A new human P2Y receptor, P2Y11, was cloned and found to uniquely couple to both phosphoinositide and adenylyl cyclase pathways, behaving as a selective purinoceptor with ATP as the most potent agonist.
The study identifies and characterizes a novel human P2Y receptor (P2Y11) that uniquely couples to both phosphoinositide and adenylyl cyclase pathways.
Clones encoding a new human P2Y receptor, provisionally called P2Y11, have been isolated from human placenta complementary DNA and genomic DNA libraries. The 1113-base pair open reading frame is interrupted by one intron. The P2Y11 receptor is characterized by considerably larger second and third extracellular loops than the subtypes described so far. The deduced amino acid sequence exhibits 33% amino acid identity with the P2Y1 receptor, its closest homolog. Northern blot analysis detected human P2Y11 receptor messenger RNA in spleen and HL-60 cells. The level of P2Y11 transcripts was strongly increased in these cells after granulocyte differentiation induced by retinoic acid or dimethyl sulfoxide. The new receptor was stably expressed in 1321N1 astrocytoma and CHO-K1 cells, where it couples to the stimulation of both the phosphoinositide and adenylyl cyclase pathways, a unique feature among the P2Y family. The rank order of agonists potency was: ATP > 2-methylthio-ATP >>> ADP, whereas UTP and UDP were inactive, indicating that it behaves as a selective purinoceptor.
Communi et al. (Mon,) reported a other. Cloning and characterization of human P2Y11 receptor was evaluated on Receptor cloning and functional characterization. A new human P2Y receptor, P2Y11, was cloned and found to uniquely couple to both phosphoinositide and adenylyl cyclase pathways, behaving as a selective purinoceptor with ATP as the most potent agonist.