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Genomic structure, developmental distribution and functional properties of the chicken P2X 5 receptor
Author(s) -
Ruppelt Anja,
Ma Weiyuan,
Borchardt Kerstin,
Silberberg Shai D.,
Soto Florentina
Publication year - 2001
Publication title -
journal of neurochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.75
H-Index - 229
eISSN - 1471-4159
pISSN - 0022-3042
DOI - 10.1046/j.1471-4159.2001.00348.x
Subject(s) - receptor , skeletal muscle , suramin , biology , microbiology and biotechnology , ppads , complementary dna , hek 293 cells , molecular cloning , cloning (programming) , protein subunit , extracellular , gene , biochemistry , chemistry , endocrinology , computer science , programming language
We report here the cloning of a chicken cDNA (402 aa) showing high sequence similarity to the previously cloned rat and human P2X 5 receptors (67 and 69%, respectively). The chicken P2X 5 subunit is encoded by a gene composed of 12 translated exons, which shows conserved genomic structure with mammalian P2X genes. In HEK‐293 cells heterologously expressing chicken P2X 5 receptors, ATP activates a current that desensitizes in a way that is dependent on the presence of extracellular divalent cations. ATP and 2‐methylthio ATP are equipotent agonists (EC 50 ∼ 2 µ m ) and suramin and pyridoxal 5‐phosphate‐6‐azophenyl‐2′,4′‐disulfonic acid are potent antagonists. Additionally, reversal potential measurements indicate that chicken P2X 5 is permeable not only to cations but also to chloride (P Cs+ /P Cl‐ ∼ 1.9), as has been described for native P2X receptor mediated responses in embryonic chicken skeletal muscle. mRNA distribution of chicken P2X 5 was determined by in situ hybridization analysis in both whole embryos and on tissue slices of heart and skeletal muscle. Our results suggest that chicken P2X 5 receptors are expressed in developing muscle and might play a role in early muscle differentiation.