Cloning, tissue distribution and functional characterization of the chicken P2X1 receptor

• Published in: FEBS letters 2003-01, Vol.533 (1), p.54-58
• Main Authors: Soto, Florentina, Krause, Ulrich, Borchardt, Kerstin, Ruppelt, Anja
• Format: Article
• Language: English
• Subjects: 2MeSATP, 2-methylthio-ATP; Adenosine Triphosphate - pharmacology; Amino Acid Sequence; Animals; ATP receptor; Base Sequence; Chick Embryo; Chickens; Cloning, Molecular; DNA, Complementary - genetics; Humans; Molecular Sequence Data; NF023; NF023, 8,8′-(carbonylbis(imino-3,1-phenylene carbonylimino)bis(1,3,5-naphthalenetrisulfonic) acid); Patch-Clamp Techniques; Perforated patch; PPADS, pyridoxal 5-phosphate 6-azophenyl-2′,4′-disulfonic acid; Purinergic P2 Receptor Agonists; Purinergic P2 Receptor Antagonists; Pyridoxal Phosphate - analogs & derivatives; Pyridoxal Phosphate - pharmacology; Receptors, Purinergic P2 - genetics; Receptors, Purinergic P2 - metabolism; Receptors, Purinergic P2X; Recombinant Proteins - agonists; Recombinant Proteins - antagonists & inhibitors; Recombinant Proteins - genetics; Recombinant Proteins - metabolism; Sequence Homology, Amino Acid; Skeletal muscle; Suramin; Suramin - analogs & derivatives; Suramin - pharmacology; Tissue Distribution; αβmeATP, α,β methylen-ATP
• ISSN: 0014-5793; 1873-3468
• DOI: 10.1016/S0014-5793(02)03751-1

We describe a new chicken P2X subunit that is an orthologue of the mammalian P2X1 receptor. Functional characterization of chicken P2X1 receptors was performed using the amphotericin B perforated patch configuration to avoid the current run‐down observed under whole‐cell patch‐clamp conditions. Responses to agonists and to the antagonist PPADS (pyridoxal 5‐phosphate 6‐azophenyl‐2′,4′‐disulfonic acid) were similar to what has been described for mammalian orthologues. However, the antagonists suramin and NF023 were much less potent at chicken P2X1 receptors than at human P2X1 receptors. In embryonic tissues, transcript expression is predominant in lung, liver and skeletal muscle. Overlapping expression with cP2X4 and cP2X5 subunits in several embryonic tissues, including skeletal muscle, indicates that the native embryonic P2X receptors could be heteromultimeric.