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Blood, Vol. 94 No. 12 (December 15), 1999:
pp. 4156-4165
A Key Role of Adenosine Diphosphate in the Irreversible Platelet
Aggregation Induced by the PAR1-Activating Peptide Through the Late
Activation of Phosphoinositide 3-Kinase
Catherine Trumel,
Bernard Payrastre,
Monique Plantavid,
Béatrice Hechler,
Cécile Viala,
Peter Presek,
Elizabeth A. Martinson,
Jean-Pierre Cazenave,
Hugues Chap, and
Christian Gachet
From Institut Fédératif de Recherche en Immunologie
Cellulaire et Moléculaire, INSERM U 326, Hôpital Purpan,
Toulouse, France; INSERM U 311, ETS, Strasbourg, France; and
Rudolf-Buchheim-Institut für Pharmakologie, Giessen, Germany.
Although adenosine diphosphate (ADP), per se, is a weak platelet
agonist, its role as a crucial cofactor in human blood platelet functions has now been clearly demonstrated in vitro and in vivo. The
molecular basis of the ADP-induced platelet activation is starting to
be understood since the discovery that 2 separate P2 purinergic
receptors may be involved simultaneously in the activation process.
However, little is known about how ADP plays its role as a cofactor in
platelet activation and which signaling pathway initiated by a specific
agonist can be modulated by the released ADP. To investigate these
points, we took advantage of a model of platelet activation through the
thrombin receptor PAR1 in which both ADP scavengers and
phosphoinositide 3-kinase (PI 3-kinase) inhibitors have been shown to
transform the classical irreversible aggregation into a reversible one.
We have observed that, among the different PI 3-kinase products, the
accumulation of phosphatidylinositol 3,4-bisphosphate
[PtdIns(3,4)P2] was dramatically and specifically
attenuated when ADP was removed by apyrase treatment. A comparison
between the effects of PI 3-kinase inhibitors and apyrase strongly
suggest that the late, ADP-dependent, PtdIns(3,4)P2 accumulation is necessary for PAR1-induced irreversible aggregation. Using selective antagonists, we found that the effect of ADP was due to
the ADP receptor coupled to inhibition of adenylyl cyclase. Finally, we
found that both ADP and PI 3-kinase play an important role in
PAR1-dependent reorganization of the cytoskeleton through a control of
myosin heavy chain translocation and the stable association of
signaling complexes with the actin cytoskeleton.
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