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• W2102292568 abstract "Thrombin activation of human platelets is accompanied by tyrosine phosphorylation of many cellular proteins, as well as changes in the cytosolic Ca2+ concentration. Consequently, we assessed tyrosine phosphorylation of the platelet inositol 1,4,5-trisphosphate receptor (IP(3)R) to determine if phosphorylation modulates Ca2+ release from internal stores. Stimulation of platelets with thrombin resulted in tyrosine phosphorylation of the type 1 IP(3)R, which peaked at 3 min followed by dephosphorylation to the basal level by 10 min. Thrombin also increased the extent of IP(3)R-mediated Ca2+ release 1.6-fold in crude platelet membranes isolated from thrombin-stimulated (3 min) platelets. Since we have previously shown that the plasma membrane Ca2+-ATPase (PMCA) is also phosphorylated on tyrosine residues during thrombin-stimulated platelet activation, resulting in inhibition of the pump (Dean et al., J Biol Chem 1997; 272: 15113-9), the present results suggest that early in thrombin-stimulated platelet activation, tyrosine phosphorylation of PMCA and IP(3)R results in transient enhancement in platelet cytosolic Ca2+, but that this enhancement is attenuated by subsequent dephosphorylation." @default.
• W2102292568 created "2016-06-24" @default.
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• W2102292568 date "1999-01-01" @default.
• W2102292568 modified "2023-09-27" @default.
• W2102292568 title "Role of tyrosine phosphorylation in regulation of inositol 1,4,5-trisphosphate-mediated Ca 2+ release in human platelets" @default.
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• W2102292568 doi "https://doi.org/10.1080/09537109975898" @default.
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