Analysis of CMF1 Reveals a Bone Morphogenetic Protein-independent Component of the Cardiomyogenic Pathway
Disruption of the CMF1 function in anterior mesoderm inhibits cardiac myogenesis in avian embryos. In the present study, we show that CMF1 is a member of an emerging family of proteins that includes centromeric protein-F, mitosin, and LEK1. These proteins are characterized by their large size (350 k...
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Veröffentlicht in: | The Journal of biological chemistry 2000-07, Vol.275 (28), p.21453-21459 |
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description | Disruption of the CMF1 function in anterior mesoderm inhibits cardiac myogenesis in avian embryos. In the present study, we show that CMF1 is a member of an emerging family of proteins that includes centromeric protein-F, mitosin, and LEK1. These proteins are characterized by their large size (350 kDa), dynamic subcellular distribution, and potential functions in cell division and differentiation. The current data suggest that CMF1 is a unique member of this family by virtue of its restricted protein expression and variant subcellular distribution. Immunochemical analysis demonstrates that CMF1 protein is expressed in cardiogenic cells prior to the activation of cardiac structural gene products. In addition, we show that expression of CMF1 is not dependent on the bone morphogenetic protein (BMP) signaling pathway during development. Still, CMF1 cannot direct cardiomyogenesis in the absence of such factors as NKX-2.5. Taken with our previous data, this study suggests that CMF1 is a BMP-independent component of the cardiomyogenic pathway. |
doi_str_mv | 10.1074/jbc.M000518200 |
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In the present study, we show that CMF1 is a member of an emerging family of proteins that includes centromeric protein-F, mitosin, and LEK1. These proteins are characterized by their large size (350 kDa), dynamic subcellular distribution, and potential functions in cell division and differentiation. The current data suggest that CMF1 is a unique member of this family by virtue of its restricted protein expression and variant subcellular distribution. Immunochemical analysis demonstrates that CMF1 protein is expressed in cardiogenic cells prior to the activation of cardiac structural gene products. In addition, we show that expression of CMF1 is not dependent on the bone morphogenetic protein (BMP) signaling pathway during development. Still, CMF1 cannot direct cardiomyogenesis in the absence of such factors as NKX-2.5. Taken with our previous data, this study suggests that CMF1 is a BMP-independent component of the cardiomyogenic pathway.</description><identifier>ISSN: 0021-9258</identifier><identifier>EISSN: 1083-351X</identifier><identifier>DOI: 10.1074/jbc.M000518200</identifier><identifier>PMID: 10747923</identifier><language>eng</language><publisher>United States: Elsevier Inc</publisher><subject>Amino Acid Sequence ; Animals ; Avian Proteins ; Bone Morphogenetic Proteins - physiology ; Cell Differentiation ; Cell Division ; Chick Embryo ; Chickens - genetics ; Chromosomal Proteins, Non-Histone - genetics ; Cloning, Molecular ; Embryo, Nonmammalian - physiology ; Embryonic Induction ; Gene Expression Regulation, Developmental ; Heart - embryology ; Microfilament Proteins ; Molecular Sequence Data ; Muscle Proteins - chemistry ; Muscle Proteins - genetics ; Muscle Proteins - metabolism ; Quail ; Restriction Mapping</subject><ispartof>The Journal of biological chemistry, 2000-07, Vol.275 (28), p.21453-21459</ispartof><rights>2000 © 2000 ASBMB. 