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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
1
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pubmed:dateCreated |
1990-5-25
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pubmed:abstractText |
The involvement of Ca2+ and PGE1 in myoblast fusion has been well documented. Extracellular Ca2+ is essential for myoblast adhesion, alignment, and fusion. There is an obligatory increase in Ca2+ influx immediately preceding fusion and the Ca2+ ionophore A23187 promotes precocious fusion. PGE1 receptors appear just prior to fusion, and an antagonist of PGE1 binding to cell surface receptors blocks fusion when added prior to Ca2+ influx. Finally, exogenous PGE1 induces precocious fusion. The present study was an initial test of the hypothesis that membrane protein phosphorylation by protein kinase C (PKC) links PGE1 receptor occupancy and the increase in Ca2+ influx. Our conclusion that PKC is an essential component in the regulation of myoblast fusion is based in part on the following evidence: (1) an activator of PKC, the tumor promoter 12-O-tetradecanoylphorbol-13-acetate (TPA), at low concentration and for a brief exposure period, induces precocious fusion and stimulates Ca2+ influx; (2) 4 alpha-phorbol-12,13-didecanoate, an inactive analog of TPA, has no discernible effect on fusion or Ca2+ influx; (3) 1-oleoyl-2-acetyl glycerol, an analog of endogenous diacylglycerol (DAG) which activates PKC, promotes precocious fusion, as does the DAG kinase inhibitor R59022 (6-[2-[4-[(4-fluorophenyl)phenylmethylene]-1-piperidinyl]ethyl]-7- methyl-5H-thiazole-[3,2 alpha]-pyrimidin-5-one) which raises the level of endogenous DAG by inhibiting its catabolism; (4) 1-(5-isoquinolinesulfonyl)-2-methylpiperazine (H-7), a highly potent PKC inhibitor, reversibly blocks myogenesis at a point between alignment and fusion; and (5) H-7 also blocks the normal increase in Ca2+ influx preceding fusion.
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pubmed:grant | |
pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/1-(5-Isoquinolinesulfonyl)-2-Methylp...,
http://linkedlifedata.com/resource/pubmed/chemical/1-oleoyl-2-acetylglycerol,
http://linkedlifedata.com/resource/pubmed/chemical/Alprostadil,
http://linkedlifedata.com/resource/pubmed/chemical/Calcium,
http://linkedlifedata.com/resource/pubmed/chemical/Diglycerides,
http://linkedlifedata.com/resource/pubmed/chemical/Isoquinolines,
http://linkedlifedata.com/resource/pubmed/chemical/Piperazines,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinases,
http://linkedlifedata.com/resource/pubmed/chemical/Pyrimidinones,
http://linkedlifedata.com/resource/pubmed/chemical/R 59022,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Thiazoles
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pubmed:status |
MEDLINE
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pubmed:month |
May
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pubmed:issn |
0012-1606
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
139
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
89-99
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pubmed:dateRevised |
2009-11-19
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pubmed:meshHeading |
pubmed-meshheading:2328843-1-(5-Isoquinolinesulfonyl)-2-Methylpiperazine,
pubmed-meshheading:2328843-Alprostadil,
pubmed-meshheading:2328843-Animals,
pubmed-meshheading:2328843-Calcium,
pubmed-meshheading:2328843-Cell Fusion,
pubmed-meshheading:2328843-Chick Embryo,
pubmed-meshheading:2328843-Diglycerides,
pubmed-meshheading:2328843-Enzyme Activation,
pubmed-meshheading:2328843-Isoquinolines,
pubmed-meshheading:2328843-Muscles,
pubmed-meshheading:2328843-Piperazines,
pubmed-meshheading:2328843-Protein Kinase C,
pubmed-meshheading:2328843-Protein Kinases,
pubmed-meshheading:2328843-Pyrimidinones,
pubmed-meshheading:2328843-Tetradecanoylphorbol Acetate,
pubmed-meshheading:2328843-Thiazoles
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pubmed:year |
1990
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pubmed:articleTitle |
Role of protein kinase C in chick embryo skeletal myoblast fusion.
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pubmed:affiliation |
Division of Biological Sciences, University of Missouri, Columbia 65211.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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