylation of the NR3C1 exon variant 1, with a particular increase in the levels of 5-hydroxymethylcytosine over 5-methylcytosine. These changes in DNA methylation were associated with reduced NR3C1 mRNA and protein expression levels in PFC, as well as other cortico-limbic regions of AUD subjects when compared with controls. Furthermore, we show that the expression of several stress-responsive genes (e.g., CRF, POMC, and FKBP5) is altered in the PFC of AUD subjects. These stress-response genes were also changed in the hippocampus, a region that is highly susceptible to stress. These data suggest that alcohol-dependent aberrant DNA methylation of NR3C1 and consequent changes in other stress-related genes might be fundamental in the pathophysiology of AUD and lay the groundwork for treatments targeting the epigenetic mechanisms regulating NR3C1 in AUD.</p>',
'date' => '2019-06-25',
'pmid' => 'http://www.pubmed.gov/31239533',
'doi' => '10.1038/s41380-019-0449-6',
'modified' => '2019-07-04 18:07:16',
'created' => '2019-07-04 10:42:34',
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[maximum depth reached]
)
),
(int) 7 => array(
'id' => '3333',
'name' => 'The L1 adhesion molecule normalizes neuritogenesis in Rett syndrome-derived neural precursor cells',
'authors' => 'Yoo M. et al.',
'description' => '<p>Therapeutic intervention is an important need in ameliorating the severe consequences of Rett Syndrome (RTT), a neurological disorder caused by mutations in the X-linked gene methyl-CpG-binding protein-2 (MeCP2). Following previously observed morphological defects in induced pluripotent stem cell (iPSC)-derived neurons obtained from female RTT patients, we hypothesized that transfection with the L1 cell adhesion molecule (L1) could contribute to normalizing a pathological male cell system bearing a nonsense mutation of MeCP2. We found a decreased expression of L1 in RTT iPSCs-derived neural precursor cells (RTT NPCs) and decreased neuritogenesis. Expression of wild-type MeCP2 in RTTNPCs revealed a positive correlation between the levels of MeCP2 and L1, and normalization of cell survival. Expression of L1 in RTTNPCs enhanced neuritogenesis and soma size. Knock-down of MeCP2 in wild type NPCs reduced neuritogenesis. L1 expression is regulated by the MeCP2 promoter. These results suggest that a deficiency in L1 may partially account for RTT phenotypes.</p>',
'date' => '2017-12-16',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/29050935',
'doi' => '',
'modified' => '2018-02-08 17:13:12',
'created' => '2018-02-08 17:13:12',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 8 => array(
'id' => '3142',
'name' => 'Epigenetic regulation of RELN and GAD1 in the frontal cortex (FC) of autism spectrum disorder (ASD) subjects',
'authors' => 'Zhubi A. et al.',
'description' => '<p>Both Reelin (RELN) and glutamate decarboxylase 67 (GAD1) have been implicated in the pathophysiology of Autism Spectrum Disorders (ASD). We have previously shown that both mRNAs are reduced in the cerebella (CB) of ASD subjects through a mechanism that involves increases in the amounts of MECP2 binding to the corresponding promoters. In the current study, we examined the expression of RELN, GAD1, GAD2, and several other mRNAs implicated in this disorder in the frontal cortices (FC) of ASD and CON subjects. We also focused on the role that epigenetic processes play in the regulation of these genes in ASD brain. Our goal is to better understand the molecular basis for the down-regulation of genes expressed in GABAergic neurons in ASD brains. We measured mRNA levels corresponding to selected GABAergic genes using qRT-PCR in RNA isolated from both ASD and CON groups. We determined the extent of binding of MECP2 and DNMT1 repressor proteins by chromatin immunoprecipitation (ChIP) assays. The amount of 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) present in the promoters of the target genes was quantified by methyl DNA immunoprecipitation (MeDIP) and hydroxyl MeDIP (hMeDIP). We detected significant reductions in the mRNAs associated with RELN and GAD1 and significant increases in mRNAs encoding the Ten-eleven Translocation (TET) enzymes 1, 2, and 3. We also detected increased MECP2 and DNMT1 binding to the corresponding promoter regions of GAD1, RELN, and GAD2. Interestingly, there were decreased amounts of 5mC at both promoters and little change in 5hmC content in these same DNA fragments. Our data demonstrate that RELN, GAD1, and several other genes selectively expressed in GABAergic neurons, are down-regulated in post-mortem ASD FC. In addition, we observed increased DNMT1 and MECP2 binding at the corresponding promoters of these genes. The finding of increased MECP2 binding to the RELN, GAD1 and GAD2 promoters, with reduced amounts of 5mC and unchanged amounts of 5hmC present in these regions, suggests the possibility that DNMT1 interacts with and alters MECP2 binding properties to selected promoters. Comparisons between data obtained from the FC with CB studies showed some common themes between brain regions which are discussed.</p>',
'date' => '2017-02-14',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28229923',
'doi' => '',
'modified' => '2017-03-23 14:58:21',
'created' => '2017-03-23 14:58:21',
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(int) 9 => array(
'id' => '2907',
'name' => 'The heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a novel tumor regulator and a prognostic marker in breast cancer',
'authors' => 'Mao X, Gauche C, Coughtrie MW, Bui C, Gulberti S, Merhi-Soussi F, Ramalanjaona N, Bertin-Jung I, Diot A, Dumas D, De Freitas Caires N, Thompson AM, Bourdon JC, Ouzzine M, Fournel-Gigleux S',
