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In P2Y12 (show P2RY12 Proteins)(-/-) mice, the growth of syngeneic ovarian cancer tumors was reduced by >85% compared with wild-type (WT) mice. In contrast, there was no difference in tumor growth between P2Y1(-/-) and WT mice.
In the brain samples, expressions of P2Y4 (show P2RY4 Proteins) and P2X7 (show P2RX7 Proteins) were significantly reduced, whereas that of P2Y1 was significantly elevated in an age-dependent manner.
Mesenteric endothelial cells are primed by schistosomiasis to a pro-inflammatory phenotype characterized by an increased expression of NTPDases 2 and 3, favoring ADP accumulation and mononuclear cell adhesion, possibly contributing to mesenteric inflammation and schistosomiasis morbidity via P2Y1 receptor signaling.
the amounts of AChE activity, AChE catalytic subunit, structure subunit PRiMA (show PRIMA1 Proteins) and the amount of acetylcholine, in the brain were not, significantly, altered, suggesting the role of P2Y1R in neuron could have different function as that in muscle.
In P2Y1R (-/-) mice, the expression of P2Y2 (show P2RY2 Proteins) receptor in muscle was reduced by over 50 %, as compared to P2Y1R (+/+) mice. P2Y1 receptor regulated the neuromuscular junction gene expression.
Our current results suggest that P2Y1 modulates heat responsiveness and chemosensation in muscle afferents to play a key role in the development of pain-related behaviors during ischemia.
Provide evidence for purinergic glio-endothelial coupling during neuronal activity, highlighting the role of ATP-mediated activation of eNOS (show NOS3 Proteins) via P2Y1 receptors in functional hyperemia.
P2Y1 couples to and activates TRPV4 (show TRPV4 Proteins). PKC inhibitors prevented P2Y1 receptor activation of TRPV4 (show TRPV4 Proteins).
The analysis of single and double KO mice demonstrated that NTPDase2 (show ENTPD2 Proteins) and P2Y1 receptors are not required for murine eye formation
Data indicate that knock down of purinergic P2Y1 receptors inhibited directed migration in neurospheres.
The negative feedback modulation between LncRNA-SARCC/AR complex and HIF-2alpha (show EPAS1 Proteins) signaling may then lead to differentially modulated RCC (show XRCC1 Proteins) progression in a VHL (show VHL Proteins)-dependent manner. Together, these results may provide us a new therapeutic approach via targeting this newly identified signal from LncRNA-SARCC to AR-mediated HIF-2alpha (show EPAS1 Proteins)/C-MYC (show MYC Proteins) signals against RCC (show XRCC1 Proteins) progression.
these data highlight a key role of the P2Y1/PI3Kbeta axis in endothelial cell proliferation downstream of ecto (show TRIM33 Proteins)-F1-ATPase activation by apoA-I (show APOA1 Proteins). Pharmacological targeting of this pathway could represent a promising approach to enhance vascular endothelial protection.
ALIX (show PDCD6IP Proteins) regulates P2Y1 degradation.
There is increased expression of P2Y1 receptors in the rectosigmoid mucosa of diarrhea-predominant irritable bowel syndrome patients.
High extracellular NaCl induces priming of the NLRP3 (show NLRP3 Proteins) inflammasome in RPE (show RPE Proteins) cells, in part via P2Y1 receptor signaling
aim of this study was to evaluate the effects of platelet receptor gene (P2Y12 (show P2RY12 Proteins), P2Y1) and glycoprotein gene (GPIIIa (show ITGB3 Proteins)) polymorphisms, as well as their interactions, on antiplatelet drug responsiveness and clinical outcomes in patients with acute MIS (show AMH Proteins)
Synergistic inhibition of both P2Y1 and P2Y12 (show P2RY12 Proteins) adenosine diphosphate receptors by GLS (show GLS Proteins)-409 immediately attenuates platelet-mediated thrombosis and effectively blocks agonist-stimulated platelet aggregation irrespective of concomitant aspirin therapy.
P2Y1 couples to and activates TRPV4 (show TRPV4 Proteins). PKC (show PRRT2 Proteins) inhibitors prevented P2Y1 receptor activation of TRPV4 (show TRPV4 Proteins).
P2Y1 receptors are a potential pharmacological target leading smooth muscle relaxation to treat spasticity in colonic motor disorders.
Data indicate that ATP-evoked Hoechst 33258 uptake was dependent on activation of P2Y receptors P2Y1 and P2Y2 (show P2RY2 Proteins).
P2Y1 receptor-mediated responses involve Flt3 (show FLT3 Proteins) transactivation, and may identify a unique mechanism whereby cancer chemotherapy with receptor tyrosine kinase (show RET Proteins) inhibitors promotes vascular dysfunction.
Purinergic P2Y1 receptor signaling mediates wound stimuli-induced cyclooxygenase-2 (show PTGS2 Proteins) expression in intestinal subepithelial myofibroblasts.
P2Y1 and P2Y13 (show P2RY13 Proteins) receptors play a major role in vasa (show DDX4 Proteins) vasorum endothelial cells growth responses.
The product of this gene belongs to the family of G-protein coupled receptors. This family has several receptor subtypes with different pharmacological selectivity, which overlaps in some cases, for various adenosine and uridine nucleotides. This receptor functions as a receptor for extracellular ATP and ADP. In platelets binding to ADP leads to mobilization of intracellular calcium ions via activation of phospholipase C, a change in platelet shape, and probably to platelet aggregation.
, P2Y purinoceptor 1
, P2Y1 receptor
, P2Y1 purinoceptor
, P2 purinoceptor subtype Y1
, platelet ADP receptor
, P2 purinoreceptor subclass 2Y
, P2Y ATP receptor 1
, ATP receptor P2Y1
, G protein-coupled receptor
, p2y1 purinoceptor