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Academic literature on the topic 'MEF2D'

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Published: 9 March 2023
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Journal articles on the topic "MEF2D"

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Zhao, Ming, Liguo New, Vladimir V. Kravchenko, Yutaka Kato, Hermann Gram, Franco di Padova, Eric N. Olson, Richard J. Ulevitch, and Jiahuai Han. "Regulation of the MEF2 Family of Transcription Factors by p38." Molecular and Cellular Biology 19, no. 1 (January 1, 1999): 21–30. http://dx.doi.org/10.1128/mcb.19.1.21.

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ABSTRACT Members of the MEF2 family of transcription factors bind as homo- and heterodimers to the MEF2 site found in the promoter regions of numerous muscle-specific, growth- or stress-induced genes. We showed previously that the transactivation activity of MEF2C is stimulated by p38 mitogen-activated protein (MAP) kinase. In this study, we examined the potential role of the p38 MAP kinase pathway in regulating the other MEF2 family members. We found that MEF2A, but not MEF2B or MEF2D, is a substrate for p38. Among the four p38 group members, p38 is the most potent kinase for MEF2A. Threonines 312 and 319 within the transcription activation domain of MEF2A are the regulatory sites phosphorylated by p38. Phosphorylation of MEF2A in a MEF2A-MEF2D heterodimer enhances MEF2-dependent gene expression. These results demonstrate that the MAP kinase signaling pathway can discriminate between different MEF2 isoforms and can regulate MEF2-dependent genes through posttranslational activation of preexisting MEF2 protein.
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Li, Lucy, Lewis P. Rubin, and Xiaoming Gong. "MEF2 transcription factors in human placenta and involvement in cytotrophoblast invasion and differentiation." Physiological Genomics 50, no. 1 (January 1, 2018): 10–19. http://dx.doi.org/10.1152/physiolgenomics.00076.2017.

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Development of the human placenta and its trophoblast cell types is critical for a successful pregnancy. Defects in trophoblast invasion and differentiation are associated with adverse pregnancy outcomes, including preeclampsia. The members of myocyte enhancer factor-2 (MEF2) family of transcription factors are key regulators of cellular proliferation, differentiation, and invasion in various cell types and tissues and might play a similarly important role in regulating trophoblast proliferation, invasion, and differentiation during human placental development. In the present study, using human cytotrophoblast cell lines (HTR8/SVneo and BeWo) and primary human cytotrophoblasts (CTBs), we show that members of the MEF2 family are differentially expressed in human placental CTBs, with MEF2B and MEF2D being highly expressed in first trimester extravillous CTBs. Overexpression of MEF2D results in cytotrophoblast proliferation and enhances the invasion and migration of extravillous-like HTR8/SVneo cells. This invasive property is blocked by overexpression of a dominant negative MEF2 (dnMEF2). In contrast, MEF2A is the principal MEF2 isoform expressed in term CTBs, MEF2C and MEF2D being expressed more weakly, and MEF2B expression being undetected. Overexpression of MEF2A induces cytotrophoblast differentiation and syncytium formation in BeWo cells. During in vitro differentiation of primary CTBs, MEF2A expression is associated with CTB differentiation into syncytiotrophoblast. Additionally, the course of p38 MAPK and ERK5 activities parallels the increase in MEF2A expression. These findings suggest individual members of MEF2 family distinctively regulate cytotrophoblast proliferation, invasion, and differentiation. Dysregulation of expression of MEF2 family or of their upstream signaling pathways may be associated with placenta-related pregnancy disorders.
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Di Giorgio, Eros, Enrico Gagliostro, Andrea Clocchiatti, and Claudio Brancolini. "The Control Operated by the Cell Cycle Machinery on MEF2 Stability Contributes to the Downregulation of CDKN1A and Entry into S Phase." Molecular and Cellular Biology 35, no. 9 (March 2, 2015): 1633–47. http://dx.doi.org/10.1128/mcb.01461-14.

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MEF2s are pleiotropic transcription factors (TFs) which supervise multiple cellular activities. During the cell cycle, MEF2s are activated at the G0/G1transition to orchestrate the expression of the immediate early genes in response to growth factor stimulation. Here we show that, in human and murine fibroblasts, MEF2 activities are downregulated during late G1. MEF2C and MEF2D interact with the E3 ligase F-box protein SKP2, which mediates their subsequent degradation through the ubiquitin-proteasome system. The cyclin-dependent kinase 4 (CDK4)/cyclin D1 complex phosphorylates MEF2D on serine residues 98 and 110, and phosphorylation of these residues is an important determinant for SKP2 binding. Unscheduled MEF2 transcription during the cell cycle reduces cell proliferation, whereas its containment sustains DNA replication. The CDK inhibitor p21/CDKN1A gene is a MEF2 target gene required to exert this antiproliferative influence. MEF2C and MEF2D bind a region within the first intron ofCDKN1A, presenting epigenetic markers of open chromatin. Importantly, H3K27 acetylation within this regulative region depends on the presence of MEF2D. We propose that following the initial engagement in the G0/G1transition, MEF2C and MEF2D must be polyubiquitylated and degraded during G1progression to diminish the transcription of theCDKN1Agene, thus favoring entry into S phase.
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Edmondson, D. G., G. E. Lyons, J. F. Martin, and E. N. Olson. "Mef2 gene expression marks the cardiac and skeletal muscle lineages during mouse embryogenesis." Development 120, no. 5 (May 1, 1994): 1251–63. http://dx.doi.org/10.1242/dev.120.5.1251.

