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PredicateObject
rdf:type
lifeskim:mentions
pubmed:dateCreated
1993-5-11
pubmed:abstractText
To examine the molecular mechanisms by which mechanical stimuli induce protooncogene expression, we cultured rat neonatal cardiocytes in deformable dishes and imposed an in vitro mechanical load by stretching the adherent cells. Myocyte stretching increased total cell RNA content and mRNA levels of c-fos and skeletal alpha-actin followed by activation of protein synthesis. CAT assay indicated that sequences containing a serum response element were required for efficient transcription of c-fos gene by stretching. This accumulation of c-fos mRNA was suppressed by protein kinase C inhibitors at the transcriptional level and was inhibited markedly by down-regulation of protein kinase C. Moreover, myocyte stretching increased inositol phosphate levels. These findings suggest that mechanical stimuli might directly induce protooncogene expression, possibly, via protein kinase C activation. Furthermore, we observed the activation of mitogen activated protein (MAP) kinase by myocyte stretching. This result suggest that MAP kinase activation might increase the efficiency of protein synthesis in ribosomes induced by mechanical stimuli.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:issn
0300-8428
pubmed:author
pubmed:issnType
Print
pubmed:volume
87 Suppl 2
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
11-8
pubmed:dateRevised
2009-11-19
pubmed:meshHeading
pubmed:year
1992
pubmed:articleTitle
Role of protein kinase system in the signal transduction of stretch-mediated myocyte growth.
pubmed:affiliation
Third Department of Internal Medicine, Faculty of Medicine, University of Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't