'description' => '<p>Heparan sulfate (HS) proteoglycan chains are key components of the breast tumor microenvironment that critically influence the behavior of cancer cells. It is established that abnormal synthesis and processing of HS play a prominent role in tumorigenesis, albeit mechanisms remain mostly obscure. HS function is mainly controlled by sulfotransferases, and here we report a novel cellular and pathophysiological significance for the 3-O-sulfotransferase 3-OST3A (HS3ST3A), catalyzing the final maturation step of HS, in breast cancer. We show that 3-OST3A is epigenetically repressed in all breast cancer cell lines of a panel representative of distinct molecular subgroups, except in human epidermal growth factor receptor 2-positive (HER2+) sloan-kettering breast cancer (SKBR3) cells. Epigenetic mechanisms involved both DNA methylation and histone modifications, producing different repressive chromatin environments depending on the cell molecular signature. Gain and loss of function experiments by cDNA and siRNA transfection revealed profound effects of 3-OST3A expression on cell behavior including apoptosis, proliferation, response to trastuzumab in vitro and tumor growth in xenografted mice. 3-OST3A exerted dual activities acting as tumor-suppressor in lumA-michigan cancer foundation (MCF)-7 and triple negative-MD Anderson (MDA) metastatic breast (MB)-231 cells, or as an oncogenic factor in HER2+-SKBR3 cells. Mechanistically, fluorescence-resonance energy transfer-fluorescence-lifetime imaging microscopy experiments indicated that the effects of 3-OST3A in MCF-7 cells were mediated by altered interactions between HS and fibroblast growth factor-7 (FGF-7). Further, this interplay between HS and FGF-7 modulated downstream ERK, AKT and p38 cascades, suggesting that altering 3-O-sulfation affects FGFR2IIIb-mediated signaling. Corroborating our cellular data, a clinical study conducted in a cohort of breast cancer patients uncovered that, in HER2+ patients, high level expression of 3-OST3A in tumors was associated with reduced relapse-free survival. Our findings define 3-OST3A as a novel regulator of breast cancer pathogenicity, displaying tumor-suppressive or oncogenic activities in a cell- and tumor-dependent context, and demonstrate the clinical value of the HS-O-sulfotransferase 3-OST3A as a prognostic marker in HER2+ patients.</p>',
'date' => '2016-04-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/27041583',
'doi' => ' 10.1038/onc.2016.44',
'modified' => '2016-05-09 09:58:38',
'created' => '2016-05-09 09:58:38',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 10 => array(
'id' => '2882',
'name' => 'Sequence features accurately predict genome-wide MeCP2 binding in vivo',
'authors' => 'Rube HT, Lee W, Hejna M, Chen H, Yasui DH, Hess JF, LaSalle JM, Song JS, Gong Q',
'description' => '<p>Methyl-CpG binding protein 2 (MeCP2) is critical for proper brain development and expressed at near-histone levels in neurons, but the mechanism of its genomic localization remains poorly understood. Using high-resolution MeCP2-binding data, we show that DNA sequence features alone can predict binding with 88<span class="mb">%</span> accuracy. Integrating MeCP2 binding and DNA methylation in a probabilistic graphical model, we demonstrate that previously reported genome-wide association with methylation is in part due to MeCP2’s affinity to GC-rich chromatin, a result replicated using published data. Furthermore, MeCP2 co-localizes with nucleosomes. Finally, MeCP2 binding downstream of promoters correlates with increased expression in <i>Mecp2</i>-deficient neurons.</p>',
'date' => '2016-03-24',
'pmid' => 'http://www.nature.com/ncomms/2016/160324/ncomms11025/abs/ncomms11025.html',
'doi' => '10.1038/ncomms11025',
'modified' => '2016-04-06 10:42:59',
'created' => '2016-04-06 10:42:59',
'ProductsPublication' => array(
[maximum depth reached]
)
),
(int) 11 => array(
'id' => '2858',
'name' => 'Adrenergic Repression of the Epigenetic Reader MeCP2 Facilitates Cardiac Adaptation in Chronic Heart Failure',
'authors' => 'Mayer SC. et al.',
'description' => '<h4>RATIONALE:</h4>
<p><abstracttext label="RATIONALE" nlmcategory="BACKGROUND">In chronic heart failure, increased adrenergic activation contributes to structural remodeling and altered gene expression. Although adrenergic signaling alters histone modifications, it is unknown, whether it also affects other epigenetic processes, including DNA methylation and its recognition.</abstracttext></p>
<h4>OBJECTIVE:</h4>
<p><abstracttext label="OBJECTIVE" nlmcategory="OBJECTIVE">The aim of this study was to identify the mechanism of regulation of the methyl-CpG-binding protein 2 (MeCP2) and its functional significance during cardiac pressure overload and unloading.</abstracttext></p>
<h4>METHODS AND RESULTS:</h4>
<p><abstracttext label="METHODS AND RESULTS" nlmcategory="RESULTS">MeCP2 was identified as a reversibly repressed gene in mouse hearts after transverse aortic constriction and was normalized after removal of the constriction. Similarly, MeCP2 repression in human failing hearts resolved after unloading by a left ventricular assist device. The cluster miR-212/132 was upregulated after transverse aortic constriction or on activation of α1- and β1-adrenoceptors and miR-212/132 led to repression of MeCP2. Prevention of MeCP2 repression by a cardiomyocyte-specific, doxycycline-regulatable transgenic mouse model aggravated cardiac hypertrophy, fibrosis, and contractile dysfunction after transverse aortic constriction. Ablation of MeCP2 in cardiomyocytes facilitated recovery of failing hearts after reversible transverse aortic constriction. Genome-wide expression analysis, chromatin immunoprecipitation experiments, and DNA methylation analysis identified mitochondrial genes and their transcriptional regulators as MeCP2 target genes. Coincident with its repression, MeCP2 was removed from its target genes, whereas DNA methylation of MeCP2 target genes remained stable during pressure overload.</abstracttext></p>
<h4>CONCLUSIONS:</h4>
<p><abstracttext label="CONCLUSIONS" nlmcategory="CONCLUSIONS">These data connect adrenergic activation with a microRNA-MeCP2 epigenetic pathway that is important for cardiac adaptation during the development and recovery from heart failure.</abstracttext></p>',
'date' => '2015-09-11',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/26195221',
'doi' => '10.1161/CIRCRESAHA.115.306721',
'modified' => '2016-03-15 14:12:52',
'created' => '2016-03-15 14:12:52',
'ProductsPublication' => array(
[maximum depth reached]
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),
(int) 12 => array(
'id' => '1742',
'name' => 'Dynamic CCAAT/Enhancer Binding Protein-Associated Changes of DNA Methylation in the Angiotensinogen Gene.',
'authors' => 'Wang F, Demura M, Cheng Y, Zhu A, Karashima S, Yoneda T, Demura Y, Maeda Y, Namiki M, Ono K, Nakamura Y, Sasano H, Akagi T, Yamagishi M, Saijoh K, Takeda Y.',