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Members of the MEF2 family of transcription factors bind a conserved A/T-rich sequence in the control regions of many skeletal and cardiac muscle genes. To begin to assess the roles of the different Mef2 genes in the control of muscle gene expression in vivo, we analyzed by in situ hybridization the expression patterns of the Mef2a, Mef2c and Mef2d genes during mouse embryogenesis. We first detected MEF2C expression at day 7.5 postcoitum (p.c.) in cells of the cardiac mesoderm that give rise to the primitive heart tube, making MEF2C one of the earliest markers for the cardiac muscle lineage yet described. By day 8.5, MEF2A, MEF2C and MEF2D mRNAs are all detected in the myocardium. By day 9.0, MEF2C is expressed in rostral myotomes, where its expression lags by about a day behind that of myf5 and several hours behind that of myogenin. MEF2A and MEF2D are expressed at a lower level than MEF2C in the myotome at day 9.5 and are detected in more embryonic tissues than MEF2C. Expression of each of the MEF2 transcripts is observed in muscle-forming regions within the limbs at day 11.5 p.c. and within muscle fibers throughout the embryo at later developmental stages. The expression of MEF2C in the somites and fetal muscle is distinct from that of MEF2A, MEF2D and the myogenic bHLH regulatory genes, suggesting that it may represent a distinct myogenic cell type. Neural crest cells also express high levels of MEF2 mRNAs between days 8.5 and 10.5 of gestation. After day 12.5 p.c., MEF2 transcripts are detected at high levels in specific regions of the brain and ultimately in a wide range of tissues. The distinct patterns of expression of the different Mef2 genes during mouse embryogenesis suggest that these genes respond to unique developmental cues and support the notion that their products play roles in the regulation of muscle-specific transcription during establishment of the cardiac and skeletal muscle lineages.
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Martin, J. F., J. M. Miano, C. M. Hustad, N. G. Copeland, N. A. Jenkins, and E. N. Olson. "A Mef2 gene that generates a muscle-specific isoform via alternative mRNA splicing." Molecular and Cellular Biology 14, no. 3 (March 1994): 1647–56. http://dx.doi.org/10.1128/mcb.14.3.1647-1656.1994.

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Members of the myocyte-specific enhancer-binding factor 2 (MEF2) family of transcription factors bind a conserved A/T-rich sequence in the control regions of numerous muscle-specific genes. Mammalian MEF2 proteins have been shown previously to be encoded by three genes, Mef2, xMef2, and Mef2c, each of which gives rise to multiple alternatively spliced transcripts. We describe the cloning of a new member of the MEF2 family from mice, termed MEF2D, which shares extensive homology with other MEF2 proteins but is the product of a separate gene. MEF2D binds to and activates transcription through the MEF2 site and forms heterodimers with other members of the MEF2 family. Deletion mutations show that the carboxyl terminus of MEF2D is required for efficient transactivation. MEF2D transcripts are widely expressed, but alternative splicing of MEF2D transcripts gives rise to a muscle-specific isoform which is induced during myoblast differentiation. The mouse Mef2, Mef2c, and Mef2d genes map to chromosomes 7, 13, and 3, respectively. The complexity of the MEF2 family of regulatory proteins provides the potential for fine-tuning of transcriptional responses as a consequence of combinatorial interactions among multiple MEF2 isoforms encoded by the four Mef2 genes.
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Martin, J. F., J. M. Miano, C. M. Hustad, N. G. Copeland, N. A. Jenkins, and E. N. Olson. "A Mef2 gene that generates a muscle-specific isoform via alternative mRNA splicing." Molecular and Cellular Biology 14, no. 3 (March 1994): 1647–56. http://dx.doi.org/10.1128/mcb.14.3.1647.

