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MEF2A knockdown accelerates human coronary artery endothelial cells senescence, and the underlying molecular mechanism may be involved in down-regulation of the genes related with cell proliferation, development, inflammation and survival, in which PIK3CG may play a key role.
MEF2 acetylation is required for development and maintenance of pathological cardiac hypertrophy, blocking MEF2 acetylation can permit recovery from hypertrophy without impairing physiologic adaptation
PCGME1 silencing by small interfering RNA significantly induced early cell apoptosis but this effect was reduced by a miR148a inhibitor. In conclusion, the present study demonstrated a positive regulatory association between MEF2 and PCGEM1, and a reciprocal negative regulatory association between PCGEM1 and miR148a that controls cell apoptosis.
H cordata promotes the activation of HIF-1A-FOXO3 and MEF2A pathways.
in leiomyosarcomas (LMS), this two-faced trait of MEF2 is relevant for tumor aggressiveness. Class IIa HDACs are overexpressed in 22% of LMS, where high levels of MEF2, HDAC4 and HDAC9 inversely correlate with overall survival. The knock out of HDAC9 suppresses the transformed phenotype of LMS cells, by restoring the transcriptional proficiency of some MEF2-target loci
The discovery of a novel MEF2A mutation in a Chinese family with premature CAD/MI suggests that MEF2A may have a significant role in the pathogenesis of premature CAD/MI.
The findings of this study are consistent with MEF2A deregulation conferring risk of formal thought disorder.
Variants in the 3'-UTR of MEF2A are associated with coronary artery disease in a Chinese Han population.
p38 MAPK is a key regulator of canonical Wnt signaling by promoting a phospho-dependent interaction between MEF2 and beta-catenin to enhance cooperative transcriptional activity and cell proliferation.
Mechanistically, MEF-2 was recruited to the viral promoter (LTR, long terminal repeat) in the context of chromatin, and constituted Tax/CREB transcriptional complex via direct binding to the HTLV-1 LTR.
Our results revealed a link and interaction between MEF2A and miR-143 and suggested a potential mechanism for MEF2A to regulate H(2)O(2) -induced VSMC senescence.
six or seven amino acid deletions and synonymous mutations (147143G-->A)in exon 11 of the MEF2A gene may be correlated with susceptibility to coronary artery disease in the Chinese population
MEF2A is targeted to lysosomes for chaperone-mediated autophagy degradation; oxidative stress-induced lysosome destabilization leads to the disruption of MEF2A degradation as well as the dysregulation of its function
MEF2 transcription factors promotes epithelial-mesenchymal transition and invasiveness of hepatocellular carcinoma through TGF-beta1 autoregulation circuitry.
MEF2 is the key cis-acting factor that regulates expression of a number of transcriptional targets involved in pulmonary vascular homeostasis, including microRNAs 424 and 503, connexins 37, and 40, and Kruppel Like Factors 2 and 4.
SENP2 plays an important role in determining the dynamics and functional outcome of MEF2A SUMOylation and transcriptional activation.
This study expands our understanding of the regulation of MEF2 in skeletal muscle and identifies the mAKAP scaffold as a facilitator of MEF2 transcription and myogenic differentiation.
Correlation studies depicted two distinct groups of soft tissue sarcomas: one in which MEF2 repression correlates with PTEN downregulation and a second group in which MEF2 repression correlates with HDAC4 levels.
Mutations in MEF2A exon12 are implicated in pathogenesis of premature coronary artery disease in the Chinese population.
Substitution of any of the TFBS from our particular search of MEF2, CREB and SRF significantly decreased the number of identified clusters.
Canonical pathway analysis of genes preferentially dysregulated in the atria and ventricles revealed distinct MEF2A-dependent cellular processes in each cardiac chamber. In the atria, MEF2A regulated genes involved in fibrosis and adhesion, whereas in the ventricles, it controlled inflammation and endocytosis.
Both synapse silencing and elimination required de novo transcription, but only silencing required the activity-dependent transcription factors MEF2A/D.
