Introduction of P2RY1
P2RY1, also known as purinergic receptor P2Y1, suppressing androgen receptor in renal cell carcinoma, P2 Purinoceptor Subtype Y1, platelet ADP receptor, SARCC, or purinergic receptor P2Y, is an about 42 kDa protein and constituted by 373 amino acids. In humans, it is encoded by the P2RY1 gene mapping at the chromosome 3q25.2. The encoded protein P2RY1 is a member of purinergic G-protein coupled receptor (GPCR) family, which has a number of receptor subtypes with diverse pharmacological selectivity, which overlaps in some cases, for many adenosine and uridine nucleotides. P2RY1 is expressed in almost all human tissues where it exerts numerous biological functions based on its G-protein coupling.
|Basic Information of P2RY1|
|Protein Name||P2Y purinoceptor 1|
|Aliases||P2Y1, ATP receptor, Purinergic receptor|
|Organism||Homo sapiens (Human)|
Function of P2RY1 Membrane Protein
P2RY1 functions as a receptor and is stimulated by nucleotides including extracellular ATP, ADP, UTP, UDP, and UDP-glucose. Up to now, there are eight P2Y receptors, particularly participate in the prejunctional inhibitory modulation of transmitter release and cell proliferation, that have been cloned in humans, involving P2Y1, P2Y2, P2Y4, P2Y6, P2Y11, P2Y12, P2Y13, and P2Y14. P2RY1 is reported to play a major role in platelet physiology. In platelets binding to ADP results in the mobilization of intracellular Ca2+ by the activation of phospholipase C, a change in platelet shape, and presumably to platelet aggregation. Pharmacological evidence suggested that P2RY1, P2RY12, and P2X1 have been identified as the existence of diverse ADP-recognizing receptors in circulating platelets. Moreover, P2RY1, P2RY2, P2RY4, and P2RY6 already have been described on subpopulations of sympathetic neurons, P2RY1 and P2RY2 on sensory neurons, P2RY2, and P2RY4 in intracardiac ganglia, while remarkably P2RY1 appears to be the dominant subtype on enteric neurons.
Fig.1 Crystal packing of P2Y1R–MRS2500 and P2Y1R–BPTU complexes. (Zhang, 2015)
Application of P2RY1 Membrane Protein in Literature
Here, BMP-7 was showed to act on extrainsular cells which express the PDX1 and BMP receptor activin-like kinase 3 (ALK3/BMPR1A). Authors confirmed the existence of progenitor cells in adult human pancreas and suggested a specific anatomical location in ductal and glandular networks.
This study provided genetic evidence that activity-induced Ca2+ accumulation in neonatal terminal/perisynaptic Schwann cells (TPSCs) is exclusively mediated by one subtype of metabotropic purinergic receptor. And in P2ry1 mutant mice, postsynaptic function is altered in response to the nerve stimulation.
The goal of present studies was to elucidate the impacts of blocking calcium pathways of astrocytes (ASs) on oxygen and glucose deprivation (OGD)-induced AS injury.
Authors observed the effects of a P2Y1 receptor antagonist, MRS2179 (2'-deoxy-N6-methyl adenosine 3', 5'-diphosphate diammonium salt) on the release of calcium and Glu of ASs upon the condition of OGD.
In contrast to canonical P2Y1 receptor induced PLC signaling, the activation of platelet P2Y1 receptor during inflammation responses by alternate pathways including Rho GTPases. This may be understood by selective molecular interactions among ligands within the orthosteric site of P2Y1 receptor.
APPPS1 mice treated with P2Y1R antagonists, and APPPS1 mice harboring a genetic deletion of signal pathways downstream of P2Y1R activation were protected from the decrease of spatial learning and memory. Summarily, the study established the restoration of network homeostasis by P2Y1R inhibition as a potential treatment target in AD.
P2RY1 Preparation Options
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