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Members of the myocyte-specific enhancer-binding factor 2 (MEF2) family of transcription factors bind a conserved A/T-rich sequence in the control regions of numerous muscle-specific genes. Mammalian MEF2 proteins have been shown previously to be encoded by three genes, Mef2, xMef2, and Mef2c, each of which gives rise to multiple alternatively spliced transcripts. We describe the cloning of a new member of the MEF2 family from mice, termed MEF2D, which shares extensive homology with other MEF2 proteins but is the product of a separate gene. MEF2D binds to and activates transcription through the MEF2 site and forms heterodimers with other members of the MEF2 family. Deletion mutations show that the carboxyl terminus of MEF2D is required for efficient transactivation. MEF2D transcripts are widely expressed, but alternative splicing of MEF2D transcripts gives rise to a muscle-specific isoform which is induced during myoblast differentiation. The mouse Mef2, Mef2c, and Mef2d genes map to chromosomes 7, 13, and 3, respectively. The complexity of the MEF2 family of regulatory proteins provides the potential for fine-tuning of transcriptional responses as a consequence of combinatorial interactions among multiple MEF2 isoforms encoded by the four Mef2 genes.
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Aude-Garcia, Catherine, Véronique Collin-Faure, Huguette Bausinger, Daniel Hanau, Thierry Rabilloud, and Claudie Lemercier. "Dual roles for MEF2A and MEF2D during human macrophage terminal differentiation and c-Jun expression." Biochemical Journal 430, no. 2 (August 13, 2010): 237–44. http://dx.doi.org/10.1042/bj20100131.

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Recent reports have evidenced a role for MEF2C (myocyte enhancer factor 2C) in myelopoiesis, although the precise functions of this transcription factor are still unclear. We show in the present study that MEF2A and MEF2D, two other MEF2 family members, are expressed in human primary monocytes and in higher amounts in monocyte-derived macrophages. High levels of MEF2A–MEF2D heterodimers are found in macrophage-differentiated HL60 cells. Chromatin immunoprecipitations demonstrate that MEF2A is present on the c-Jun promoter, both in undifferentiated and in macrophage-differentiated cells. Moreover, c-Jun expression is derepressed in undifferentiated cells in the presence of HDAC (histone deacetylase) inhibitor, indicating the importance of chromatin acetylation in this process. We show that MEF2A/D dimers strongly interact with HDAC1, and to a lesser extent with HDAC7 in macrophages, whereas low levels of MEF2A/D–HDAC1 complexes are found in undifferentiated cells or in monocytes. Since trichostatin A does not disrupt MEF2A/D–HDAC1 complexes, we analysed the potential interaction of MEF2A with p300 histone acetyltransferase, whose expression is up-regulated in macrophages. Interestingly, endogenous p300 only associates with MEF2A in differentiated macrophages, indicating that MEF2A/D could activate c-Jun expression in macrophages through a MEF2A/D–p300 activator complex. The targets of MEF2A/D–HDAC1–HDAC7 multimers remain to be identified. Nevertheless, these data highlight for the first time the possible dual roles of MEF2A and MEF2D in human macrophages, as activators or as repressors of gene transcription.
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Xia, Xin, Caroline Y. Yu, Minjuan Bian, Catalina B. Sun, Bogdan Tanasa, Kun-Che Chang, Dawn M. Bruffett, et al. "MEF2 transcription factors differentially contribute to retinal ganglion cell loss after optic nerve injury." PLOS ONE 15, no. 12 (December 14, 2020): e0242884. http://dx.doi.org/10.1371/journal.pone.0242884.

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Loss of retinal ganglion cells (RGCs) in optic neuropathies results in permanent partial or complete blindness. Myocyte enhancer factor 2 (MEF2) transcription factors have been shown to play a pivotal role in neuronal systems, and in particular MEF2A knockout was shown to enhance RGC survival after optic nerve crush injury. Here we expanded these prior data to study bi-allelic, tri-allelic and heterozygous allele deletion. We observed that deletion of all MEF2A, MEF2C, and MEF2D alleles had no effect on RGC survival during development. Our extended experiments suggest that the majority of the neuroprotective effect was conferred by complete deletion of MEF2A but that MEF2D knockout, although not sufficient to increase RGC survival on its own, increased the positive effect of MEF2A knockout. Conversely, MEF2A over-expression in wildtype mice worsened RGC survival after optic nerve crush. Interestingly, MEF2 transcription factors are regulated by post-translational modification, including by calcineurin-catalyzed dephosphorylation of MEF2A Ser-408 known to increase MEF2A-dependent transactivation in neurons. However, neither phospho-mimetic nor phospho-ablative mutation of MEF2A Ser-408 affected the ability of MEF2A to promote RGC death in vivo after optic nerve injury. Together these findings demonstrate that MEF2 gene expression opposes RGC survival following axon injury in a complex hierarchy, and further support the hypothesis that loss of or interference with MEF2A expression might be beneficial for RGC neuroprotection in diseases such as glaucoma and other optic neuropathies.
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Zhang, Pengcheng, Lianzhong Zhao, Shaowei Qiu, Ravi Bhatia, and Rui Lu. "Essential Roles of Transcription Factor MEF2D in the Maintenance of MLL-Rearranged Acute Myeloid Leukemia." Blood 138, Supplement 1 (November 5, 2021): 2218. http://dx.doi.org/10.1182/blood-2021-149232.

