Abstract
We report here the cloning of a chicken cDNA (402 aa) showing high sequence similarity to the previously cloned rat and human P2X5 receptors (67 and 69%, respectively). The chicken P2X5 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 P2X5 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 (EC50 ∼ 2 μM) and suramin and pyridoxal 5-phosphate-6-azophenyl-2′,4′-disulfonic acid are potent antagonists. Additionally, reversal potential measurements indicate that chicken P2X5 is permeable not only to cations but also to chloride (Pcs+/Pcl- ∼ 1.9), as has been described for native P2X receptor mediated responses in embryonic chicken skeletal muscle. mRNA distribution of chicken P2X5 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 P2X5 receptors are expressed in developing muscle and might play a rote in early muscle differentiation.
Original language | English |
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Pages (from-to) | 1256-1265 |
Number of pages | 10 |
Journal | Journal of Neurochemistry |
Volume | 77 |
Issue number | 5 |
DOIs | |
State | Published - 21 Jun 2001 |
Keywords
- Chicken embryo
- Desensitization
- Gene structure
- Heart
- Permeability
- Skeletal muscle
- Somite
ASJC Scopus subject areas
- Biochemistry
- Cellular and Molecular Neuroscience