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In the present study, we show that CMF1 is a member of an emerging family of proteins that includes centromeric protein-F, mitosin, and LEK1. These proteins are characterized by their large size (350 kDa), dynamic subcellular distribution, and potential functions in cell division and differentiation. The current data suggest that CMF1 is a unique member of this family by virtue of its restricted protein expression and variant subcellular distribution. Immunochemical analysis demonstrates that CMF1 protein is expressed in cardiogenic cells prior to the activation of cardiac structural gene products. In addition, we show that expression of CMF1 is not dependent on the bone morphogenetic protein (BMP) signaling pathway during development. Still, CMF1 cannot direct cardiomyogenesis in the absence of such factors as NKX-2.5. Taken with our previous data, this study suggests that CMF1 is a BMP-independent component of the cardiomyogenic pathway.</description><subject>Amino Acid Sequence</subject><subject>Animals</subject><subject>Avian Proteins</subject><subject>Bone Morphogenetic Proteins - physiology</subject><subject>Cell Differentiation</subject><subject>Cell Division</subject><subject>Chick Embryo</subject><subject>Chickens - genetics</subject><subject>Chromosomal Proteins, Non-Histone - genetics</subject><subject>Cloning, Molecular</subject><subject>Embryo, Nonmammalian - physiology</subject><subject>Embryonic Induction</subject><subject>Gene Expression Regulation, Developmental</subject><subject>Heart - embryology</subject><subject>Microfilament Proteins</subject><subject>Molecular Sequence Data</subject><subject>Muscle Proteins - chemistry</subject><subject>Muscle Proteins - genetics</subject><subject>Muscle Proteins - metabolism</subject><subject>Quail</subject><subject>Restriction Mapping</subject><issn>0021-9258</issn><issn>1083-351X</issn><fulltext>true</fulltext><rsrctype>article</rsrctype><creationdate>2000</creationdate><recordtype>article</recordtype><sourceid>EIF</sourceid><recordid>eNp1kEtLxDAUhYMoOo5uXUoWbjveJH0ux-ILZlBEwV1I09tpBtuUtDrMvzelgm7cJFl83yHnEHLBYMEgCa-3hV6sASBiKQc4IDMGqQhExN4PyQyAsyDjUXpCTvt-6zEIM3ZMTkY1ybiYEbNs1ce-Nz21Fc3Xd4y-4Beqj54qemNbpGvrutpusMXBaPrs7ICmDUxbYof-aAea26bzpH_5iKFGmitXGtvsR2t01FDv1P6MHFU-F89_7jl5u7t9zR-C1dP9Y75cBVok6RAUsYAqrjQvdcyigitVZKBZKMoIQGDCFGOFCFXM0yLUSiBCFcYZVL6OTngk5mQx5Wpn-95hJTtnGuX2koEci0u_mfzdzAuXk9B9Fg2Wf_BpJA9cTUBtNvXOOJSFsbrGRvIkkjyVnIXRiKUThr7dl0Ene22w1Vh6RQ-ytOa_L3wD1jmGrg</recordid><startdate>20000714</startdate><enddate>20000714</enddate><creator>Pabón-Peña, Lil M.</creator><creator>Goodwin, Richard L.</creator><creator>Cise, Linda J.</creator><creator>Bader, David</creator><general>Elsevier Inc</general><general>American Society for Biochemistry and Molecular Biology</general><scope>6I.</scope><scope>AAFTH</scope><scope>CGR</scope><scope>CUY</scope><scope>CVF</scope><scope>ECM</scope><scope>EIF</scope><scope>NPM</scope><scope>AAYXX</scope><scope>CITATION</scope></search><sort><creationdate>20000714</creationdate><title>Analysis of CMF1 Reveals a Bone Morphogenetic Protein-independent Component of the Cardiomyogenic Pathway</title><author>Pabón-Peña, Lil M. ; Goodwin, Richard L. ; Cise, Linda J. ; Bader, David</author></sort><facets><frbrtype>5</frbrtype><frbrgroupid>cdi_FETCH-LOGICAL-c378t-b630f6fc2dc615b2aab90c143d5003e71a11b34a628b4ca3ee0f4690f923c7253</frbrgroupid><rsrctype>articles</rsrctype><prefilter>articles</prefilter><language>eng</language><creationdate>2000</creationdate><topic>Amino Acid Sequence</topic><topic>Animals</topic><topic>Avian Proteins</topic><topic>Bone Morphogenetic Proteins - physiology</topic><topic>Cell Differentiation</topic><topic>Cell Division</topic><topic>Chick Embryo</topic><topic>Chickens - genetics</topic><topic>Chromosomal Proteins, Non-Histone - genetics</topic><topic>Cloning, Molecular</topic><topic>Embryo, Nonmammalian - physiology</topic><topic>Embryonic Induction</topic><topic>Gene Expression Regulation, Developmental</topic><topic>Heart - embryology</topic><topic>Microfilament Proteins</topic><topic>Molecular Sequence Data</topic><topic>Muscle Proteins - chemistry</topic><topic>Muscle Proteins - genetics</topic><topic>Muscle Proteins - metabolism</topic><topic>Quail</topic><topic>Restriction Mapping</topic><toplevel>peer_reviewed</toplevel><toplevel>online_resources</toplevel><creatorcontrib>Pabón-Peña, Lil M.