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Vol. 273, Issue 4, 2024-2029, January 23, 1998
From the Acting through cell surface receptors, ADP
activates platelets resulting in shape change, aggregation, thromboxane
A2 production, and release of granule contents. ADP
also causes a number of intracellular events including inhibition of
adenylyl cyclase, mobilization of calcium from intracellular stores,
and rapid calcium influx in platelets. However, the receptors that
transduce these events remain unidentified and their molecular
mechanisms of action have not been elucidated. The receptor responsible
for the actions of ADP on platelets has been designated the P2T
receptor. In this study we have used ARL 66096, a potent antagonist of
ADP-induced platelet aggregation, and a P2X ionotropic receptor
agonist,
Molecular Basis for ADP-induced Platelet Activation
I. EVIDENCE FOR THREE DISTINCT ADP RECEPTORS ON HUMAN
PLATELETS
§,,§,§, and Departments of Pharmacology,
¶ Physiology, and § Sol Sherry Thrombosis Research
Center, Temple University Medical School,
Philadelphia, Pennsylvania 19150
,
-methylene adenosine 5
-triphosphate, to distinguish
the ADP-induced intracellular events. ARL 66096 blocked ADP-induced
inhibition of adenylyl cyclase, but did not affect ADP-mediated
intracellular calcium increases or shape change. Both ADP and
2-methylthio-ADP caused a 3-fold increase in the level of inositol
1,4,5-trisphosphate over control levels which peaked in a similar
fashion to the Ca2+ transient. The increase in inositol
1,3,4-trisphosphate was of similar magnitude to that of inositol
1,4,5-trisphosphate. ,-Methylene adenosine 5-triphosphate did
not cause an increase in either of the inositol trisphosphates. These
results clearly demonstrate the presence of two distinct platelet ADP
receptors in addition to the P2X receptor: one coupled to adenylyl
cyclase and the other coupled to mobilization of calcium from
intracellular stores through inositol trisphosphates.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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