alphaIIb beta 3-integrin mediated adhesion of human platelets to a fibrinogen matrix triggers phospholipase C activation and phosphatidylinositol 3',4'-biphosphate accumulation.

Abstract:

:This study focused on the variations in phosphoinositide metabolism depending upon alphaIIbbeta3-integrin/fibrinogen interaction without previous activation of platelet agonist receptors. We found that adhesion of resting human platelets to immobilized fibrinogen stimulates phosphatidic acid production and a concomitant decrease in phosphatidylinositol 4',5'-bisphosphate. These results, and the absence of a transphosphatidylation reaction, argue in favor of the activation of a phospholipase C. Moreover, we observed the accumulation of phosphatidylinositol 3',4'-bisphosphate in adherent platelets as a consequence of the activation of a phosphatidylinositol 3-kinase. This effect was inhibited by ADP scavengers. Our results demonstrate that in adherent platelets, whereas phosphatidylinositol 3-kinase activation is controlled by both alphaIIbbeta-integrin engagement and released ADP, phospholipase C stimulation is triggered only by alphaIIbbeta-integrin/fibrinogen interaction.

journal_name

FEBS Lett

journal_title

FEBS letters

authors

Gironcel D,Racaud-Sultan C,Payrastre B,Haricot M,Borchert G,Kieffer N,Breton M,Chap H

doi

10.1016/0014-5793(96)00595-9

subject

Has Abstract

pub_date

1996-07-08 00:00:00

pages

253-6

issue

3

eissn

0014-5793

issn

1873-3468

pii

0014579396005959

journal_volume

389

pub_type

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