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Platelet activating factor (PAF‐acether) promotes an early degradation of phosphatidylinositol‐4,5‐biphosphate in rabbit platelets
Author(s) -
Mauco Gérard,
Hugues Chap,
Louis Douste-Blazy
Publication year - 1983
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(83)80643-7
Subject(s) - phosphatidic acid , phosphatidylinositol , platelet , chemistry , platelet activating factor , phospholipase c , incubation , cytosol , biochemistry , phosphatidylinositol 4,5 bisphosphate , stimulation , phosphomonoesterase , phospholipase , platelet activation , phospholipid , phospholipase d , receptor , endocrinology , enzyme , biology , signal transduction , immunology , phosphatase , membrane
32 P‐Labelled washed rabbit platelets were incubated with 0.6 nM platelet activating factor (PAF‐acether), giving a full aggregation and release response within 30–60 s. The major phospholipid changes observed under these conditions were: (1) An increased labelling of phosphatidic acid (PA) within 10 s and of phosphatidylinositol (MPI) at 30 s, reflecting the activation of the MPI cycle via the cytosolic phospholipase C; (2) an enhancement of phosphatidylinositol‐4‐phosphate (DPI) and phosphatidylinositol‐4,5‐ bis phosphate (TPI) labelling at later incubation times; (3) an early degradation of TPI with a counterbalancing formation of DPI. The latter changes suggest a receptor‐mediated stimulation of TPI‐phosphomonoesterase, the role of which in the mechanism of platelet activation is discussed.