'description' => 'DNA methylation patterns are maintained in adult somatic cells. Recent findings, however, suggest that all methylation patterns are not preserved. We demonstrate that stimulatory signals can change the DNA methylation status at a CCAAT/enhancer binding protein (CEBP) binding site and a transcription start site and activate expression of the angiotensinogen gene (AGT). A CEBP binding site in the human AGT promoter was hypomethylated in tissues with high expression of AGT, but not in those with low expression. The transcriptional activity of AGT promoter sequences cloned into a reporter plasmid depended on DNA methylation. In cultured human cells, interleukin 6 stimulation caused DNA demethylation around a CEBP binding site and a transcription start site; demethylation was accompanied by increased CEBP-β recruitment and chromatin accessibility of the AGT promoter. DNA methylation activity decreased in the nucleus. Excess circulating aldosterone upregulated AGT expression and was accompanied by DNA hypomethylation around a CEBP binding site and a transcription start site in human visceral adipose tissue. High salt intake led to upregulation of Agt expression, DNA hypomethylation around 2 CEBP binding sites and a transcription start site, and decreased DNA methylation activity in rat visceral adipose tissue. Taken together, CEBP binding initiates chromatin relaxation and transcription, which are followed by DNA demethylation around a CEBP binding site and a transcription start site in the AGT promoter. Decreased DNA methylation activity in the nucleus may play a role in DNA demethylation. DNA demethylation switches the phenotype of AGT expression from an inactive to an active state.',
'date' => '2013-11-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/24191285',
'doi' => '',
'modified' => '2015-07-24 15:39:01',
'created' => '2015-07-24 15:39:01',
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[maximum depth reached]
)
),
(int) 13 => array(
'id' => '81',
'name' => 'Survival motor neuron gene 2 silencing by DNA methylation correlates with spinal muscular atrophy disease severity and can be bypassed by histone deacetylase inhibition.',
'authors' => 'Hauke J, Riessland M, Lunke S, Eyüpoglu IY, Blümcke I, El-Osta A, Wirth B, Hahnen E',
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<p><small><strong> Figure 1 ChIP results obtained with the Diagenode antibody directed against MeCP2</strong><br /> ChIP assays were performed using human osteosarcoma (U2OS) cells, the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) and optimized PCR primer sets. Sheared chromatin from 1x10e6 cells and 5 μg of antibody were used per ChIP experiment. IgG (1 μg/IP) was used as a negative IP control. Quantitative PCR was performed with primers for the promoters of the ZMYND10 gene (used as a positive control) and CDC6 gene (used as a negative control). Figure 1 shows the recovery, expressed as a % of input (the relative amount of immunoprecipitated DNA compared to input DNA after qPCR analysis). </small></p>
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<p><small><strong> Figure 2 Determination of the antibody titer</strong><br /> To determine the titer of the antibody, an ELISA was performed using a serial dilution of the Diagenode antibody directed against MeCP2 (Cat. No. pAb-052-050) and the crude serum. The plates were coated with the peptide used for immunization of the rabbit. By plotting the absorbance against the antibody dilution (Figure 2), the titer of the purified antibody was estimated to be: 1:32,900. </small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<p><small><strong> Figure 3 Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Nuclear extracts (40 μg) from HeLa cells were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. pAb-052-050) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left. </small></p>
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<p><small><strong> Figure 4. Western blot analysis using the Diagenode antibody directed against MeCP2</strong><br /> Whole cell extracts (40 μg) from HeLa cells transfected with MeCP2 siRNA (lane 2) and from an untransfected control (lane 1) were analysed by Western blot using the Diagenode antibody against MeCP2 (Cat. No. C15410052) diluted 1:1,000 in TBS-Tween containing 5% skimmed milk. The position of the protein of interest is indicated on the right; the marker (in kDa) is shown on the left.</small></p>
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<div class="small-10 columns">
<h3>Epigenetic antibodies you can trust!</h3>
<p>Antibody quality is essential for assay success. Diagenode offers antibodies that are actually validated and have been widely used and published by the scientific community. Now we are adding a new level of siRNA knockdown validation to assure the specificity of our non-histone antibodies.</p>
<p><strong>Short interfering RNA (siRNA)</strong> degrades target mRNA, followed by the knock-down of protein production. If the antibody that recognizes the protein of interest is specific, the Western blot of siRNA-treated cells will show a significant reduction of signal vs. untreated cells.</p>
<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
</div>
<div class="small-2 columns">
<p><img src="https://www.diagenode.com/emailing/images/epi-success-guaranteed-icon.png" alt="Epigenetic success guaranteed" /></p>
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<div class="spaced"></div>
<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>',
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<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
<ul>
<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
<li>Expert technical support</li>
<li>Sample sizes available</li>
<li>100% satisfaction guarantee</li>
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'description' => '<p><span style="font-weight: 400;">All Diagenode’s antibodies are listed below. Please, use our Quick search field to find the antibody of interest by target name, application, purity.</span></p>
<p><span style="font-weight: 400;">Diagenode’s highly validated antibodies:</span></p>
<ul>
<li>Highly sensitive and specific</li>
<li>Cost-effective (requires less antibody per reaction)</li>
<li>Batch-specific data is available on the website</li>
<li>Expert technical support</li>
<li>Sample sizes available</li>
<li>100% satisfaction guarantee</li>
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<div class="small-12 columns"><center></center>
<p><br />Chromatin immunoprecipitation (<b>ChIP</b>) is a technique to study the associations of proteins with the specific genomic regions in intact cells. One of the most important steps of this protocol is the immunoprecipitation of targeted protein using the antibody specifically recognizing it. The quality of antibodies used in ChIP is essential for the success of the experiment. Diagenode offers extensively validated ChIP-grade antibodies, confirmed for their specificity, and high level of performance in ChIP. Each batch is validated, and batch-specific data are available on the website.</p>
<p></p>
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<p><strong>ChIP results</strong> obtained with the antibody directed against H3K4me3 (Cat. No. <a href="../p/h3k4me3-polyclonal-antibody-premium-50-ug-50-ul">C15410003</a>). </p>
