Cloning and characterization of two novel zebrafish P2X receptor subunits

被引：33

作者：

Diaz-Hernandez, M ^{[1
]}

Cox, JA ^{[1
]}

Migita, K ^{[1
]}

Haines, W ^{[1
]}

Egan, TM ^{[1
]}

Voigt, MM ^{[1
]}

机构：

[1] St Louis Univ, Sch Med, Dept Pharmacol & Physiol Sci, St Louis, MO 63104 USA

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 2002年 / 295卷 / 04期

关键词：

ionotropic; receptor; ligand-gated channel; purinoceptor; nucleotide; zebrafish; ATP;

D O I：

10.1016/S0006-291X(02)00760-X

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：

In this report we describe the cloning and characterization of two P2X receptor subunits cloned from the zebrafish (Danio rerio). Primary sequence analysis suggests that one cDNA encodes an ortholog of the mammalian P2X(4) subunit and the second cDNA encodes the ortholog of the mammalian P2X(5) subunit. The zP2X(4) subunit form; a homo-oligomeric receptor that displays a low affinity for ATP (EC50 = 274 +/- 48 muM) and very low affinity (EC50 > 500 muM) for other purinergic ligands such as alphabetameATP, suramin, and PPADS. As seen with the mammalian orthologs, the zP2X(5) subunit forms a homo-oligomeric receptor that yields very small whole-cell currents (<20 pA), making determination of an EC50 problematic. Both subunit genes were physically mapped onto the zebrafish genome using radiation hybrid analysis of the T51 panel, with the zp2x4 localized to LG21 and zp2x5 to LG5. (C) 2002 Elsevier Science (USA). All rights reserved.

引用

页码：849 / 853

页数：5

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