Identification of a P2X1 purinoceptor expressed on human platelets

被引:39
作者
Scase, TJ
Heath, MF
Allen, JM
Sage, SO
Evans, RJ
机构
[1] Univ Cambridge, Ctr Vet Sci, Cambridge CB3 0ES, England
[2] Univ Glasgow, Inst Biomed & Life Sci, Div Biochem & Mol Biol, Glasgow G12 8QQ, Lanark, Scotland
[3] Univ Cambridge, Dept Physiol, Cambridge CB2 3EG, England
基金
英国惠康基金;
关键词
D O I
10.1006/bbrc.1997.8001
中图分类号
Q5 [生物化学]; Q7 [分子生物学];
学科分类号
071010 ; 081704 ;
摘要
It has been proposed that platelets possess a P-2X1-purinoceptor-like ligand-gated cation channel, through which Ca2+ enters platelets from the extracellular medium upon ADP or ATP stimulation. In this paper we describe the cloning of human P-2X1-specific cDNA from human platelets, K562 and human erythroleukaemic cell lines. Sequence analyses of these cDNAs show 100% nucleotide sequence identity with that of human P-2X1 cloned from urinary bladder. Western blotting of platelet lysates separated by SDS-PAGE and probed with anti-P-2X1 IgG shows the expected protein with a molecular mass of 60kDa and a second protein of 45kDa. These data confirm that platelets possess at least two distinct purinoceptors: a P-2T purinoceptor which mediates platelet aggregation, inhibition of adenylate cyclase, and release of intracellular Ca2+ stores and a platelet P-2X1, purinoceptor which upon ATP and ADP stimulation mediates the rapid entry of extracellular Ca2+ into platelets. (C) 1998 Academic Press.
引用
收藏
页码:525 / 528
页数:4
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