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Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases
The signal transduction pathway or pathways linking extracellular signals to myogenesis are poorly defined. Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK...
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| Published in: | Science (American Association for the Advancement of Science) 1997-11, Vol.278 (5341), p.1288-1291 |
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| Language: | English |
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| cited_by | cdi_FETCH-LOGICAL-c785t-d17e075ded81528120b5404b33213271152e48ea373fde44091a9ce55afbcc473 |
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| cites | cdi_FETCH-LOGICAL-c785t-d17e075ded81528120b5404b33213271152e48ea373fde44091a9ce55afbcc473 |
| container_end_page | 1291 |
| container_issue | 5341 |
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| container_title | Science (American Association for the Advancement of Science) |
| container_volume | 278 |
| creator | Bennett, Anton M. Tonks, Nicholas K. |
| description | The signal transduction pathway or pathways linking extracellular signals to myogenesis are poorly defined. Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. This indicates that muscle-specific gene expression is necessary but not sufficient to commit differentiated myocytes to myotubes and suggests a function for the MAPKs during the early and late stages of skeletal muscle differentiation. |
| doi_str_mv | 10.1126/science.278.5341.1288 |
| format | article |
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Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. This indicates that muscle-specific gene expression is necessary but not sufficient to commit differentiated myocytes to myotubes and suggests a function for the MAPKs during the early and late stages of skeletal muscle differentiation.</description><identifier>ISSN: 0036-8075</identifier><identifier>EISSN: 1095-9203</identifier><identifier>DOI: 10.1126/science.278.5341.1288</identifier><identifier>PMID: 9360925</identifier><identifier>CODEN: SCIEAS</identifier><language>eng</language><publisher>Washington, DC: American Society for the Advancement of Science</publisher><subject>Animals ; Antibodies ; Biological and medical sciences ; Calcium-Calmodulin-Dependent Protein Kinases - metabolism ; Cell cycle ; Cell Cycle Proteins ; Cell Differentiation ; Cell differentiation, maturation, development, hematopoiesis ; Cell Division ; Cell Line ; Cell physiology ; Cellular signal transduction ; Cloning, Molecular ; Culture Media ; Cyclin D1 - genetics ; Cyclins ; Dual Specificity Phosphatase 1 ; Fundamental and applied biological sciences. 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Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. 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metabolism</topic><topic>Cell cycle</topic><topic>Cell Cycle Proteins</topic><topic>Cell Differentiation</topic><topic>Cell differentiation, maturation, development, hematopoiesis</topic><topic>Cell Division</topic><topic>Cell Line</topic><topic>Cell physiology</topic><topic>Cellular signal transduction</topic><topic>Cloning, Molecular</topic><topic>Culture Media</topic><topic>Cyclin D1 - genetics</topic><topic>Cyclins</topic><topic>Dual Specificity Phosphatase 1</topic><topic>Fundamental and applied biological sciences. 