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Abstract Acute myeloid leukemia (AML) is an aggressive disease with uncontrolled proliferation of myeloid progenitor cells and a failure of proper cell differentiation. Chromosomal translocations of the KMT2A (MLL) gene are found in about 10% AMLs affecting both children and adults. Patients harboring MLL rearrangement (MLL-r) have a high relapse rate and poor overall survival, emphasizing an unmet need to understand MLL-r AML pathogenesis and develop new therapeutic means. Through a comparative analysis of super-enhancers in AML cell lines and primary samples, we discovered that MLL-r leukemia cells preferentially gain super-enhancer signals at the MEF2D gene. MEF2D is aberrantly activated in MLL-r AML patient samples and predicts poor disease outcomes, implying a potential oncogenic role of MEF2D. Indeed, depletion of MEF2D inhibits human MLL-r leukemia growth and induces profound differentiation. Mechanistically, MEF2D directly represses CEBPE, a master regulator of myeloid differentiation. CEBPE depletion could rescue the growth defect and cell differentiation induced by MEF2D loss. We also demonstrated that MEF2D is positively regulated by HOXA9, and downregulation of MEF2D is an important mechanism for DOT1L inhibitor-induced anti-leukemia effects. Interestingly, MEF2C, a target of MLL fusion oncoproteins, is by far the most studied MEF2 family member with essential roles in MLL-r AML. Our genetic, biochemical, and integrative genomic data shows that MEF2D and MEF2C, both upregulated in MLL-r AML, interact with each other, colocalize genome-widely, and co-regulate target gene expression. We are currently investigating the molecular mechanisms underlying the interdependent function between MEF2 paralogs in MLL-r AML. Collectively, our findings suggest that MEF2D is a novel transcriptional dependency in MLL-r AML and uncover the MEF2-CEBPE axis as a crucial transcriptional mechanism regulating leukemia cell self-renewal and differentiation block. Disclosures No relevant conflicts of interest to declare.
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Han, T. H., and R. Prywes. "Regulatory role of MEF2D in serum induction of the c-jun promoter." Molecular and Cellular Biology 15, no. 6 (June 1995): 2907–15. http://dx.doi.org/10.1128/mcb.15.6.2907.

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Serum induction of c-jun expression in HeLa cells requires a MEF2 site at -59 in the c-jun promoter. MEF2 sites, found in many muscle-specific enhancers, are bound by a family of transcription factors, MEF2A through -D, which are related to serum response factor in their DNA binding domains. We have found that MEF2D is the predominant protein in HeLa cells that binds to the c-jun MEF2 site. Serum induction of a MEF2 reporter gene was not observed in a line of NIH 3T3 cells which contain low MEF2 site binding activity. Transfection of MEF2D into NIH 3T3 cells reconstituted serum induction, demonstrating that MEF2D is required for the serum response. Deletion analysis of MEF2D showed that its DNA binding domain, when fused to a heterologous transcriptional activation domain, was sufficient for serum induction of a MEF2 reporter gene. This is the domain homologous to that in the serum response factor which is required for serum induction of the c-fos serum response element, suggesting that serum regulation of c-fos and c-jun may share a common mechanism.
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Dissertations / Theses on the topic "MEF2D"

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Schlenker, Friderike [Verfasser], and Boris [Akademischer Betreuer] Fehse. "Der Einfluss der Transkriptionsfaktoren Mef2c und Mef2d auf die Hämatopoese / Friderike Schlenker ; Betreuer: Boris Fehse." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2019. http://d-nb.info/1175584606/34.

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Schlenker, Friderike Verfasser], and Boris [Akademischer Betreuer] [Fehse. "Der Einfluss der Transkriptionsfaktoren Mef2c und Mef2d auf die Hämatopoese / Friderike Schlenker ; Betreuer: Boris Fehse." Hamburg : Staats- und Universitätsbibliothek Hamburg, 2019. http://nbn-resolving.de/urn:nbn:de:gbv:18-95067.

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AROSIO, ALESSANDRO. "Study of transcriptional alterations in Amyotrophic Lateral Sclerosis." Doctoral thesis, Università degli Studi di Milano-Bicocca, 2015. http://hdl.handle.net/10281/94396.

