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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
18
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pubmed:dateCreated |
1991-7-24
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pubmed:abstractText |
Growth activation of quiescent Swiss 3T3 fibroblasts leads to a rapid induction of vinculin and beta 1-integrin gene expression. Addition of serum, epidermal growth factor (EGF), or platelet-derived growth factor to serum-starved, density-arrested cells resulted in a rapid increase in vinculin and beta 1-integrin mRNA levels and a corresponding increase in vinculin synthesis. The increase in vinculin and beta 1-integrin mRNA expression by serum or EGF was not blocked by the inhibition of protein synthesis by cycloheximide. The kinetics of induction of vinculin and beta 1-integrin mRNAs by EGF are different: vinculin mRNA levels reached a peak of expression 4-5-fold greater than that measured in quiescent cells by 2 h after addition of growth factor, whereas beta 1-integrin mRNA levels increased more slowly and to a lesser extent, reaching peaks of 2-3-fold induction at 5 h poststimulation. Down-regulation of protein kinase C by prolonged pretreatment of cells with phorbol 1,2-myristate 1,3-acetate had no effect on the ability of EGF or platelet-derived growth factor to activate vinculin or beta 1-integrin mRNA expression. Furthermore, direct activation of protein kinase C with 1,2-myristate 1,3-acetate did not induce the expression of vinculin or beta 1-integrin mRNA, but did activate c-fos expression. In vitro nuclear "run-on" transcription assays demonstrate a greater than 7-fold increase in vinculin and beta 1-integrin transcription at 40-60 min after addition of EGF when compared with levels in quiescent cells. This activation was rapid and transient, but appeared to occur later than the increase in c-fos and actin transcription. These results demonstrate that vinculin and beta 1-integrin, important components of the cell adhesion apparatus, are members of a group of immediate early growth-responsive genes, along with c-fos, c-myc, actin, and fibronectin. In addition, regulation of these cell adhesion genes occurs exclusively through a protein kinase C-independent pathway in serum-deprived, density-arrested Swiss 3T3 cells.
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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/Cytoskeletal Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Epidermal Growth Factor,
http://linkedlifedata.com/resource/pubmed/chemical/Integrins,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/RNA,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger,
http://linkedlifedata.com/resource/pubmed/chemical/Tetradecanoylphorbol Acetate,
http://linkedlifedata.com/resource/pubmed/chemical/Vinculin
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pubmed:status |
MEDLINE
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pubmed:month |
Jun
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
25
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pubmed:volume |
266
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
12008-14
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:1711046-Animals,
pubmed-meshheading:1711046-Blotting, Northern,
pubmed-meshheading:1711046-Blotting, Western,
pubmed-meshheading:1711046-Cytoskeletal Proteins,
pubmed-meshheading:1711046-Electrophoresis, Gel, Two-Dimensional,
pubmed-meshheading:1711046-Enzyme Activation,
pubmed-meshheading:1711046-Epidermal Growth Factor,
pubmed-meshheading:1711046-Fibroblasts,
pubmed-meshheading:1711046-Integrins,
pubmed-meshheading:1711046-Mice,
pubmed-meshheading:1711046-Protein Kinase C,
pubmed-meshheading:1711046-RNA,
pubmed-meshheading:1711046-RNA, Messenger,
pubmed-meshheading:1711046-Tetradecanoylphorbol Acetate,
pubmed-meshheading:1711046-Transcription, Genetic,
pubmed-meshheading:1711046-Vinculin
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pubmed:year |
1991
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pubmed:articleTitle |
Epidermal growth factor activation of vinculin and beta 1-integrin gene transcription in quiescent Swiss 3T3 cells. Regulation through a protein kinase C-independent pathway.
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pubmed:affiliation |
Department of Biochemistry, Boston University School of Medicine, Massachusetts.
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pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
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