AVIAN AND HUMAN HOMOLOGS OF THE P2Y(1) RECEPTOR - PHARMACOLOGICAL, SIGNALING, AND MOLECULAR-PROPERTIES

The P2Y receptor on turkey erythrocyte membranes was the first P2 rece ptor to be shown to activate phospholipase C (PLC) in a strictly guani ne nucleotide-dependent manner and remains the only G protein-coupled P2 receptor for which G protein-coupling kinetics have been defined. T his membrane receptor has provided a model system for detailed pharmac ological analyses of a series of chain-extended 2-thioether derivative s of adenine nucleotides that exhibit remarkable selectivity and poten cy for P2Y receptors. This model system also has led recently to ident ification of a novel series of P2 receptor antagonists. The turkey ery throcyte receptor is the species homologue of the chick P2Y(1) recepto r originally cloned by Webb and coworkers [Webb et al., 1993]. We also have cloned the human homologue of the P2Y(1) receptor, which exhibit s identical pharmacological and second messenger signaling properties to that of the avian P2Y(1) receptor. (C) 1997 Wiley-Liss, Inc.