alphaIIb beta 3-integrin mediated adhesion of human platelets to a fibrinogen matrix triggers phospholipase C activation and phosphatidylinositol 3',4'-biphosphate accumulation.
FEBS Lett
; 389(3): 253-6, 1996 Jul 08.
Article
en En
| MEDLINE
| ID: mdl-8766710
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.
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Banco de datos:
MEDLINE
Asunto principal:
Fosfolipasas de Tipo C
/
Plaquetas
/
Fibrinógeno
/
Adhesividad Plaquetaria
/
Fosfatos de Fosfatidilinositol
/
Complejo GPIIb-IIIa de Glicoproteína Plaquetaria
Límite:
Humans
Idioma:
En
Año:
1996
Tipo del documento:
Article