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• W1857477498 startingPage "925" @default.
• W1857477498 abstract "We showed previously that direct platelet activation by collagen involves an increase in the platelet cytosolic free Ca2+ concentration ([Ca2+]i) but that this increase is not required for the adhesion of platelets to collagen. We now report that collagen-induced arachidonic acid liberation, myosin phosphorylation and 5-hydroxytryptamine secretion are dependent on increases in [Ca2+]i, as they were markedly inhibited in platelets loaded with the acetoxymethyl ester of the Ca2+ chelator BAPTA but not in cells loaded with the acetoxymethyl ester of the non-chelating diazo-3. BAPTA also partially inhibited the rate of collagen-induced phosphatidic acid (PtdA) formation but had little effect on increases in phosphorylation of pleckstrin (47 kDa protein; P47). From these results we infer that collagen-induced increases in [Ca2+]i are required for dense granule secretion and arachidonic acid liberation, but are not necessary for stimulation of the protein kinase C pathway." @default.
• W1857477498 created "2016-06-24" @default.
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• W1857477498 date "1992-12-15" @default.
• W1857477498 modified "2023-10-16" @default.
• W1857477498 title "Cytosolic calcium as a second messenger for collagen-induced platelet responses" @default.
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• W1857477498 doi "https://doi.org/10.1042/bj2880925" @default.
• W1857477498 hasPubMedCentralId "https://www.ncbi.nlm.nih.gov/pmc/articles/1131975" @default.
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