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Amyotrophic Lateral Sclerosis (ALS) is a progressive fatal neuromuscular disease characterized by selective motorneurons loss. Since mutations in TARDBP and FUS genes were discovered to cause familial form of ALS and TDP-43 and FUS proteins play important roles in RNA metabolism, transcriptional alterations emerged as potential pathogenic mechanism. RNA metabolism include several aspects of RNA regulation such as RNA transcription, maturations and regulation. In this study we have investigated two different fields of RNA metabolism: the first one concerns to microRNAs (miRNA) which regulate translation of several mRNAs, and the second one is related to a specific muscular and neuronal transcription factor potential involved in ALS. First, we have assessed any selected miRNAs with neuronal functions in human neuroblastoma cell lines expressing the pathological SOD1(G93A) mutation and we found a small group of altered miRNAs. Subsequently, we explored these miRNAs in the spinal cord of transgenic SOD1(G93A) mice identified a panel of targets commonly altered in SOD1 ALS models. Furthermore, we assessed the expression levels of a panel of selected miRNAs in circulating cells obtain from patients affected by sporadic ALS form (sALS). This approach let us to identify two microRNAs (miR129-5p and miR200c) that were up-regulated in both SOD1 ALS models and in blood cells of patients with sporadic form of disease, evidencing two possible parameters potentially involved in the pathogenesis of both the sporadic and the familial form of ALS. Moreover, we also identified HuD protein as a potential molecular target of miR129-5p; this protein has been previously reported to play a role in neuronal plasticity and in recovery from axonal injury. Indeed, in a cell line stably overespressing mir129-5p we found a reduction in neurite outgrowth and decreased expression levels of differentiation markers with respect to control cells. Taken together these data strongly suggest that microRNAs play a role in ALS pathogenesis and in particular that mir129-5p can affect neuronal plasticity by modulating HuD levels. In the second part of the study we investigated the possible involvement of two members of myocyte enhancer factor 2 (MEF2) family in the pathogenesis of ALS. MEF2D and MEF2C are transcriptional factors playing crucial roles both in muscle and in neuron development and maintenance. We have performed gene expression analysis in peripheral blood mononuclear cells (PBMCs), we showed a strong increased in MEF2D and MEF2C levels both in sporadic and in familial ALS (SOD1+) patients and a direct correlation between MEF2D and MEF2C mRNA levels was observed in patients and controls. Although protein levels were unchanged, a different pattern of distribution for MEF2D-MEF2C proteins in patient cells was found, suggesting a possible lack of their function. To evaluate the transcriptional activity of MEF2 proteins mRNA levels of their downstream targets BDNF, KLF6, RUFY3 and NPEPPS were assessed. Our results showed a significant down-regulation of BDNF, KLF6 and RUFY3 levels confirming that transcriptional activity of both MEF2D and MEF2C isoforms was altered in sporadic and familial ALS patients. In conclusion, our results evidenced a systemic alteration of MEF2D and MEF2C pathways in ALS patients independently from the presence of SOD1 gene mutations, highlighting a possible common feature between the sporadic and the familiar form of disease which are characterized by a different clinical phenotype and pathological hallmarks.
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Rakopoulos, Patricia. "Deciphering the Role of MEF2D Splice Forms During Skeletal Muscle Differentiation." Thèse, Université d'Ottawa / University of Ottawa, 2011. http://hdl.handle.net/10393/19900.

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Members of the Mef2 transcription factor family are extensively studied within the muscle field for their ability to cooperate with the myogenic regulatory factors MyoD and myogenin during muscle differentiation. Although it is known that Mef2 pre-mRNAs undergo alternative splicing, the different splice forms have not been functionally annotated. In this thesis, my studies aimed to characterize three Mef2D splice forms: MEF2Dα'β, MEF2Dαβ, MEF2Dαø. Our results show that MEF2D splice forms can be differentially phosphorylated by p38 MAPK and PKA in vitro. Gene expression analysis using cell lines over-expressing each Mef2D splice form suggests that they can differentially activate desmin, myosin heavy chain and myogenin expression. Mass spectrometry analyses from our pull-down assays reveal known and novel MEF2D binding partners. Our work suggests that Mef2D splice forms have overlapping but distinct roles and provides new insight into the importance of Mef2D alternative splicing during skeletal myogenesis.
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Chan, Shing Fai. "ATM phosphorylates and activates the transcription factor MEF2D for neuronal survival in response to DNA damage." Diss., [La Jolla] : University of California, San Diego, 2009. http://wwwlib.umi.com/cr/ucsd/fullcit?p3359980.

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Thesis (Ph. D.)--University of California, San Diego, 2009.
Title from first page of PDF file (viewed July 22, 2009). Available via ProQuest Digital Dissertations. Vita. Includes bibliographical references (p. 73-92).
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Lima, Guilherme Alves de. "O diabetes abole o aumento da expressão do gene SLC2A4 induzido pela contração muscular \"in vitro\": participação das cinases AMPK E CAMKII e dos fatores transcricionais MEF2D, GEF, HIF-1a e TRa." Universidade de São Paulo, 2011. http://www.teses.usp.br/teses/disponiveis/42/42137/tde-23012012-165455/.

