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- W2946822116 abstract "The inhibition of platelet function by PGE1, which is mediated by cyclic AMP, is associated with an increased phosphorylation of a 24,000 dalton platelet polypeptide (P24) (Haslam et al. (1979) Biochem J. 178, 397). The significance of this phosphorylation reaction has been investigated. Washed human platelets that had been labelled with 32P were I incubated with 2 μM PGE1 for 2min, sonicated and separated into subcellular fractions by differential centrifugation. Analysis of the phosphopolypeptides present in these fractions by SDS-polyacrylamide gel electrophoresis showed that P24 was enriched in a 19,000- 90,000 g fraction that contained both plasma and intracellular membranes and accumulated 45Ca2+ by an ATP-dependent, oxalate-stimulated process. Uptake of 45Ca2+ by membranes from PGE1-treated platelets was significantly greater (approx. 50%) than by membranes from control platelets. When the former membranes were loaded with 45Ca2+ in the presence of oxalate and centrifuged througll a discontinuous sucrose density gradient, thre membrane fractions were obtained. Enrichment of both 45Ca2+ and P24 was greatest in the most dense of these. Since platelet responses to aggregating agents are believed to be mediated by Ca2+ ions, we suggest that PGE1 may inhibit these processes by causing the cyclic AMP-dependent phosphorylation of the membrane-bound P24 which then stimulates the active transport of Ca2+ ions out of the platelet cytosol." @default.
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- W2946822116 date "1979-01-01" @default.
- W2946822116 modified "2023-09-29" @default.
- W2946822116 title "Possible Role of a Membrane Phosphopolypeptide in the Inhibition of Platelet Function by Cyclic Amp" @default.
- W2946822116 doi "https://doi.org/10.1055/s-0039-1684459" @default.
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