Title : Comparison of the modes of action of Ca2+ ionophore A23187 and thrombin in protein kinase C activation in human platelets.

Pub. Date : 1985 Nov 11

PMID : 3932095






6 Functional Relationships(s)
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1 In human platelets, the Ca2+ ionophore A23187 stimulated the phosphorylation of a 40 kDa protein and myosin light chain (MLC) to the same extents as those induced by thrombin, but the doses of A23187 for 40 kDa protein phosphorylation were higher than those for MLC phosphorylation, although the doses of thrombin for both reactions were nearly the same. Calcimycin coagulation factor II, thrombin Homo sapiens
2 In human platelets, the Ca2+ ionophore A23187 stimulated the phosphorylation of a 40 kDa protein and myosin light chain (MLC) to the same extents as those induced by thrombin, but the doses of A23187 for 40 kDa protein phosphorylation were higher than those for MLC phosphorylation, although the doses of thrombin for both reactions were nearly the same. Calcimycin coagulation factor II, thrombin Homo sapiens
3 However, the sites of the 40 kDa protein phosphorylated by the action of A23187 and thrombin were identical, and the 40 kDa protein phosphorylation induced by A23187 and thrombin was inhibited by tetracaine, an inhibitor for protein kinase C. Neither A23187 nor thrombin induced the production of a catalytic fragment of protein kinase C which might be generated by limited proteolysis with Ca2+-dependent protease. Calcimycin coagulation factor II, thrombin Homo sapiens
4 However, the sites of the 40 kDa protein phosphorylated by the action of A23187 and thrombin were identical, and the 40 kDa protein phosphorylation induced by A23187 and thrombin was inhibited by tetracaine, an inhibitor for protein kinase C. Neither A23187 nor thrombin induced the production of a catalytic fragment of protein kinase C which might be generated by limited proteolysis with Ca2+-dependent protease. Calcimycin coagulation factor II, thrombin Homo sapiens
5 However, the sites of the 40 kDa protein phosphorylated by the action of A23187 and thrombin were identical, and the 40 kDa protein phosphorylation induced by A23187 and thrombin was inhibited by tetracaine, an inhibitor for protein kinase C. Neither A23187 nor thrombin induced the production of a catalytic fragment of protein kinase C which might be generated by limited proteolysis with Ca2+-dependent protease. Calcimycin coagulation factor II, thrombin Homo sapiens
6 However, the sites of the 40 kDa protein phosphorylated by the action of A23187 and thrombin were identical, and the 40 kDa protein phosphorylation induced by A23187 and thrombin was inhibited by tetracaine, an inhibitor for protein kinase C. Neither A23187 nor thrombin induced the production of a catalytic fragment of protein kinase C which might be generated by limited proteolysis with Ca2+-dependent protease. Calcimycin coagulation factor II, thrombin Homo sapiens