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O gene SLC2A4 codifica a proteína GLUT4, fundamental na homeostasia glicêmica. OBJETIVO: Investigar o efeito do diabetes na expressão do GLUT4 pela atividade contrátil. MÉTODOS: Músculos sóleos de ratos não diabéticos (ND) e diabéticos tratados com insulina (DI) ou salina (DS) foram incubados e contraídos. A expressão de GLUT4, pAMPK e CAMKII foram analisados por PCR e Western blotting, e a atividade de MEF2D, GEF, HIF-1a e TRa1 por gel shift. Células C2C12 transfectadas com plasmídeos contendo os sítios de ligação para MEF2, HIF, e TR foram tratadas com AICAR ou cafeína. RESULTADOS: Em animais ND e DI, a contração aumentou o conteúdo de GLUT4, mas não nos DS. Em animais ND, a contração aumentou a atividade da AMPK e dos fatores MEF2D, GEF e TRa1, mas não nos DS. Em animais ND, os inibidores de AMPK e CAMKII aboliram o aumento do GLUT4 e da atividade de MEF2D e GEF. Em células C2C12 a cafeína e a AMPK ativaram os 3 sítios. CONCLUSÃO: O diabetes abole o aumento da expressão do GLUT4 sob a atividade contrátil devido a redução da atividade de MEF2D, GEF e TRa1 e AMPK.
The SLC2A4 gene encodes the GLUT4 protein, which is essential in glucose homeostasis. OBJECTIVE: To investigate the diabetes effect on muscle contraction-induced in SLC2A4 gene expression. METHODS: Soleus muscles of Non diabetic rats (ND) and diabetic treated with insulin (DI) or saline (DS) were incubated and contracted. The GLUT4, pAMPK and CAMKII expressions were analyzed by PCR and Western blotting, and the MEF2D, GEF, HIF-1a and TRa1 activity by gel shift. C2C12 cells transfected with plasmids containing the binding sites for MEF2, HIF, and TR were treated with AICAR or caffeine. RESULTS: Contraction increased the GLUT4 amount in animals ND and DI, but not in DS. In ND animals, contraction increased AMPK, MEF2D, GEF and TRa1 activity, but not in DS. In ND animals, AMPK and CAMKII inhibitors abolished the GLUT4 increase as like MEF2D and GEF activity. In C2C12 cells AMPK and caffeine activated the 3 sites. CONCLUSION: Diabetes abolishes the muscle contraction-induced GLUT4 increase due to reduced of MEF2D, GEF, TRa1 and AMPK activity.
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Pon, Julia. "The MEF2B regulatory network." Thesis, University of British Columbia, 2015. http://hdl.handle.net/2429/53973.

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Myocyte enhancer factor 2B (MEF2B) is a transcription factor with somatic mutation hotspots at K4, Y69 and D83 in diffuse large B-cell lymphoma (DLBCL) and follicular lymphoma. The recurrence of these mutations indicates that they may drive lymphoma development. However, inferring the mechanisms by which they may drive lymphoma development was complicated by our limited understanding of MEF2B’s normal functions. To expand our understanding of the cellular activities of wildtype and mutant MEF2B, I developed and addressed two hypotheses: (1) identifying genes regulated by wildtype MEF2B will allow identification of cellular phenotypes affected by MEF2B activity and (2) contrasting the DNA binding sites, effects on gene expression and effects on cellular phenotypes of mutant and wildtype MEF2B will indicate mechanisms through which MEF2B mutations may contribute to lymphoma development. To address these hypotheses, I first identified genome-wide MEF2B binding sites and transcriptome-wide gene expression changes mediated by MEF2B. Using these data I identified and validated novel MEF2B target genes. I found that target genes of MEF2B included the cancer genes MYC, TGFB1, CARD11, NDRG1, RHOB, BCL2 and JUN. The identification of target genes led to findings that MEF2B promotes expression of mesenchymal markers, promotes HEK293A cell migration, and inhibits DLBCL cell chemotaxis. I then investigated how K4E, Y69H and D83V mutations change MEF2B’s activity. I found that K4E, Y69H and D83V mutations decreased MEF2B’s capacity to promote gene expression in both HEK293A and DLBCL cells. These mutations also reduced MEF2B’s capacity to alter HEK293A and DLBCL cell movement. Overall, these data support the concept that MEF2B mutations may promote lymphoma development by reducing expression of MEF2B target genes that would otherwise function to help confine germinal centre B-cells to germinal centres. My research demonstrates how observations from genome-scale data can aid in the functional characterization of candidate driver mutations. Moreover, my work provides a unique resource for exploring the role of MEF2B in cell biology. I map for the first time the MEF2B regulome, demonstrating connections between a relatively understudied transcription factor and genes significant to oncogenesis.
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Reilly, Katherine. "MEF2 Isotypes During Skeletal Myogenesis." Thesis, Université d'Ottawa / University of Ottawa, 2015. http://hdl.handle.net/10393/33406.

