MEF2C
- Known as:
- MEF2C
- Catalog number:
- 000599A
- Product Quantity:
- 250ul
- Category:
- -
- Supplier:
- ABM
- Gene target:
- MEF2C
Related genes to: MEF2C
- Gene:
- MEF2C NIH gene
- Name:
- myocyte enhancer factor 2C
- Previous symbol:
- -
- Synonyms:
- -
- Chromosome:
- 5q14.3
- Locus Type:
- gene with protein product
- Date approved:
- 1995-02-08
- Date modifiied:
- 2015-08-25
Related products to: MEF2C
Anti-Human MEF2C, Rabbit Polyclonalanti-MEF2Canti-MEF2Canti-MEF2Canti-MEF2Canti-MEF2C (Ser396)anti-MEF2C (Ser59)Anti-MEF2C Antibodyanti-MEF2C type: Primary antibodies host: Mouseanti-MEF2C type: Primary antibodies host: RabbitAnti-MEF2C, Rabbit Polyclonal to MEF2C, Isotype , Host RabbitAnti-MEF2C, Rabbit Polyclonal to MEF2C, Isotype , Host RabbitBovine myocyte enhancer factor 2C (MEF2C) ELISA kit, Species Bovine, Sample Type serum, plasmaBovine Myocyte-specific enhancer factor 2C (MEF2C) ELISA KitBovine Myocyte-specific enhancer factor 2C (MEF2C) ELISA Kit Related articles to: MEF2C
- This study aimed to develop a KeMA hydrogel encapsulating cartilage-affinity peptide (CAP)-modified extracellular vesicles (EVs) derived from MEF2C-overexpressing macrophages (KeMA@CAP-EVs-MEF2C) to modulate the MEF2C/P21/CDK2 axis, attenuating inflammation in cartilaginous endplate chondrocytes (CEPCs) and cellular senescence in nucleus pulposus cells (NPCs) to slow intervertebral disc degeneration (IVDD) progression. Single-cell RNA sequencing (scRNA-seq) identified MEF2C as a key regulator, upregulating p21 and suppressing CDK2 to reduce inflammation and cellular senescence. CAP-modified EVs within KeMA hydrogel demonstrated enhanced delivery and sustained-release properties. In vivo validation showed effective mitigation of cellular senescence and structural restoration in IVDD. This biomimetic system offers a promising strategy for IVDD treatment, emphasizing its targeting efficiency, biocompatibility, and sustained therapeutic benefits. - Source: PubMed
Publication date: 2026/04/17
Guan Jian-BinLin Kai-YuanWang Shan-XiWang Ying-GuangLi Ling-JiangWang Ren-JiZou PengBai Xiao-FanWang Si-BoYan LiangZhao Yuan-TingYu Xiao-Jun - During the hair cycle and wound regeneration, various developmental transcriptomic features are reactivated. Consequently, studying skin development provides critical insights into both fundamental biology and skin regeneration. However, chromatin accessibility during skin development remains underexplored. To address this gap, we conducted integrated single-cell chromatin and transcriptomic analyses of developing mouse skin. Our investigation revealed key gene network axes underlying skin lineage specification. In particular, our multi-omics approach identified Mef2c+ upper fibroblasts as putative precursor cells for smooth muscle-like appendages, such as the arrector pili muscle. Furthermore, leveraging the fetal human skin atlas, we uncovered strong cross-species correlations between mouse and human skin during development. We identified an MEF2C+ fibroblast counterpart in human fetal skin and further delineated fibroblast lineages, including dermal sheath and arrector pili muscle, demonstrating that fibroblast developmental timelines are conserved between mouse and human. Together, this study establishes a robust, human-translatable foundation for future investigations into skin development and regeneration. - Source: PubMed
Publication date: 2026/04/17
Lee HanjaeLee SeungheeJo Seong JinLee SunhyoungGo HyunjungKwon OhsangKim Jong-Il - Skeletal muscle fiber composition is a key determinant of meat quality and metabolic traits. The early postnatal period constitutes a primary window for muscle fiber transformation. In this study, distinct muscle fiber composition is analyzed by histological and molecular characterization of longissimus dorsi muscle of 2-week-old lean-type and Chinese indigenous pigs. Multi-omics analyses reveal divergence in chromatin states, enhancer landscapes, and promoter activity between breeds. Lean-type pigs show increased chromatin accessibility and enhancer activation at genes involved in oxidative metabolism and myogenesis, whereas Chinese indigenous pigs exhibit enriched regulatory features at glycolytic and biosynthetic loci. Breed-specific SNPs and indels