pubmed-article:8626602 | rdf:type | pubmed:Citation | lld:pubmed |
pubmed-article:8626602 | lifeskim:mentions | umls-concept:C0003009 | lld:lifeskim |
pubmed-article:8626602 | lifeskim:mentions | umls-concept:C0441655 | lld:lifeskim |
pubmed-article:8626602 | lifeskim:mentions | umls-concept:C2587213 | lld:lifeskim |
pubmed-article:8626602 | pubmed:issue | 17 | lld:pubmed |
pubmed-article:8626602 | pubmed:dateCreated | 1996-6-21 | lld:pubmed |
pubmed-article:8626602 | pubmed:abstractText | Angiotensin II is the major effector peptide of the renin-angiotensin system, and it exerts its physiologic functions via a G protein-coupled cell surface receptor called AT1. We found that in rat aortic smooth muscle cells, angiotensin II stimulated the formation of Ras-GTP, Ras-Raf-1 complex formation, and the tyrosine phosphorylation of two important Ras GTPase-activating proteins (GAPs), p120 Ras-GAP and p190 Rho-GAP. Electroporation of anti-pp60c-src antibody into cultured, adherent smooth muscle cells blocked the angiotensin II stimulation of Ras-GAP and Rho-GAP tyrosine phosphorylation. In contrast electroporation of antibodies against c-Yes or c-Fyn had no effect. Anti-pp60c-src antibody also blocked angiotensin II-stimulated Ras activation and Ras-Raf-1 complex formation. These data strongly suggest that a G protein-coupled receptor such as the AT1 receptor can activate the Ras protein cascade via the tyrosine kinase pp60c-src. | lld:pubmed |
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pubmed-article:8626602 | pubmed:language | eng | lld:pubmed |
pubmed-article:8626602 | pubmed:journal | http://linkedlifedata.com/r... | lld:pubmed |
pubmed-article:8626602 | pubmed:citationSubset | IM | lld:pubmed |
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pubmed-article:8626602 | pubmed:status | MEDLINE | lld:pubmed |
pubmed-article:8626602 | pubmed:month | Apr | lld:pubmed |
pubmed-article:8626602 | pubmed:issn | 0021-9258 | lld:pubmed |
pubmed-article:8626602 | pubmed:author | pubmed-author:ChadTT | lld:pubmed |
pubmed-article:8626602 | pubmed:author | pubmed-author:BernsteinK... | lld:pubmed |
pubmed-article:8626602 | pubmed:author | pubmed-author:SchiefferBB | lld:pubmed |
pubmed-article:8626602 | pubmed:author | pubmed-author:MarreroM BMB | lld:pubmed |
pubmed-article:8626602 | pubmed:author | pubmed-author:PaxtonW GWG | lld:pubmed |
pubmed-article:8626602 | pubmed:issnType | Print | lld:pubmed |
pubmed-article:8626602 | pubmed:day | 26 | lld:pubmed |
pubmed-article:8626602 | pubmed:volume | 271 | lld:pubmed |
pubmed-article:8626602 | pubmed:owner | NLM | lld:pubmed |
pubmed-article:8626602 | pubmed:authorsComplete | Y | lld:pubmed |
pubmed-article:8626602 | pubmed:pagination | 10329-33 | lld:pubmed |
pubmed-article:8626602 | pubmed:dateRevised | 2009-11-19 | lld:pubmed |
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pubmed-article:8626602 | pubmed:year | 1996 | lld:pubmed |
pubmed-article:8626602 | pubmed:articleTitle | Angiotensin II controls p21ras activity via pp60c-src. | lld:pubmed |
pubmed-article:8626602 | pubmed:affiliation | Department of Pathology Center for Molecular and Cellular Signaling, Emory University, Atlanta, Georgia 30322, USA. | lld:pubmed |
pubmed-article:8626602 | pubmed:publicationType | Journal Article | lld:pubmed |
pubmed-article:8626602 | pubmed:publicationType | Research Support, U.S. Gov't, P.H.S. | lld:pubmed |
pubmed-article:8626602 | pubmed:publicationType | Research Support, Non-U.S. Gov't | lld:pubmed |
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