A. Ruppelt et al., Genomic structure, developmental distribution and functional properties ofthe chicken P2X(5) receptor, J NEUROCHEM, 77(5), 2001, pp. 1256-1265
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 compos
ed of 12 translated exons, which shows conserved genomic structure with mam
malian P2X genes. In HEK-293 cells heterologously expressing chicken P2X(5)
receptors, ATP activates a current that desensitizes in a way that is depe
ndent on the presence of extracellular divalent cations. ATP and 2-methylth
io ATP are equipotent agonists (EC50 similar to 2 muM) and suramin and pyri
doxal 5-phosphate-6-azophenyl-2 ' ,4 ' -disulfonic acid are potent antagoni
sts. Additionally, reversal potential measurements indicate that chicken P2
XS is permeable not only to cations but also to chloride (PCs+/PCl- similar
to 1.9), as has been described for native P2X receptor mediated responses
in embryonic chicken skeletal muscle. mRNA distribution of chicken P2X(5) w
as determined by in situ hybridization analysis in both whole embryos and o
n tissue slices of heart and skeletal muscle. Our results suggest that chic
ken P2X(5) receptors are expressed in developing muscle and might play a ro
le in early muscle differentiation.