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- W2175466008 endingPage "H1065" @default.
- W2175466008 startingPage "H1059" @default.
- W2175466008 abstract "In cultured vascular smooth muscle cells (VSMC), angiotensin II (ANG II) stimulated tyrosine phosphorylation of multiple proteins including a 130-kDa protein. This 130-kDa protein was identified as a Crk-associated substrate, p130 Cas . ANG II-stimulated tyrosine phosphorylation of p130 Cas was rapid, concentration dependent, and inhibited by the AT 1 -receptor antagonist CV-11974. Neither downregulation of protein kinase C by long exposure of cells to phorbol 12,13-dibutyrate nor blockade of Ca 2+ mobilization by 1,2-bis(2-aminophenoxy)ethane- N, N, N′, N′-tetraacetic acid acetoxymethyl ester had an effect on ANG II-stimulated tyrosine phosphorylation of p130 Cas . Stimulation with ANG II enhanced the specific association of p130 Cas with c-Crk II. The time course of the association of p130 Cas and c-Crk II was similar to that of tyrosine phosphorylation of p130 Cas . c-Crk II was also tyrosine phosphorylated in response to ANG II. These results indicate that ANG II induces tyrosine phosphorylation of p130 Cas and c-Crk II and their specific association, suggesting a potential role of the p130 Cas -c-Crk II complex in ANG II signal transduction in VSMC." @default.
- W2175466008 created "2016-06-24" @default.
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- W2175466008 date "1998-04-01" @default.
- W2175466008 modified "2023-10-17" @default.
- W2175466008 title "Tyrosine phosphorylation and association of p130<sup>Cas</sup>and c-Crk II by ANG II in vascular smooth muscle cells" @default.
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- W2175466008 doi "https://doi.org/10.1152/ajpheart.1998.274.4.h1059" @default.
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