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J Biol Chem, Vol. 273, Issue 19, 11544-11547, May 8, 1998
From the Department of Thrombosis and Vascular Biology, Maryland
Research Laboratories, Otsuka America Pharmaceutical, Inc.,
Rockville, Maryland 20850
ADP is an important physiological platelet
agonist. The molecular identity of the ADP receptor(s) in human
platelets, however, is still unclear. Although P2T purinoceptor was
believed to be the ligand-gated cation channel for ADP in human
platelets, recent patch clamp studies now suggest it is
P2X1 type. In the present study, we have cloned a
cDNA encoding a P2X1 purinoceptor from human platelets
using degenerate reverse transcription and polymerase chain reaction.
Northern blotting with a P2X1-specific probe revealed a
band of 1.8 kilobases in human platelets as well as in several megakaryoblastic cell lines. 1321N1 human astrocytoma cells expressing the cloned P2X1 cDNA exhibited both ATP- and
ADP-stimulated Ca2+ influx that could be blocked by the
purinoceptor antagonist pyridoxalphosphate-6-azophenyl-2',4'-disulfonic acid and suramin. Additionally, a polyclonal antibody raised against glutathione-S-transferase-P2X1 fusion peptide
reacted with a 70-kDa band on Western blot of human platelets. It is
therefore concluded that functional P2X1 purinoceptors are
present in human platelets.
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