are enriched in a subset of enhancers and potentially influence transcriptional regulation. Higher-order genome architecture further contributes to transcriptional divergence through A/B compartment switching and topologically associating domain boundary remodeling. Promoter-enhancer interaction mapping reveals breed-specific cis-regulatory networks, and transcriptional output correlates with enhancer density. Functional validation identifies a super-enhancer upstream of PPP3CB that recruits MEF2C to activate oxidative fiber programs. In vitro and in vivo perturbation assays confirm that the PPP3CB-MEF2C feedback loop governs muscle fiber-type specification. Collectively, these findings delineate the epigenomic and 3D genomic architecture underlying early muscle fiber characteristics and provide mechanistic insights relevant to improving meat quality. - Source: PubMed
Publication date: 2026/04/17
Zheng ShuailongWu HainanLiu MinWu KunpengHuang ShuntaoAhmed ZulfiqarPius LenoxZhu MengjinXu Dequan - (words: 246): Fortilin, a 172 amino acid modulator protein that positively regulates survival and growth pathways, is one of the most abundantly expressed proteins in the heart, and its loss leads to lethal heart failure. While fortilin binds and protects catenin alpha-3 (CTNNA3)-a cardiomyocyte structural and survival protein-against degradation, its role in the transcriptional regulation of CTNNA3 has remained unknown. Here, we report that fortilin also promotes CTNNA3 transcription. Mechanistically, we found that fortilin specifically bound to the N-terminal region (amino acids 1-85) of myocyte enhancer factor 2C (MEF2C)-a transcription factor that drives CTNNA3 expression-but not to MEF2A, MEF2B, or MEF2D, under the experimental conditions tested and as shown by microscale thermophoresis, proximity ligation assay, and in vitro and in vivo co-immunoprecipitation western blot analyses. Molecular docking and site-directed mutagenesis identified a critical binding interface involving Asp of fortilin, whereby an Asp-to-alanine mutation markedly weakened binding to MEF2C. Additionally, fortilin protected MEF2C against ubiquitination and proteasomal degradation and promoted MEF2C serine 59 phosphorylation, a modification essential for its transcriptional activity, both in a binding-dependent manner. Loss of fortilin significantly impaired MEF2C binding to nuclear DNA, reduced CTNNA3 promoter-driven luciferase activity in a MEF2C-dependent fashion, and lowered RNA polymerase II occupancy on the CTNNA3 locus. These data suggest that fortilin is a previously unrecognized transcriptional co-factor of MEF2C. By stabilizing MEF2C and promoting its activating phosphorylation, fortilin enhances the transcription of CTNNA3 while simultaneously stabilizing CTNNA3 protein, thereby sustaining CTNNA3 expression and supporting myocardial structural integrity. - Source: PubMed
Publication date: 2026/03/31
Nakashima MariMukherjee SandipanPinkaew DechaPal Uttariyavan Hengel JolandaBerx GeertFujise Ken - Skeletal muscle responds to stressors such as exercise and muscle injury by adaptive remodelling. The resilience of skeletal muscle involves not only mature muscle fibres but also the adjacent muscle satellite cells (MuSCs). We previously found that transient receptor potential vanilloid type 2 (TRPV2) is expressed in MuSCs and is essential for MuSC proliferation and activation in MuSC-specific conditional knockout mice. These mice show no mechanical-load-induced muscle hypertrophy and delayed injury-induced muscle regeneration. The effect of TRPV2 on Ca signalling during early myogenesis is unknown; however, here, we demonstrate that tranilast, an inhibitor of TRPV2, suppressed IPR-derived Ca oscillations in early myogenesis. The addition of adenovirus (Ad)-TRPV2 or Ad-Cre recombinase to floxed-TRPV2 cells modulated TRPV2 expression, and demonstrated the TRPV2 dependence of IPR and MEF2c expression, nuclear translocation of MEF2c, and Ca oscillations. These findings indicate that TRPV2 regulates intracellular Ca signalling during early myogenesis and highlight its potential as a target for the prevention and treatment of muscle disorders. - Source: PubMed
Publication date: 2026/03/25
Chen YanzhuKatanosaka KimiakiKatanosaka Yuki