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<div class="small-12 medium-6 large-6 columns"><img src="https://www.diagenode.com/img/product/antibodies/C15410003-fig1-ChIP.jpg" alt="" width="400" height="315" /> </div>
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<p></p>
<p></p>
<p></p>
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<p></p>
<p>Our aim at Diagenode is to offer the largest collection of highly specific <strong>ChIP-grade antibodies</strong>. We add new antibodies monthly. Find your ChIP-grade antibody in the list below and check more information about tested applications, extensive validation data, and product information.</p>',
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'description' => '<p style="text-align: justify;"><span>Epigenetic research tools have evolved over time from endpoint PCR to qPCR to the analyses of large sets of genome-wide sequencing data. ChIP sequencing (ChIP-seq) has now become the gold standard method for chromatin studies, given the accuracy and coverage scale of the approach over other methods. Successful ChIP-seq, however, requires a higher level of experimental accuracy and consistency in all steps of ChIP than ever before. Particularly crucial is the quality of ChIP antibodies. </span></p>',
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'name' => 'Mu opioid receptor expressing neurons in the rostral ventromedial medullaare the source of mechanical hypersensitivity induced by repeated restraintstress.',
'authors' => 'Imbe Hiroki and Ihara Hayato',
'description' => '<p>Repeated exposure to psychophysical stress often causes an increase in sensitivity and response to pain. This phenomenon is commonly called stress-induced hyperalgesia (SIH). Although psychophysical stress is a well-known risk factor for numerous chronic pain syndromes, the neural mechanism underlying SIH has not yet been elucidated. The rostral ventromedial medulla (RVM) is a key output element of the descending pain modulation system. Descending signals from the RVM have a major impact on spinal nociceptive neurotransmission. In the present study, to clarify changes in the descending pain modulatory system in rats with SIH, we examined the expression of Mu opioid receptor (MOR) mRNA, MeCP2 and global DNA methylation in the RVM after repeated restraint stress for 3 weeks. Additionally, we microinjected neurotoxin dermorphin-SAP into the RVM. The repeated restraint stress for 3 weeks induced mechanical hypersensitivity in the hind paw, a significant increase in the expression of MOR mRNA and MeCP2, and a significant decrease in global DNA methylation in the RVM. The MeCP2 binding to MOR gene promoter in the RVM was significantly decreased in rats with repeated restraint stress. Furthermore, microinjection of dermorphin-SAP into the RVM prevented the mechanical hypersensitivity induced by repeated restraint stress. Although, because of the lack of specific antibody to MOR, we could not show a quantitative analysis in the number of MOR-expressing neurons after the microinjection, these results suggest that MOR-expressing neurons in the RVM induce SIH after repeated restraint stress.</p>',
'date' => '2023-06-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/37331575',
'doi' => '10.1016/j.brainres.2023.148465',
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'id' => '4275',
'name' => 'Epigenetic Silencing of OR and TAS2R Genes Expression inHuman Orbitofrontal Cortex At Early Stages of SporadicAlzheimer’s Disease',
'authors' => 'Alves Victoria Cunha et al.',
'description' => '<p>Modulation of brain olfactory (OR) and taste receptors (TASR) expression was recently reported in neurological diseases. We explored the possible expression and regulation of selected OR and TASR genes in human orbitofrontal cortex of sporadic Alzheimer’s disease (AD) and found that these are expressed and markedly downregulated at early stages. The expression pattern did not follow disease progression suggesting regulation through epigenetic mechanisms. We found an increase of global H3K9me3 levels and substantial enrichment of this repressive signature at ORs and TAS2Rs proximal promoter at early stages, ultimately lost at advanced stages. By mass spectrometry-based proteomic and further validation, we found that H3K9me3 interacts with MeCP2 at early stages and that this protein is increased in sporadic AD. Findings suggest MeCP2 might be implicated in OR and TAS2R genes expression regulation through interaction with H3K9me3, and as an early event, it may uncover a novel etiopathogenetic mechanism of sporadic AD.</p>',
'date' => '2021-12-01',
'pmid' => 'https://doi.org/10.21203%2Frs.3.rs-1098461%2Fv1',
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'id' => '4242',
'name' => 'Rett syndrome linked to defects in forming the MeCP2/Rbfox/LASRcomplex in mouse models',
'authors' => 'Jiang Yan et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder and a leading cause of intellectual disability in young females. RTT is mainly caused by mutations found in the X-linked gene encoding methyl-CpG binding protein 2 (MeCP2). Despite extensive studies, the molecular mechanism underlying RTT pathogenesis is still poorly understood. Here, we report MeCP2 as a key subunit of a higher-order multiunit protein complex Rbfox/LASR. Defective MeCP2 in RTT mouse models disrupts the assembly of the MeCP2/Rbfox/LASR complex, leading to reduced binding of Rbfox proteins to target pre-mRNAs and aberrant splicing of Nrxns and Nlgn1 critical for synaptic plasticity. We further show that MeCP2 disease mutants display defective condensate properties and fail to promote phase-separated condensates with Rbfox proteins in vitro and in cultured cells. These data link an impaired function of MeCP2 with disease mutation in splicing control to its defective properties in mediating the higher-order assembly of the MeCP2/Rbfox/LASR complex.</p>',
'date' => '2021-10-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34599184',
'doi' => '10.1038/s41467-021-26084-3',
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'id' => '4324',
'name' => 'Environmental enrichment preserves a young DNA methylation landscape inthe aged mouse hippocampus',
'authors' => 'Zocher S. et al. ',