Deficiency of AKT2 in myocardium results in diminished MEF2A abundance, which induced decreased size of cardiomyocytes. We additionally confirmed that EndoG, which is also regulated by AKT2, is a suppressor of MEF2A in myocardium.
these data indicate that MEF2 and AP-1 confer antagonistic regulation of Hspb7 gene expression in skeletal muscle, with implications for autophagy and muscle atrophy.
Nuclear HDAC4 binds to chromatin as well as to MEF2A transcription factor, leading to histone deacetylation and altered neuronal gene expression. By using a Cdkl5 knockout (Cdkl5 -/Y) mouse model, we found that hypophosphorylated HDAC4 translocates to the nucleus of neural precursor cells, thereby reducing histone 3 acetylation.
Knockdown of MEF2A significantly reduced hyperglycemia-induced cardiac fibroblast proliferation and migration, myofibroblast differentiation, matrix metalloproteinase activities, and collagen production.
Lentivirus-mediated MEF 2A shRNA accelerates inflammation and atherosclerosis in APOE knockout mice, but has no effect on lipoprotein levels in plasma.
microRNAs encoded by the Gtl2-Dio3 noncoding RNA locus function downstream of the MEF2A
Our results indicated that exercise-induced CPT1b expression was at least in part mediated by HDAC5/MEF2A interaction.
Whereas MEF2A is absolutely required for proper myoblast differentiation, MEF2B, -C, and -D were found to be dispensable for this process.
A role for endogenous MEF2 factors exclusively in hormone/Fsk/cAMP-induced Nr4a1 gene expression in mouse MA-10 Leydig cells.
Combined deletion of the Mef2a, c, and d genes results in a blockade to muscle regeneration.
Cross-talk between p38MAPK and GSK3beta signaling converges on MEF2 activity.
Myocyte enhancer factor 2A (MEF2A) controls skeletal muscle regeneration in adult mice through direct regulation of the largest known mammalian microRNA (miRNA) cluster, the Gtl2-Dio3 locus.
These results give novel insight into the molecular interplay of GR and MEF2 in the control of genes important for neuronal plasticity.
MEF2A, but not MEF2C or MEF2D, is modified by ubiquitination in dopaminergic neuronal cell line SN4741 cells.
The data highlighted the key in vivo role of MEF2C isoform in the brain and suggest that MEF2A and MEF2D have only subtle roles in regulating hippocampal synaptic function.
establish miR-155 as an important regulator of MEF2A expression and uncover its function in muscle gene expression and myogenic differentiation.
Exercise increases the nuclear MEF2A content and binding of MEF2A to their binding sites on the Glut4 gene by an AMPKalpha2-dependent mechanism.
Mef2 controls skeletal muscle formation after terminal differentiation.
Results suggest that myocyte-specific enhancer factor 2A is essential for cardiac contractility
Results suggest that myocyte enhancer factor 2A is essential for zebrafish posterior somite development.
MEF2A is a positive regulator in skeletal muscle myoblast proliferation
polymorphisms in the bovine MEF2A gene and their effect on the MEF2A mRNA expression level in the longissimus dorsi muscle
The discovery of new alternatively spliced transcripts of the MEF2A gene may be utilized in understanding its biological functions.
These results show that NLK specifically regulates the MEF2A activity required for anterior formation in Xenopus development.
The protein encoded by this gene is a DNA-binding transcription factor that activates many muscle-specific, growth factor-induced, and stress-induced genes. The encoded protein can act as a homodimer or as a heterodimer and is involved in several cellular processes, including muscle development, neuronal differentiation, cell growth control, and apoptosis. Defects in this gene could be a cause of autosomal dominant coronary artery disease 1 with myocardial infarction (ADCAD1). Several transcript variants encoding different isoforms have been found for this gene.
MADS box transcription enhancer factor 2, polypeptide A (myocyte enhancer factor 2A)
, myocyte-specific enhancer factor 2A
, serum response factor-like protein 1
, myocyte enhancer factor 2a
, myocyte-specific enhancer factor 2a
, myocyte-specific enhancer factor 2A homolog
, serum response factor-like protein 2
, myocyte enhancer factor 2A
, myocyte-specific enhancer factor 2A-like