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The MEF2 family of transcription factors (MEF2A, MEF2C, and MEF2D) are crucial during skeletal muscle differentiation. Although the roles of MEF2D isoforms are well established, the roles of MEF2A and MEF2C are not as well understood. This thesis, we investigated the expression, localization, and function of MEF2A and MEF2C, using specific antibodies. While MEF2A is expressed in both proliferating and differentiated myoblasts, protein levels of MEF2C were only detected during differentiation. During early stages of differentiation MEF2A is expressed in both the cytoplasm and the nucleus. However during later stages of differentiation, it is localized predominately in the nucleus. MEF2C appears to be localized differently depending on which isoform is being investigated. Using an affinity purification and mass spectrometry based approach we identified PRMT1 as a unique interacting protein with MEF2A during skeletal muscle differentiation. PRMT1 is a protein arginine methyltransferase which mediates the addition of methyl groups onto various proteins including histone H4 arginine 3 (H3R4) which is associated with gene activation. Both MEF2A and PRMT1 occupy genomic targets of MEF2A. Inhibition of PRMT1 with a specific inhibitor delays C2C12 myoblast differentiation in the early stages of differentiation but no effect was observed during late stage differentiation. The MEF2 family of transcription factors show distinct but overlapping function during skeletal muscle differentiation.
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Lazzarano, Stefano. "On MEF2C regulation of the chondrocyte phenotype." Thesis, Imperial College London, 2014. http://hdl.handle.net/10044/1/44016.

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Articular cartilage is a highly specialised tissue composed of a mechanically competent matrix and a single cell population - the chondrocytes. The maintaining of a specialised phenotype requires the integration of intracellular signalling, that in response to appropriate extracellular stimuli, results in expression of cell-specific genes. Previous work in our laboratory has identified hypoxia as one such key stimulus, which through HIF-2α, enhances expression of cartilage master regulator SOX9 and its matrix-encoding target genes (COL2A1, AGC and COL9A1). MEF2C transcription factor is known to be involved in muscle and cardiovascular development; however, recently it has been shown to play a key role in chondrocyte hypertrophy co-ordinately with SOX9. In a previous microarray analysis, we found that MEF2C was upregulated during hypoxia-induced re-dedifferentiation of human articular chondrocytes (HACs); interestingly where its suggested genetic target - COL10A1 - was barely detectable. In this research we therefore investigated a possible new and unknown function of MEF2C transcription factor as a potential genetic regulator of the permanent articular chondrocyte phenotype. In this study, MEF2C protein was detected with a nuclear localisation in chondrocytes in situ in intact healthy human articular cartilage. Experiments in isolated HACs revealed that, at both gene and protein levels, hypoxia enhances MEF2C expression in a HIF-2α and SOX9 dependent fashion. Subsequently, depletion experiments of MEF2C indicated that it is required for SOX9 gene expression both in normoxia and hypoxia. Our results, therefore suggest a mutual positive regulation between MEF2C and SOX9 transcription factors in articular cartilage. Thus, based on our studies a new and critical function for transcription factor MEF2C in HACs has been identified, where it helps promote expression of the differentiated chondrocyte phenotype through mutual regulation with SOX9. These findings give important new insights into our understanding of the transcription factor networks that regulate expression of the articular chondrocyte phenotype.
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Agarwal, Pooja. "Transcriptional control of neural crest development by MEF2C." Diss., Search in ProQuest Dissertations & Theses. UC Only, 2009. http://gateway.proquest.com/openurl?url_ver=Z39.88-2004&rft_val_fmt=info:ofi/fmt:kev:mtx:dissertation&res_dat=xri:pqdiss&rft_dat=xri:pqdiss:3390029.

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Books on the topic "MEF2D"

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Flavell, Steven Willem. Regulation of synapse development by the activity-regulated transcription factor MEF2. 2009.

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Book chapters on the topic "MEF2D"

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Mao, Zixu, and Xuemin Wang. "Expression, Function, and Regulation of Transcription Factor MEF2 in Neurons." In Transcription Factors in the Nervous System, 285–305. Weinheim, FRG: Wiley-VCH Verlag GmbH & Co. KGaA, 2006. http://dx.doi.org/10.1002/3527608036.ch14.

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"Design of HBc-based nanoparticles for efficient delivery of MEF2D siRNA and induction of apoptosis of hepatoma cells." In Advances in Engineering Materials and Applied Mechanics, 555–60. CRC Press, 2015. http://dx.doi.org/10.1201/b19268-97.

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Chen, Yen-Hao, Saleh Heneidi, and Ricardo Azziz. "Transcriptional Activator MEF2A Is Overexressed in Adipocytes of PCOS Patients." In BASIC/TRANSLATIONAL - Diabetes & Glucose Homeostasis: Genetic & Translational Approaches, P2–521—P2–521. The Endocrine Society, 2011. http://dx.doi.org/10.1210/endo-meetings.2011.part3.p6.p2-521.

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Cox, David M., Min Du, and John C. McDermott. "Proteomic Analysis of MEF2 Post-Translational Regulation in the Heart." In Heart Development and Regeneration, 805–24. Elsevier, 2010. http://dx.doi.org/10.1016/b978-0-12-381332-9.00038-4.

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Black, Brian L., and Eric N. Olson. "Control of Cardiac Development by the MEF2 Family of Transcription Factors." In Heart Development, 131–42. Elsevier, 1999. http://dx.doi.org/10.1016/b978-012329860-7/50010-6.