'description' => '<p>The decline of brain function during aging is associated with epigenetic changes, including DNA methylation. Lifestyle interventions can improve brain function during aging, but their influence on age-related epigenetic changes is unknown. Using genome-wide DNA methylation sequencing, we here show that experiencing a stimulus-rich environment counteracts age-related DNA methylation changes in the hippocampal dentate gyrus of mice. Specifically, environmental enrichment prevented the aging-induced CpG hypomethylation at target sites of the methyl-CpG-binding protein Mecp2, which is critical to neuronal function. The genes at which environmental enrichment counteracted aging effects have described roles in neuronal plasticity, neuronal cell communication and adult hippocampal neurogenesis and are dysregulated with age-related cognitive decline in the human brain. Our results highlight the stimulating effects of environmental enrichment on hippocampal plasticity at the level of DNA methylation and give molecular insights into the specific aspects of brain aging that can be counteracted by lifestyle interventions.</p>',
'date' => '2021-06-01',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/34162876',
'doi' => '10.1038/s41467-021-23993-1',
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'id' => '4347',
'name' => 'MeCP2 controls neural stem cell fate specification throughmiR-199a-mediated inhibition of BMP-Smad signaling.',
'authors' => 'Nakashima H. et al.',
'description' => '<p>Rett syndrome (RTT) is a severe neurological disorder, with impaired brain development caused by mutations in MECP2; however, the underlying mechanism remains elusive. We know from previous work that MeCP2 facilitates the processing of a specific microRNA, miR-199a, by associating with the Drosha complex to regulate neuronal functions. Here, we show that the MeCP2/miR-199a axis regulates neural stem/precursor cell (NS/PC) differentiation. A shift occurs from neuronal to astrocytic differentiation of MeCP2- and miR-199a-deficient NS/PCs due to the upregulation of a miR-199a target, Smad1, a downstream transcription factor of bone morphogenetic protein (BMP) signaling. Moreover, miR-199a expression and treatment with BMP inhibitors rectify the differentiation of RTT patient-derived NS/PCs and development of brain organoids, respectively, suggesting that facilitation of BMP signaling accounts for the impaired RTT brain development. Our study illuminates the molecular pathology of RTT and reveals the MeCP2/miR-199a/Smad1 axis as a potential therapeutic target for RTT.</p>',
'date' => '2021-05-01',
'pmid' => 'https://doi.org/10.1016%2Fj.celrep.2021.109124',
'doi' => '10.1016/j.celrep.2021.109124',
'modified' => '2022-08-03 16:35:57',
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(int) 5 => array(
'id' => '4032',
'name' => 'MeCP2 regulates gene expression through recognition of H3K27me3.',
'authors' => 'Lee, W and Kim, J and Yun, JM and Ohn, T and Gong, Q',
'description' => '<p>MeCP2 plays a multifaceted role in gene expression regulation and chromatin organization. Interaction between MeCP2 and methylated DNA in the regulation of gene expression is well established. However, the widespread distribution of MeCP2 suggests it has additional interactions with chromatin. Here we demonstrate, by both biochemical and genomic analyses, that MeCP2 directly interacts with nucleosomes and its genomic distribution correlates with that of H3K27me3. In particular, the methyl-CpG-binding domain of MeCP2 shows preferential interactions with H3K27me3. We further observe that the impact of MeCP2 on transcriptional changes correlates with histone post-translational modification patterns. Our findings indicate that MeCP2 interacts with genomic loci via binding to DNA as well as histones, and that interaction between MeCP2 and histone proteins plays a key role in gene expression regulation.</p>',
'date' => '2020-07-19',
'pmid' => 'http://www.pubmed.gov/32561780',
'doi' => '10.1038/s41467-020-16907-0',
'modified' => '2020-12-16 18:05:17',
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'id' => '3720',
'name' => 'Genome-wide methylation in alcohol use disorder subjects: implications for an epigenetic regulation of the cortico-limbic glucocorticoid receptors (NR3C1).',
'authors' => 'Gatta E, Grayson DR, Auta J, Saudagar V, Dong E, Chen Y, Krishnan HR, Drnevich J, Pandey SC, Guidotti A',
'description' => '<p>Environmental factors, including substance abuse and stress, cause long-lasting changes in the regulation of gene expression in the brain via epigenetic mechanisms, such as DNA methylation. We examined genome-wide DNA methylation patterns in the prefrontal cortex (PFC, BA10) of 25 pairs of control and individuals with alcohol use disorder (AUD), using the Infinium MethylationEPIC BeadChip. We identified 5254 differentially methylated CpGs (p < 0.005). Bioinformatic analyses highlighted biological processes containing genes related to stress adaptation, including the glucocorticoid receptor (encoded by NR3C1). Considering that alcohol is a stressor, we focused our attention on differentially methylated regions of the NR3C1 gene and validated the differential methylation of several genes in the NR3C1 network. Chronic alcohol drinking results in a significant increased methylation of the NR3C1 exon variant 1, with a particular increase in the levels of 5-hydroxymethylcytosine over 5-methylcytosine. These changes in DNA methylation were associated with reduced NR3C1 mRNA and protein expression levels in PFC, as well as other cortico-limbic regions of AUD subjects when compared with controls. Furthermore, we show that the expression of several stress-responsive genes (e.g., CRF, POMC, and FKBP5) is altered in the PFC of AUD subjects. These stress-response genes were also changed in the hippocampus, a region that is highly susceptible to stress. These data suggest that alcohol-dependent aberrant DNA methylation of NR3C1 and consequent changes in other stress-related genes might be fundamental in the pathophysiology of AUD and lay the groundwork for treatments targeting the epigenetic mechanisms regulating NR3C1 in AUD.</p>',
'date' => '2019-06-25',
'pmid' => 'http://www.pubmed.gov/31239533',
'doi' => '10.1038/s41380-019-0449-6',
'modified' => '2019-07-04 18:07:16',
'created' => '2019-07-04 10:42:34',
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'id' => '3333',
'name' => 'The L1 adhesion molecule normalizes neuritogenesis in Rett syndrome-derived neural precursor cells',
'authors' => 'Yoo M. et al.',
'description' => '<p>Therapeutic intervention is an important need in ameliorating the severe consequences of Rett Syndrome (RTT), a neurological disorder caused by mutations in the X-linked gene methyl-CpG-binding protein-2 (MeCP2). Following previously observed morphological defects in induced pluripotent stem cell (iPSC)-derived neurons obtained from female RTT patients, we hypothesized that transfection with the L1 cell adhesion molecule (L1) could contribute to normalizing a pathological male cell system bearing a nonsense mutation of MeCP2. We found a decreased expression of L1 in RTT iPSCs-derived neural precursor cells (RTT NPCs) and decreased neuritogenesis. Expression of wild-type MeCP2 in RTTNPCs revealed a positive correlation between the levels of MeCP2 and L1, and normalization of cell survival. Expression of L1 in RTTNPCs enhanced neuritogenesis and soma size. Knock-down of MeCP2 in wild type NPCs reduced neuritogenesis. L1 expression is regulated by the MeCP2 promoter. These results suggest that a deficiency in L1 may partially account for RTT phenotypes.</p>',
