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J. Biol. Chem., Vol. 266, Issue 24, 15705-15709, 08, 1991
P Grondin, M Plantavid, C Sultan, M Breton, G Mauco and H Chap
Phosphatidylinositol (PtdIns)-4- and -3-kinases, PtdIns(4)P-5-kinase,
diacylglycerol (DAG) kinase, and PtdIns-phospholipase C were all detected
in cytoskeletons of resting human platelets. The total cytoskeletal enzyme
activities were greatly increased upon thrombin stimulation of the intact
cells. Those reached a maximum after a 60-s stimulation for
PtdIns(4)P-5-kinase and phospholipase C, while the other kinases appeared
to be slightly delayed. Specific activities were stimulated from about
4-fold (PtdIns-3-kinase) to about 6-fold (PtdIns- 4-kinase). Thrombin
treatment also promoted a co-extraction of pp60c- src with the
cytoskeletons and its disappearance from the Triton X-100 soluble fraction.
These results suggest that stimulation of platelets by thrombin causes the
association of enzymes responsible for lipid phosphorylation and hydrolysis
with the cytoskeletons. This could occur at cytoskeleton anchoring points
to the membranes.
Interaction of pp60c-src, phospholipase C, inositol-lipid, and diacyglycerol kinases with the cytoskeletons of thrombin-stimulated platelets
Institut National de la Sante et de la Recherche Medicale, Unite 326, Hopital Purpan, Toulouse, France.
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