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Our results clearly demonstrate the involvement of P2Y2R subtypes in the pathogenesis of fibrotic lung diseases in humans and mice and hence support the development of selective P2Y2R antagonists for the treatment of IPF.
both LRP1 (show LRP1 Proteins) and LDLR (show LDLR Proteins) expression and agLDL uptake are regulated by P2Y2R in vascular smooth muscle cells, and agLDL uptake due to P2Y2R activation is dependent upon cytoskeletal reorganization mediated by P2Y2R binding to FLN-A (show FLNA Proteins)
knockdown of P2Y2R retarded cyst expansion in vitro and prevented ATP- and HIF-1alpha (show HIF1A Proteins)-dependent cyst growth. In conclusion, P2Y2R mediates ATP-dependent cyst growth and is transcriptionally regulated by HIF-1alpha (show HIF1A Proteins).
P2Y2R is an inhibitor of arterial intimal calcification, regulating the osteoblastic trans-differentiation of smooth muscle cells through P2Y2R-mediated Runx2 (show RUNX2 Proteins) antagonism.
These findings are consistent with the notion that the primary action of P2Y2 receptor signalling in bone is to regulate extracellular ATP levels.
Results demonstrate that P2Y2 contributes to response properties of cutaneous afferents, as P2Y2 deletion reduces responsiveness of conventional unmyelinated polymodal afferents to heat and appears to result in the acquisition of mechanical responsiveness in a subset of TRPV1 (show TRPV1 Proteins)-expressing afferents.
This study suggests that P2Y2 may participate in cardiomyopathy in mdx (show DMD Proteins) mice.
Extracellular ATP induces vascular inflammation and atherosclerosis via activation of P2Y2.
Endothelial cell-specific P2Y2R deficiency reduces atherosclerotic burden and promotes plaque stability in ApoE (show APOE Proteins)(-/-) mice through impaired macrophage infiltration acting together with reduced matrix metalloproteinase-2 (show MMP2 Proteins) activity and increased smooth muscle cell migration.
expression of P2Y (show P2RY1 Proteins)(2) receptor in peripheral sensory neurons that innervate the injured tissue and the activation of P2Y (show P2RY1 Proteins) receptors contributes to mechanical allodynia following inflammation
Study demonstrated that the P2Y2 receptor was highly expressed in MCF7 and Hs578T breast cancer cells and indicated that the P2Y2 receptor promoted cell migration and invasion in breast cancer cells via EMT (show ITK Proteins)-related genes Snail (show SNAI1 Proteins) and E-cadherin (show CDH1 Proteins).
Proliferation and migration of functionally impaired cardiac progenitor cells are enhanced by P2Y2R-mediated YAP (show YAP1 Proteins) activation, revealing a novel link between extracellular nucleotides released during injury/stress and Hippo signaling-a central regulator of cardiac regeneration.
nterleukin-8 release after purinergic stimulation in ALI-cultured HEECs is mediated through P2Y2 receptor activation.
Human umbilical vein endothelial cells exposed to either P2Y2 receptor antagonists or siRNA showed impaired fluid shear stress-induced cell alignment, and actin stress fiber formation as early as 6 h.
There is increased expression of P2Y2 receptors in the rectosigmoid mucosa of diarrhea-predominant irritable bowel syndrome patients. P2Y2 correlated with abdominal pain.
A novel SNP-systemic lupus erythematosus association was identified between FCHSD2 and P2RY2, peaking at rs11235667 on a 33-kb haplotype upstream of ATG16L2.
Hypoxia and upregulated HIF-1a (show HIF1A Proteins) both upregulated the P2Y2 levels in hepatocellular carcinoma cells and increased their survival.
Results show that purinergic receptor P2Y2 (P2Y2R) requires N-glycosylation for expression on the cell surface.
Data indicate that knockdown of caveolin-1 (Cav-1 (show CAV1 Proteins)) expression causes redistribution of the P2Y2 nucleotide receptor (P2Y2R) from membrane rafts.
P2Y2 and Gq/G11 (show STK19 Proteins) are required for basal endothelial NO formation, vascular tone, and blood pressure.
the effect of ATP on Na+-ATPase activity could be involved in antinatriuresis induced by P2Y4 receptor (show P2RY4 Proteins) or a mechanism to counterbalance the natriuretic effect of P2Y2 receptor, promoting fine control of sodium reabsorption in proximal tubule cells.
The product of this gene belongs to the family of P2 receptors, which is activated by extracellular nucleotides and subdivided into P2X ligand-gated ion channels and P2Y 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, found on many cell types, is activated by ATP and UTP and is reported to be overexpressed on some cancer cell types. It is involved in many cellular functions, such as proliferation, apoptosis and inflammation. Three transcript variants encoding the same protein have been identified for this gene.
P2Y purinoceptor 2
, ATP receptor
, P2U purinoceptor 1
, P2U nucleotide receptor
, P2U receptor 1
, purinergic receptor P2Y2
, purinoceptor P2Y2
, P2Y ATP receptor 2
, P2Y2 nucleotide receptor