'date' => '2017-12-16',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/29050935',
'doi' => '',
'modified' => '2018-02-08 17:13:12',
'created' => '2018-02-08 17:13:12',
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[maximum depth reached]
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'id' => '3142',
'name' => 'Epigenetic regulation of RELN and GAD1 in the frontal cortex (FC) of autism spectrum disorder (ASD) subjects',
'authors' => 'Zhubi A. et al.',
'description' => '<p>Both Reelin (RELN) and glutamate decarboxylase 67 (GAD1) have been implicated in the pathophysiology of Autism Spectrum Disorders (ASD). We have previously shown that both mRNAs are reduced in the cerebella (CB) of ASD subjects through a mechanism that involves increases in the amounts of MECP2 binding to the corresponding promoters. In the current study, we examined the expression of RELN, GAD1, GAD2, and several other mRNAs implicated in this disorder in the frontal cortices (FC) of ASD and CON subjects. We also focused on the role that epigenetic processes play in the regulation of these genes in ASD brain. Our goal is to better understand the molecular basis for the down-regulation of genes expressed in GABAergic neurons in ASD brains. We measured mRNA levels corresponding to selected GABAergic genes using qRT-PCR in RNA isolated from both ASD and CON groups. We determined the extent of binding of MECP2 and DNMT1 repressor proteins by chromatin immunoprecipitation (ChIP) assays. The amount of 5-methylcytosine (5mC) and 5-hydroxymethylcytosine (5hmC) present in the promoters of the target genes was quantified by methyl DNA immunoprecipitation (MeDIP) and hydroxyl MeDIP (hMeDIP). We detected significant reductions in the mRNAs associated with RELN and GAD1 and significant increases in mRNAs encoding the Ten-eleven Translocation (TET) enzymes 1, 2, and 3. We also detected increased MECP2 and DNMT1 binding to the corresponding promoter regions of GAD1, RELN, and GAD2. Interestingly, there were decreased amounts of 5mC at both promoters and little change in 5hmC content in these same DNA fragments. Our data demonstrate that RELN, GAD1, and several other genes selectively expressed in GABAergic neurons, are down-regulated in post-mortem ASD FC. In addition, we observed increased DNMT1 and MECP2 binding at the corresponding promoters of these genes. The finding of increased MECP2 binding to the RELN, GAD1 and GAD2 promoters, with reduced amounts of 5mC and unchanged amounts of 5hmC present in these regions, suggests the possibility that DNMT1 interacts with and alters MECP2 binding properties to selected promoters. Comparisons between data obtained from the FC with CB studies showed some common themes between brain regions which are discussed.</p>',
'date' => '2017-02-14',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/28229923',
'doi' => '',
'modified' => '2017-03-23 14:58:21',
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'id' => '2907',
'name' => 'The heparan sulfate sulfotransferase 3-OST3A (HS3ST3A) is a novel tumor regulator and a prognostic marker in breast cancer',
'authors' => 'Mao X, Gauche C, Coughtrie MW, Bui C, Gulberti S, Merhi-Soussi F, Ramalanjaona N, Bertin-Jung I, Diot A, Dumas D, De Freitas Caires N, Thompson AM, Bourdon JC, Ouzzine M, Fournel-Gigleux S',
'description' => '<p>Heparan sulfate (HS) proteoglycan chains are key components of the breast tumor microenvironment that critically influence the behavior of cancer cells. It is established that abnormal synthesis and processing of HS play a prominent role in tumorigenesis, albeit mechanisms remain mostly obscure. HS function is mainly controlled by sulfotransferases, and here we report a novel cellular and pathophysiological significance for the 3-O-sulfotransferase 3-OST3A (HS3ST3A), catalyzing the final maturation step of HS, in breast cancer. We show that 3-OST3A is epigenetically repressed in all breast cancer cell lines of a panel representative of distinct molecular subgroups, except in human epidermal growth factor receptor 2-positive (HER2+) sloan-kettering breast cancer (SKBR3) cells. Epigenetic mechanisms involved both DNA methylation and histone modifications, producing different repressive chromatin environments depending on the cell molecular signature. Gain and loss of function experiments by cDNA and siRNA transfection revealed profound effects of 3-OST3A expression on cell behavior including apoptosis, proliferation, response to trastuzumab in vitro and tumor growth in xenografted mice. 3-OST3A exerted dual activities acting as tumor-suppressor in lumA-michigan cancer foundation (MCF)-7 and triple negative-MD Anderson (MDA) metastatic breast (MB)-231 cells, or as an oncogenic factor in HER2+-SKBR3 cells. Mechanistically, fluorescence-resonance energy transfer-fluorescence-lifetime imaging microscopy experiments indicated that the effects of 3-OST3A in MCF-7 cells were mediated by altered interactions between HS and fibroblast growth factor-7 (FGF-7). Further, this interplay between HS and FGF-7 modulated downstream ERK, AKT and p38 cascades, suggesting that altering 3-O-sulfation affects FGFR2IIIb-mediated signaling. Corroborating our cellular data, a clinical study conducted in a cohort of breast cancer patients uncovered that, in HER2+ patients, high level expression of 3-OST3A in tumors was associated with reduced relapse-free survival. Our findings define 3-OST3A as a novel regulator of breast cancer pathogenicity, displaying tumor-suppressive or oncogenic activities in a cell- and tumor-dependent context, and demonstrate the clinical value of the HS-O-sulfotransferase 3-OST3A as a prognostic marker in HER2+ patients.</p>',
'date' => '2016-04-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/27041583',
'doi' => ' 10.1038/onc.2016.44',
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'name' => 'Sequence features accurately predict genome-wide MeCP2 binding in vivo',
'authors' => 'Rube HT, Lee W, Hejna M, Chen H, Yasui DH, Hess JF, LaSalle JM, Song JS, Gong Q',