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or pathways linking extracellular signals to myogenesis are poorly defined. Upon mitogen withdrawal from C2C12 myoblasts, the mitogen-activated protein kinase (MAPK) p42Erk2 is inactivated concomitant with up-regulation of muscle-specific genes. Overexpression of MAPK phosphatase-1 (MKP-1) inhibited p42Erk2 activity and was sufficient to relieve the inhibitory effects of mitogens on muscle-specific gene expression. Later during myogenesis, endogenous expression of MKP-1 decreased. MKP-1 overexpression during differentiation prevented myotube formation despite appropriate expression of myosin heavy chain. This indicates that muscle-specific gene expression is necessary but not sufficient to commit differentiated myocytes to myotubes and suggests a function for the MAPKs during the early and late stages of skeletal muscle differentiation.</abstract><cop>Washington, DC</cop><pub>American Society for the Advancement of Science</pub><pmid>9360925</pmid><doi>10.1126/science.278.5341.1288</doi><tpages>4</tpages></addata></record> |
| fulltext | fulltext |
| identifier | ISSN: 0036-8075 |
| ispartof | Science (American Association for the Advancement of Science), 1997-11, Vol.278 (5341), p.1288-1291 |
| issn | 0036-8075 1095-9203 |
| language | eng |
| recordid | cdi_proquest_miscellaneous_79399815 |
| source | American Association for the Advancement of Science; Social Science Premium Collection; Alma/SFX Local Collection; Education Collection |
| subjects | Animals Antibodies Biological and medical sciences Calcium-Calmodulin-Dependent Protein Kinases - metabolism Cell cycle Cell Cycle Proteins Cell Differentiation Cell differentiation, maturation, development, hematopoiesis Cell Division Cell Line Cell physiology Cellular signal transduction Cloning, Molecular Culture Media Cyclin D1 - genetics Cyclins Dual Specificity Phosphatase 1 Fundamental and applied biological sciences. Psychology Gene expression regulation Gene Expression Regulation, Developmental Genes Genetically modified organisms Immediate-Early Proteins - genetics Immediate-Early Proteins - metabolism Individualized Instruction Inhibition JNK Mitogen-Activated Protein Kinases Mice Mitogen-Activated Protein Kinase 1 - antagonists & inhibitors Mitogen-Activated Protein Kinase 1 - metabolism Mitogen-Activated Protein Kinases Mitogens Mitogens - pharmacology Molecular and cellular biology Muscle cells Muscle development Muscle fibers Muscle Proteins - genetics Muscle, Skeletal - cytology Muscle, Skeletal - enzymology Muscle, Skeletal - metabolism Muscular system Myoblasts Phosphoprotein Phosphatases Phosphorylation Protein Phosphatase 1 Protein Tyrosine Phosphatases - genetics Protein Tyrosine Phosphatases - metabolism Proteins Recombinant Fusion Proteins - metabolism Signal Transduction Skeletal muscle Skeletal system Tetracycline - pharmacology Transcription, Genetic |
| title | Regulation of Distinct Stages of Skeletal Muscle Differentiation by Mitogen-Activated Protein Kinases |
| url | http://sfxeu10.hosted.exlibrisgroup.com/loughborough?ctx_ver=Z39.88-2004&ctx_enc=info:ofi/enc:UTF-8&ctx_tim=2025-01-01T01%3A00%3A59IST&url_ver=Z39.88-2004&url_ctx_fmt=infofi/fmt:kev:mtx:ctx&rfr_id=info:sid/primo.exlibrisgroup.com:primo3-Article-gale_proqu&rft_val_fmt=info:ofi/fmt:kev:mtx:journal&rft.genre=article&rft.atitle=Regulation%20of%20Distinct%20Stages%20of%20Skeletal%20Muscle%20Differentiation%20by%20Mitogen-Activated%20Protein%20Kinases&rft.jtitle=Science%20(American%20Association%20for%20the%20Advancement%20of%20Science)&rft.au=Bennett,%20Anton%20M.&rft.date=1997-11-14&rft.volume=278&rft.issue=5341&rft.spage=1288&rft.epage=1291&rft.pages=1288-1291&rft.issn=0036-8075&rft.eissn=1095-9203&rft.coden=SCIEAS&rft_id=info:doi/10.1126/science.278.5341.1288&rft_dat=%3Cgale_proqu%3EA20035390%3C/gale_proqu%3E%3Cgrp_id%3Ecdi_FETCH-LOGICAL-c785t-d17e075ded81528120b5404b33213271152e48ea373fde44091a9ce55afbcc473%3C/grp_id%3E%3Coa%3E%3C/oa%3E%3Curl%3E%3C/url%3E&rft_id=info:oai/&rft_pqid=213573199&rft_id=info:pmid/9360925&rft_galeid=A20035390&rft_jstor_id=2894192&rfr_iscdi=true |