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Shalizi, Aryaman K., and Azad Bonni. "Brawn for Brains: The Role of MEF2 Proteins in the Developing Nervous System." In Current Topics in Developmental Biology, 239–66. Elsevier, 2005. http://dx.doi.org/10.1016/s0070-2153(05)69009-6.

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Conference papers on the topic "MEF2D"

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Giorgio, Eros Di, Liqing Wang, Yan Xiong, Rongxiang Han, Arabinda Samanta, Matteo Trevisanut, and Wayne W. Hancock. "Abstract 69: A biological circuit involving Mef2c, Mef2d and Hdac9 controls the immunosuppressive functions of CD4+Foxp3+ T-regulatory cells and anti-cancer immunity." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-69.

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Kong, Jing, Xiaoping Liu, Jun Chen, and Fang Fang. "Down-regulation of MEF2D via HBc Nanoparticle Mediated siRNA Inhibits HepG2 Cell Proliferation in vitro." In 5th International Conference on Information Engineering for Mechanics and Materials. Paris, France: Atlantis Press, 2015. http://dx.doi.org/10.2991/icimm-15.2015.44.

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Cao, Zhendong, Krista A. Budinich, Hua Huang, Bin Lu, Zhen Zhang, Diqiu Ren, Yeqiao Zhou, et al. "Abstract LB205: The IRF8-MEF2D transcription factor circuit regulated by a druggable multiple post-translational modification (PTM) reader ZMYND8 in acute myeloid leukemia." In Proceedings: AACR Annual Meeting 2021; April 10-15, 2021 and May 17-21, 2021; Philadelphia, PA. American Association for Cancer Research, 2021. http://dx.doi.org/10.1158/1538-7445.am2021-lb205.

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Basiev, Tasoltan T., Sergey B. Mirov, and S. A. Sychev. "Passive laser Q-switches based on MeF2:Nd2+(Me-Ca, Sr, Ba) crystals." In XIV International Conference on Coherent and Nonlinear Optics, edited by Vyacheslav V. Osiko. SPIE, 1992. http://dx.doi.org/10.1117/12.131772.

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Martis, Prithy C., Atira Dudley, Melissa A. Laramore, Barry H. Smith, and Lawrence S. Gazda. "Abstract 4609: MEF2 plays a critical role in RENCA macrobead-induced tumor cell growth inhibition." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4609.

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Li, Ruihua. "Investigation of the main crystals in a MeF2-YF3-AlF3 (Me=Mg+Ca+Sr+Ba) glass." In International Conference on Optoelectronic Science and Engineering '90. SPIE, 1990. http://dx.doi.org/10.1117/12.2294839.

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Zheng, Ruifang, Xuening Wang, and George P. Studzinski. "Abstract 4233: Mef2C enhances 1,25-dihydroxyvitamin D3-induced monocytic differentiation of human myeloid leukemia cells by regulating C/EBPβ expression." In Proceedings: AACR Annual Meeting 2014; April 5-9, 2014; San Diego, CA. American Association for Cancer Research, 2014. http://dx.doi.org/10.1158/1538-7445.am2014-4233.

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Bhawe, Kaumudi, Quentin Felty, Changwon Yoo, and Deodutta Roy. "Abstract 4391: Aberrant transcription factor activity of NRF1, NFE2L2, E2F1, RFX1, and MEF2 associated with severity of astrocytoma." In Proceedings: AACR Annual Meeting 2020; April 27-28, 2020 and June 22-24, 2020; Philadelphia, PA. American Association for Cancer Research, 2020. http://dx.doi.org/10.1158/1538-7445.am2020-4391.

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Martis, Prithy C., Melissa A. Laramore, Atira Dudley, Barry H. Smith, and Lawrence S. Gazda. "Abstract 1675: MEF2 plays a significant role in the tumor inhibitory effects of agarose encapsulated RENCA cells through the EGF receptor." In Proceedings: AACR 106th Annual Meeting 2015; April 18-22, 2015; Philadelphia, PA. American Association for Cancer Research, 2015. http://dx.doi.org/10.1158/1538-7445.am2015-1675.

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Martis, Prithy C., Melissa A. Laramore, Atira T. Dudley, Barry H. Smith, and Lawrence S. Gazda. "Abstract B36: RENCA macrobead-induced AKT hyperphosphorylation leads to MEF2 activation and inhibition of the proliferation of human DU145 prostate carcinoma cells." In Abstracts: AACR Special Conference on Developmental Biology and Cancer; November 30 - December 3, 2015; Boston, Massachusetts. American Association for Cancer Research, 2016. http://dx.doi.org/10.1158/1557-3125.devbiolca15-b36.

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Reports on the topic "MEF2D"

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Morfin, C., and G. G. Loots. Characterizing the role of Mef2c in regulating osteoclast differentiation and energy metabolism. Office of Scientific and Technical Information (OSTI), April 2018. http://dx.doi.org/10.2172/1459127.

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