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J. Biol. Chem., Vol. 266, Issue 35, 23554-23557, 12, 1991
C Sultan, M Plantavid, C Bachelot, P Grondin, M Breton, G Mauco, S Levy- Toledano, JP Caen and H Chap
32P-Labeled human platelets were incubated with thrombin (1 unit/ml) for 5
min at 37 degrees C under conditions allowing maximal synthesis of
[32P]phosphatidylinositol 3',4'-bisphosphate (PtdIns(3,4)P2). Incorporation
of 32P into the latter phosphoinositide was dose- dependently reduced (to a
maximal level averaging 60%) by the tetrapeptide RGDS, an inhibitor of
fibrinogen binding to activated glycoprotein IIb-IIIa (alpha IIb-beta 3
integrin). Identical results were obtained with the fibrinogen gamma-chain
dodecapeptide HHLGGAKQAGDV, whereas the tripeptide RGD and the tetrapeptide
RGES displayed reduced or undetectable effects on 32P labeling of
PtdIns(3,4)P2, respectively, in good correlation with their ability to
inhibit platelet aggregation and fibrinogen binding to activated alpha
IIb-beta 3 integrin. In addition, pathological platelets from three
patients suffering thrombasthenia, which lack alpha IIb-beta 3 integrin and
fail to aggregate in response to thrombin, displayed hardly detectable
increases in the 32P labeling of PtdIns(3,4)P2. In contrast,
thrombin-stimulated synthesis of PtdIns(3,4)P2 was unaltered in other
deficient platelets lacking the glycoprotein Ib-IX complex (Bernard-
Soulier syndrome). Although additional pathways seem to be involved in the
regulation of phosphatidylinositol-3-kinase, these data indicate a strong
relationship between platelet aggregation involving fibrinogen binding to
activated alpha IIb-beta 3 integrin and the synthesis of the novel
phosphoinositides phosphorylated at position D-3 of the inositol ring.
Involvement of platelet glycoprotein IIb-IIIa (alpha IIb-beta 3 integrin) in thrombin-induced synthesis of phosphatidylinositol 3',4'- bisphosphate
Institut National de la Sante et de la Recherche Medicale, Unite 326, Hopital Purpan, Toulouse, France.
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