'description' => '<p>Methyl-CpG binding protein 2 (MeCP2) is critical for proper brain development and expressed at near-histone levels in neurons, but the mechanism of its genomic localization remains poorly understood. Using high-resolution MeCP2-binding data, we show that DNA sequence features alone can predict binding with 88<span class="mb">%</span> accuracy. Integrating MeCP2 binding and DNA methylation in a probabilistic graphical model, we demonstrate that previously reported genome-wide association with methylation is in part due to MeCP2’s affinity to GC-rich chromatin, a result replicated using published data. Furthermore, MeCP2 co-localizes with nucleosomes. Finally, MeCP2 binding downstream of promoters correlates with increased expression in <i>Mecp2</i>-deficient neurons.</p>',
'date' => '2016-03-24',
'pmid' => 'http://www.nature.com/ncomms/2016/160324/ncomms11025/abs/ncomms11025.html',
'doi' => '10.1038/ncomms11025',
'modified' => '2016-04-06 10:42:59',
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'id' => '2858',
'name' => 'Adrenergic Repression of the Epigenetic Reader MeCP2 Facilitates Cardiac Adaptation in Chronic Heart Failure',
'authors' => 'Mayer SC. et al.',
'description' => '<h4>RATIONALE:</h4>
<p><abstracttext label="RATIONALE" nlmcategory="BACKGROUND">In chronic heart failure, increased adrenergic activation contributes to structural remodeling and altered gene expression. Although adrenergic signaling alters histone modifications, it is unknown, whether it also affects other epigenetic processes, including DNA methylation and its recognition.</abstracttext></p>
<h4>OBJECTIVE:</h4>
<p><abstracttext label="OBJECTIVE" nlmcategory="OBJECTIVE">The aim of this study was to identify the mechanism of regulation of the methyl-CpG-binding protein 2 (MeCP2) and its functional significance during cardiac pressure overload and unloading.</abstracttext></p>
<h4>METHODS AND RESULTS:</h4>
<p><abstracttext label="METHODS AND RESULTS" nlmcategory="RESULTS">MeCP2 was identified as a reversibly repressed gene in mouse hearts after transverse aortic constriction and was normalized after removal of the constriction. Similarly, MeCP2 repression in human failing hearts resolved after unloading by a left ventricular assist device. The cluster miR-212/132 was upregulated after transverse aortic constriction or on activation of α1- and β1-adrenoceptors and miR-212/132 led to repression of MeCP2. Prevention of MeCP2 repression by a cardiomyocyte-specific, doxycycline-regulatable transgenic mouse model aggravated cardiac hypertrophy, fibrosis, and contractile dysfunction after transverse aortic constriction. Ablation of MeCP2 in cardiomyocytes facilitated recovery of failing hearts after reversible transverse aortic constriction. Genome-wide expression analysis, chromatin immunoprecipitation experiments, and DNA methylation analysis identified mitochondrial genes and their transcriptional regulators as MeCP2 target genes. Coincident with its repression, MeCP2 was removed from its target genes, whereas DNA methylation of MeCP2 target genes remained stable during pressure overload.</abstracttext></p>
<h4>CONCLUSIONS:</h4>
<p><abstracttext label="CONCLUSIONS" nlmcategory="CONCLUSIONS">These data connect adrenergic activation with a microRNA-MeCP2 epigenetic pathway that is important for cardiac adaptation during the development and recovery from heart failure.</abstracttext></p>',
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'name' => 'Dynamic CCAAT/Enhancer Binding Protein-Associated Changes of DNA Methylation in the Angiotensinogen Gene.',
'authors' => 'Wang F, Demura M, Cheng Y, Zhu A, Karashima S, Yoneda T, Demura Y, Maeda Y, Namiki M, Ono K, Nakamura Y, Sasano H, Akagi T, Yamagishi M, Saijoh K, Takeda Y.',
'description' => 'DNA methylation patterns are maintained in adult somatic cells. Recent findings, however, suggest that all methylation patterns are not preserved. We demonstrate that stimulatory signals can change the DNA methylation status at a CCAAT/enhancer binding protein (CEBP) binding site and a transcription start site and activate expression of the angiotensinogen gene (AGT). A CEBP binding site in the human AGT promoter was hypomethylated in tissues with high expression of AGT, but not in those with low expression. The transcriptional activity of AGT promoter sequences cloned into a reporter plasmid depended on DNA methylation. In cultured human cells, interleukin 6 stimulation caused DNA demethylation around a CEBP binding site and a transcription start site; demethylation was accompanied by increased CEBP-β recruitment and chromatin accessibility of the AGT promoter. DNA methylation activity decreased in the nucleus. Excess circulating aldosterone upregulated AGT expression and was accompanied by DNA hypomethylation around a CEBP binding site and a transcription start site in human visceral adipose tissue. High salt intake led to upregulation of Agt expression, DNA hypomethylation around 2 CEBP binding sites and a transcription start site, and decreased DNA methylation activity in rat visceral adipose tissue. Taken together, CEBP binding initiates chromatin relaxation and transcription, which are followed by DNA demethylation around a CEBP binding site and a transcription start site in the AGT promoter. Decreased DNA methylation activity in the nucleus may play a role in DNA demethylation. DNA demethylation switches the phenotype of AGT expression from an inactive to an active state.',
'date' => '2013-11-04',
'pmid' => 'http://www.ncbi.nlm.nih.gov/pubmed/24191285',
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'authors' => 'Hauke J, Riessland M, Lunke S, Eyüpoglu IY, Blümcke I, El-Osta A, Wirth B, Hahnen E',
'description' => 'Spinal muscular atrophy (SMA), a common neuromuscular disorder, is caused by homozygous absence of the survival motor neuron gene 1 (SMN1), while the disease severity is mainly influenced by the number of SMN2 gene copies. This correlation is not absolute, suggesting the existence of yet unknown factors modulating disease progression. We demonstrate that the SMN2 gene is subject to gene silencing by DNA methylation. SMN2 contains four CpG islands which present highly conserved methylation patterns and little interindividual variations in SMN1-deleted SMA patients. The comprehensive analysis of SMN2 methylation in patients suffering from severe versus mild SMA carrying identical SMN2 copy numbers revealed a correlation of CpG methylation at the positions -290 and -296 with the disease severity and the activity of the first transcriptional start site of SMN2 at position -296. These results provide first evidence that SMN2 alleles are functionally not equivalent due to differences in DNA methylation. We demonstrate that the methyl-CpG-binding protein 2, a transcriptional repressor, binds to the critical SMN2 promoter region in a methylation-dependent manner. However, inhibition of SMN2 gene silencing conferred by DNA methylation might represent a promising strategy for pharmacologic SMA therapy. We identified histone deacetylase (HDAC) inhibitors including vorinostat and romidepsin which are able to bypass SMN2 gene silencing by DNA methylation, while others such as valproic acid and phenylbutyrate do not, due to HDAC isoenzyme specificities. These findings indicate that DNA methylation is functionally important regarding SMA disease progression and pharmacological SMN2 gene activation which might have implications for future SMA therapy regimens.',
