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- W2057100306 abstract "Angiotensin II induces the rapid temporal tyrosine phosphorylation and activation of phospholipase C-γ1 (PLC-γ1) and the elevation of intracellular calcium levels. To investigate the relationship of these intracellular signaling events, rat aortic smooth muscle cells were treated with the calcium chelator BAPTA-AM, the calcium channel blocker verapamil, the intracellular calcium antagonist TMB-8, and the calcium ionophore ionomycin. The effects of these agents on PLC-γ1 tyrosine phosphorylation were then measured. We found that treatment of these cells with the calcium inhibitors augmented the basal level of PLC-γ1 tyrosine phosphorylation, without changing the peak level of tyrosine phosphorylation induced by angiotensin II. The rapid dephosphorylation of PLC-γ1 that follows angiotensin II stimulation was prevented by these calcium antagonists. In contrast, angiotensin II-induced tyrosine phosphorylation of PLC-γ1 was inhibited by ionomycin. These results suggest that the angiotensin II-induced tyrosine phosphorylation of PLC-γ1 is calcium-independent, while the dephosphorylation is calcium-dependent." @default.
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- W2057100306 date "1997-03-01" @default.
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- W2057100306 title "Role of Intracellular Calcium in the Angiotensin II-Mediated Tyrosine Phosphorylation and Dephosphorylation of PLC-γ1" @default.
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- W2057100306 doi "https://doi.org/10.1006/bbrc.1997.6322" @default.
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