Characterization and chromosomal localization of a human P2X receptor from the urinary bladder.
A cDNA encoding an ion channel (hP2X), gated by extracellular ATP, was isolated from the human urinary bladder. It encodes a 399 amino acid protein, composed of a cysteine-rich central domain, flanked by two hydrophobic regions. A comparison of the sequence with those of the corresponding rat and mouse proteins shows predominantly conservative substitutions of hydrophilic residues. Northern blot analysis demonstrated the presence of the mRNA in several human tissues and established that the distal untranslated portion of the mRNA includes an 'expressed sequence tag' for the differentiation of the hemopoetic cell line, HL60. By fluorescent in situ hybridization the hP2X gene was mapped to the short arm of human chromosome 17. Expressed in Xenopus oocytes, the receptor was sensitive to the purinergic agonists ATP and alpha,beta-methylene ATP.
Valera
S
S
Glaxo Institute for Molecular Biology, Geneva, Switzerland.
Talabot
F
F
Evans
R J
RJ
Gos
A
A
Antonarakis
S E
SE
Morris
M A
MA
Buell
G N
GN
D000595:Amino Acid Sequence; D001483:Base Sequence; D015152:Blotting, Northern; D002874:Chromosome Mapping; D002886:Chromosomes, Human, Pair 17; D018076:DNA, Complementary; D018922:HL-60 Cells; D006801:Humans; D017404:In Situ Hybridization, Fluorescence; D008969:Molecular Sequence Data; D012333:RNA, Messenger / Q000235:genetics / Q000378:metabolism; D018048:Receptors, Purinergic P2 / Q000235:genetics*; D017386:Sequence Homology, Amino Acid; D001743:Urinary Bladder / Q000378:metabolism*
D018076:DNA, Complementary; D012333:RNA, Messenger; D018048:Receptors, Purinergic P2