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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
35
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pubmed:dateCreated |
1994-1-13
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pubmed:abstractText |
Angiotensin II is a potent growth factor for vascular smooth muscle cells and shares many signal transduction mechanisms with mitogens, including stimulation of mitogen-activated protein (MAP) kinases and protein tyrosine phosphorylation. Regulation of tyrosine phosphorylation involves both protein-tyrosine kinases and protein-tyrosine phosphatases (PTPases). To investigate the role of PTPases in angiotensin II-mediated events, we studied the expression of a transcriptionally regulated PTPase, 3CH134, which has selective activity toward MAP kinase. Angiotensin II rapidly induced 3CH134 mRNA (30 min maximum) in a concentration-dependent manner (100 nM maximum). Platelet-derived growth factor, alpha-thrombin, hydrogen peroxide, phorbol 12-myristate 13-acetate, and ionomycin also induced 3CH134 but to levels lower than angiotensin II. Induction of 3CH134 by angiotensin II was partially inhibited after down-regulating protein kinase C but was fully inhibited after chelating intracellular Ca2+. Treatment with both phorbol 12-myristate 13-acetate and ionomycin induced 3CH134 mRNA to levels seen with angiotensin II, indicating that Ca2+ mobilization and protein kinase C activation can act synergistically to induce 3CH134. Angiotensin II stimulated 3CH134 protein synthesis after 1 h as measured by immunoprecipitation of 3CH134 from [35S]methionine-labeled cells using affinity-purified antibodies. These results establish 3CH134 as a dynamically regulated, immediate early gene in vascular smooth muscle cells and suggest a role for PTPases in regulating angiotensin II-stimulated events mediated by MAP kinases and tyrosine kinases.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
IM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Angiotensin II,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Cycle Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Dual Specificity Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Immediate-Early Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphoprotein Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Kinase C,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Phosphatase 1,
http://linkedlifedata.com/resource/pubmed/chemical/Protein Tyrosine Phosphatases,
http://linkedlifedata.com/resource/pubmed/chemical/RNA, Messenger
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pubmed:status |
MEDLINE
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pubmed:month |
Dec
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pubmed:issn |
0021-9258
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:day |
15
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pubmed:volume |
268
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
26037-40
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pubmed:dateRevised |
2007-11-15
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pubmed:meshHeading |
pubmed-meshheading:8253712-Angiotensin II,
pubmed-meshheading:8253712-Animals,
pubmed-meshheading:8253712-Cell Cycle Proteins,
pubmed-meshheading:8253712-Cells, Cultured,
pubmed-meshheading:8253712-Dual Specificity Phosphatase 1,
pubmed-meshheading:8253712-Enzyme Induction,
pubmed-meshheading:8253712-Immediate-Early Proteins,
pubmed-meshheading:8253712-Male,
pubmed-meshheading:8253712-Muscle, Smooth, Vascular,
pubmed-meshheading:8253712-Phosphoprotein Phosphatases,
pubmed-meshheading:8253712-Protein Kinase C,
pubmed-meshheading:8253712-Protein Phosphatase 1,
pubmed-meshheading:8253712-Protein Tyrosine Phosphatases,
pubmed-meshheading:8253712-RNA, Messenger,
pubmed-meshheading:8253712-Rats,
pubmed-meshheading:8253712-Rats, Sprague-Dawley,
pubmed-meshheading:8253712-Signal Transduction
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pubmed:year |
1993
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pubmed:articleTitle |
Angiotensin II induces 3CH134, a protein-tyrosine phosphatase, in vascular smooth muscle cells.
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pubmed:affiliation |
Department of Biochemistry, Emory University School of Medicine, Atlanta, Georgia 30322.
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pubmed:publicationType |
Journal Article
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