Disease relevance of P2RY1

• Both the purinergic receptor stimulation of phospholipase A2 and the enhanced activity mediated by rhodopsin are completely pertussis toxin-sensitive, suggesting the regulation of phospholipase A2 by a member of the Gi family of G proteins [1].

High impact information on P2RY1

• We have assessed the relative contribution of Ca2+ entry and Ca2+ release from internal stores to the [Ca2+]i transients evoked by purinergic receptor activation in bovine adrenal chromaffin cells [2].
• To probe the effect of increased intracellular pH (pHi) on Ca2+ homeostasis in cultured bovine aortic endothelial cells (BAEC), we studied the effect of weak bases, ammonium chloride (NH4Cl) and methylamine (agents which increase pHi by direct passive diffusion), on resting and ATP (purinergic receptor agonist)-induced Ca2+ fluxes [3].
• These results suggest (1) that rhodopsin is similar to other receptors that normally couple to Gi when expressed in cultured cells and (2) that regulation of adenylyl cyclase and PLA2 in CHO cells by rhodopsin and the purinergic receptor occur via distinct pathways [1].
• However, the photoreceptor does potentiate purinergic receptor-mediated phospholipase A2 activation in a light-dependent manner [1].
• The purinergic receptor has been reported to activate both phospholipase C and phospholipase A2 in this cell line [1].

Biological context of P2RY1

• 2-Methylthio-ATP and UTP, selectively activating P2Y1 and P2Y2 purinoceptors respectively, and ATP, a non-selective agonist at these two receptors, stimulate the tyrosine phosphorylation of both p42mapk and p44mapk, as revealed by Western blots with an antiserum specific for the tyrosine-phosphorylated forms of the enzymes [4].

Anatomical context of P2RY1

• Cloning and expression of a P2y purinoceptor from the adult bovine corpus callosum [5].
• Using a chick P2Y1 receptor cDNA probe we have isolated a mammalian P2Y receptor clone from a bovine aortic endothelial cell library [6].
• The regulation of phospholipase A2 by G protein-coupled receptors is examined in CHO cells which normally express the purinergic receptor and have been transfected with bovine rhodopsin [1].
• 10. We conclude that the ATP, co-released with catecholamines in the intact adrenal gland, may inhibit the secretory process by down-regulating the Ca2+ channel via a P2-type purinergic receptor coupled to a PTX-sensitive G protein [7].
• 1. In the present study we have classified the receptor(s) mediating increases in intracellular calcium concentration ([Ca2+]i) in human washed platelets and compared the pharmacological profile obtained with that observed in Jurkat cells, stably transfected with a bovine P2Y1-receptor [8].

Associations of P2RY1 with chemical compounds

• The order of potency for ATP receptor agonists was 2-MeSATP approximately ATP >> alpha, beta-MeATP > adenosine, and UTP was ineffective, a pharmacological profile consistent with that of a P2y purinoceptor [5].
• Pretreatment of cells with the nonselective purinergic receptor antagonist suramin (200 microM), exogenous apyrases, which break down nucleotides (10 U/mL), or the PLC inhibitor U-73122 (10 microM) reduced the wave propagation, whereas the ecto-ATPase inhibitor ARL-67156 (100 microM) significantly enhanced it [9].
• Stimulation of P2Y1 or P2Y2 purinoceptors leads to a severalfold increase in PGI2 efflux; this was blocked in a dose-dependent manner by the selective MAPK kinase inhibitor PD98059 [4].
• Single cells were stimulated with the purinergic receptor agonist ATP resulting in an increase of [Ca2+]i due to intracellular Ca2+ release from inositol 1,4,5-trisphosphate (IP3)-sensitive stores [10].
• Our main conclusions are: (1) a GTP-binding protein participates in the Ca(2+)-induced production of InsPs by phospholipase C, and (2) ATP markedly potentiates the stimulated formation of InsPs, an effect with arises from its role in polyphosphoinositide synthesis and does not involve purinergic receptor activation in permeabilized cells [11].

Analytical, diagnostic and therapeutic context of P2RY1

• RT-PCR showed mRNAs for P2Y1 and P2Y2 receptors and ecto-ATPases in BCECs [9].
• 6. RT - PCR analysis showed that PMA treatment for 4 - 24 h up-regulated P2Y1 and P2Y2 receptors at the mRNA levels [12].

References