</creatorcontrib><creatorcontrib>Goodwin, Richard L.</creatorcontrib><creatorcontrib>Cise, Linda J.</creatorcontrib><creatorcontrib>Bader, David</creatorcontrib><collection>ScienceDirect Open Access Titles</collection><collection>Elsevier:ScienceDirect:Open Access</collection><collection>Medline</collection><collection>MEDLINE</collection><collection>MEDLINE (Ovid)</collection><collection>MEDLINE</collection><collection>MEDLINE</collection><collection>PubMed</collection><collection>CrossRef</collection><jtitle>The Journal of biological chemistry</jtitle></facets><delivery><delcategory>Remote Search Resource</delcategory><fulltext>fulltext</fulltext></delivery><addata><au>Pabón-Peña, Lil M.</au><au>Goodwin, Richard L.</au><au>Cise, Linda J.</au><au>Bader, David</au><format>journal</format><genre>article</genre><ristype>JOUR</ristype><atitle>Analysis of CMF1 Reveals a Bone Morphogenetic Protein-independent Component of the Cardiomyogenic Pathway</atitle><jtitle>The Journal of biological chemistry</jtitle><addtitle>J Biol Chem</addtitle><date>2000-07-14</date><risdate>2000</risdate><volume>275</volume><issue>28</issue><spage>21453</spage><epage>21459</epage><pages>21453-21459</pages><issn>0021-9258</issn><eissn>1083-351X</eissn><abstract>Disruption of the CMF1 function in anterior mesoderm inhibits cardiac myogenesis in avian embryos. In the present study, we show that CMF1 is a member of an emerging family of proteins that includes centromeric protein-F, mitosin, and LEK1. These proteins are characterized by their large size (350 kDa), dynamic subcellular distribution, and potential functions in cell division and differentiation. The current data suggest that CMF1 is a unique member of this family by virtue of its restricted protein expression and variant subcellular distribution. Immunochemical analysis demonstrates that CMF1 protein is expressed in cardiogenic cells prior to the activation of cardiac structural gene products. In addition, we show that expression of CMF1 is not dependent on the bone morphogenetic protein (BMP) signaling pathway during development. Still, CMF1 cannot direct cardiomyogenesis in the absence of such factors as NKX-2.5. Taken with our previous data, this study suggests that CMF1 is a BMP-independent component of the cardiomyogenic pathway.</abstract><cop>United States</cop><pub>Elsevier Inc</pub><pmid>10747923</pmid><doi>10.1074/jbc.M000518200</doi><tpages>7</tpages><oa>free_for_read</oa></addata></record> |
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subjects | Amino Acid Sequence Animals Avian Proteins Bone Morphogenetic Proteins - physiology Cell Differentiation Cell Division Chick Embryo Chickens - genetics Chromosomal Proteins, Non-Histone - genetics Cloning, Molecular Embryo, Nonmammalian - physiology Embryonic Induction Gene Expression Regulation, Developmental Heart - embryology Microfilament Proteins Molecular Sequence Data Muscle Proteins - chemistry Muscle Proteins - genetics Muscle Proteins - metabolism Quail Restriction Mapping |
title | Analysis of CMF1 Reveals a Bone Morphogenetic Protein-independent Component of the Cardiomyogenic Pathway |
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