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<h3>Epigenetic antibodies you can trust!</h3>
<p>Antibody quality is essential for assay success. Diagenode offers antibodies that are actually validated and have been widely used and published by the scientific community. Now we are adding a new level of siRNA knockdown validation to assure the specificity of our non-histone antibodies.</p>
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<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
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<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>',
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<h3>Epigenetic antibodies you can trust!</h3>
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<p><strong>Short interfering RNA (siRNA)</strong> degrades target mRNA, followed by the knock-down of protein production. If the antibody that recognizes the protein of interest is specific, the Western blot of siRNA-treated cells will show a significant reduction of signal vs. untreated cells.</p>
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)
$description = '<div class="row">
<div class="small-10 columns">
<h3>Epigenetic antibodies you can trust!</h3>
<p>Antibody quality is essential for assay success. Diagenode offers antibodies that are actually validated and have been widely used and published by the scientific community. Now we are adding a new level of siRNA knockdown validation to assure the specificity of our non-histone antibodies.</p>
<p><strong>Short interfering RNA (siRNA)</strong> degrades target mRNA, followed by the knock-down of protein production. If the antibody that recognizes the protein of interest is specific, the Western blot of siRNA-treated cells will show a significant reduction of signal vs. untreated cells.</p>
<center><img src="https://www.diagenode.com/emailing/images/C15100144-wb.png" alt="" /></center>
<p class="text-center"><small>WB results obtained with the HDAC1 pAb (Cat. No. C15100144) <br />on siRNA transfected cells (lane 2) and on untransfected control cells (lane 1).</small></p>
</div>
<div class="small-2 columns">
<p><img src="https://www.diagenode.com/emailing/images/epi-success-guaranteed-icon.png" alt="Epigenetic success guaranteed" /></p>
</div>
</div>
<div class="spaced"></div>
<p style="text-align: left;"><span style="font-weight: 400;">The below list shows our first siRNA validated antibodies. More results - coming soon</span>.</p>'
$name = 'siRNA Knockdown'
$document = array(
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'name' => 'Epigenetic Antibodies Brochure',
'description' => '<p>More than in any other immuoprecipitation assays, quality antibodies are critical tools in many epigenetics experiments. Since 10 years, Diagenode has developed the most stringent quality production available on the market for antibodies exclusively focused on epigenetic uses. All our antibodies have been qualified to work in epigenetic applications.</p>',
'image_id' => null,
'type' => 'Brochure',
'url' => 'files/brochures/Epigenetic_Antibodies_Brochure.pdf',
'slug' => 'epigenetic-antibodies-brochure',
'meta_keywords' => '',
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'modified' => '2016-06-15 11:24:06',
'created' => '2015-07-03 16:05:27',
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'name' => 'MeCP2 Antibody SDS ES es',
'language' => 'es',
'url' => 'files/SDS/MeCP2/SDS-C15410052-MeCP2_Antibody-ES-es-GHS_3_0.pdf',
'countries' => 'ES',
'modified' => '2023-01-26 14:24:41',
'created' => '2023-01-26 14:24:41',
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$publication = array(
'id' => '81',
'name' => 'Survival motor neuron gene 2 silencing by DNA methylation correlates with spinal muscular atrophy disease severity and can be bypassed by histone deacetylase inhibition.',
'authors' => 'Hauke J, Riessland M, Lunke S, Eyüpoglu IY, Blümcke I, El-Osta A, Wirth B, Hahnen E',
'description' => 'Spinal muscular atrophy (SMA), a common neuromuscular disorder, is caused by homozygous absence of the survival motor neuron gene 1 (SMN1), while the disease severity is mainly influenced by the number of SMN2 gene copies. This correlation is not absolute, suggesting the existence of yet unknown factors modulating disease progression. We demonstrate that the SMN2 gene is subject to gene silencing by DNA methylation. SMN2 contains four CpG islands which present highly conserved methylation patterns and little interindividual variations in SMN1-deleted SMA patients. The comprehensive analysis of SMN2 methylation in patients suffering from severe versus mild SMA carrying identical SMN2 copy numbers revealed a correlation of CpG methylation at the positions -290 and -296 with the disease severity and the activity of the first transcriptional start site of SMN2 at position -296. These results provide first evidence that SMN2 alleles are functionally not equivalent due to differences in DNA methylation. We demonstrate that the methyl-CpG-binding protein 2, a transcriptional repressor, binds to the critical SMN2 promoter region in a methylation-dependent manner. However, inhibition of SMN2 gene silencing conferred by DNA methylation might represent a promising strategy for pharmacologic SMA therapy. We identified histone deacetylase (HDAC) inhibitors including vorinostat and romidepsin which are able to bypass SMN2 gene silencing by DNA methylation, while others such as valproic acid and phenylbutyrate do not, due to HDAC isoenzyme specificities. These findings indicate that DNA methylation is functionally important regarding SMA disease progression and pharmacological SMN2 gene activation which might have implications for future SMA therapy regimens.',
'date' => '2009-01-15',
'pmid' => 'https://www.ncbi.nlm.nih.gov/pubmed/18971205',
'doi' => '',
'modified' => '2015-07-24 15:38:56',
'created' => '2015-07-24 15:38:56',
'ProductsPublication' => array(
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