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- W1989226644 abstract "In cultured rat vascular smooth muscle cells, angiotensin II (Ang II) induced a rapid increase in mitogen-activated protein kinase (MAPK) activity through the Ang II type 1 receptor, which was insensitive to pertussis toxin but was abolished by the phospholipase C inhibitor, U73122. The Ang II-induced MAPK activation was not affected by the protein kinase C inhibitor, GF109203X, and was only partially impaired by pretreatment with a phorbol ester, whereas both treatments completely prevented MAPK activation by the phorbol ester. Intracellular Ca<sup>2+</sup> chelation by TMB-8, but not extracellular Ca<sup>2+</sup> chelation or inhibition of Ca<sup>2+</sup> influx, abolished Ang II-induced MAPK activation. The calmodulin inhibitor, calmidazolium, and the tyrosine kinase inhibitor, genistein, completely blocked MAPK activation by Ang II as well as by the Ca<sup>2+</sup> ionophore A23187. Ang II caused a rapid increase in the binding of GTP to p21<sup>ras</sup>, and this was inhibited by genistein, TMB-8, and calmidazolium but not by pertussis toxin or GF109203X. These data suggest that Ang II-induced MAPK activation through the Ang II type 1 receptor could be mediated by p21<sup>ras</sup> activation through a currently unidentified tyrosine kinase that lies downstream of G<sub>q</sub>-coupled Ca<sup>2+</sup>/calmodulin signals." @default.
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- W1989226644 date "1996-06-01" @default.
- W1989226644 modified "2023-10-16" @default.
- W1989226644 title "Identification of an Essential Signaling Cascade for Mitogen-activated Protein Kinase Activation by Angiotensin II in Cultured Rat Vascular Smooth Muscle Cells" @default.
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- W1989226644 doi "https://doi.org/10.1074/jbc.271.24.14169" @default.
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