Ask about this productRelated genes to: P2ry1 antibody
- Gene:
- P2RY1 NIH gene
- Name:
- purinergic receptor P2Y1
- Previous symbol:
- -
- Synonyms:
- P2Y1, SARCC
- Chromosome:
- 3q25.2
- Locus Type:
- gene with protein product
- Date approved:
- 1995-10-20
- Date modifiied:
- 2019-04-23
Related products to: P2ry1 antibody
Related articles to: P2ry1 antibody
- Chronic kidney disease (CKD) affects over 850 million people worldwide and is characterized by progressive renal fibrosis driven by activated interstitial fibroblasts. Signaling by extracellular nucleotides and P2 receptors plays an important role in renal pathophysiology, yet its contribution to fibroblast activation and fibrosis remains poorly understood. Here, we investigated the expression and function of G-coupled P2Y receptors in renal interstitial fibroblasts and their involvement in experimental kidney fibrosis. Using highly selective RNA in situ hybridization, we detected P2Y () and P2Y () receptor expression in interstitial fibroblasts. Notably, P2Y expression was markedly upregulated in several experimental mouse models of renal fibrosis. Functional assays in primary cultured renal fibroblasts confirmed G-coupled P2Y receptor activity, as evidenced by transient intracellular Ca elevations upon nucleotide stimulation. Primary cultured renal fibroblasts exhibited enhanced migration in response to extracellular uridine diphosphate (UDP). To assess the contribution of interstitial P2Y receptors to fibrosis progression, we employed an adenine-induced nephropathy model with or without the selective P2Y antagonist MRS2578. Pharmacological inhibition of P2Y significantly reduced the mRNA expression of the myofibroblast marker α-smooth muscle actin and collagen I. Collectively, these findings suggest that upregulated P2Y receptor signaling promotes the transition of resident interstitial cells into myofibroblasts during renal fibrosis, likely by modulating fibroblast migration. Inhibition of P2Y signaling could represent a new strategy for reducing excessive renal fibrosis. - Source: PubMed
Publication date: 2026/03/31
Süß Lena MariePetzendorfer AnnaTran Minh LinhFirmke BettinaSüß AnjaWarth RichardBroeker Katharina Anna-ElisabethForst Anna-Lena - Chronic kidney disease (CKD) affects over 850 million people worldwide and is characterized by progressive renal fibrosis driven by activated interstitial fibroblasts. Signaling by extracellular nucleotides and P2 receptors plays an important role in renal pathophysiology, yet its contribution to fibroblast activation and fibrosis remains poorly understood. Here, we investigated the expression and function of G-coupled P2Y receptors in renal interstitial fibroblasts and their involvement in experimental kidney fibrosis. Using highly selective RNA in situ hybridization, we detected P2Y () and P2Y () receptor expression in interstitial fibroblasts. Notably, P2Y expression was markedly upregulated in several experimental mouse models of renal fibrosis. Functional assays in primary cultured renal fibroblasts confirmed G-coupled P2Y receptor activity, as evidenced by transient intracellular Ca elevations upon nucleotide stimulation. Primary cultured renal fibroblasts exhibited enhanced migration in response to extracellular uridine diphosphate (UDP). To assess the contribution of interstitial P2Y receptors to fibrosis progression, we employed an adenine-induced nephropathy model with or without the selective P2Y antagonist MRS2578. Pharmacological inhibition of P2Y significantly reduced the mRNA expression of the myofibroblast marker α-smooth muscle actin and collagen I. Collectively, these findings suggest that upregulated P2Y receptor signaling promotes the transition of resident interstitial cells into myofibroblasts during renal fibrosis, likely by modulating fibroblast migration. Inhibition of P2Y6 signaling could represent a new strategy for reducing excessive renal fibrosis. - Source: PubMed
Publication date: 2026/01/29
Süß Lena MariePetzendorfer AnnaFirmke BettinaSüß AnjaWarth RichardBroeker Katharina Anna-ElisabethForst Anna-Lena - The tripartite motif (TRIM) family of E3 ubiquitin ligases is known to play a crucial role in the initiation, growth, and metastasis of various tumors. However, little is known about the biological features and relevant molecular mechanism of Tripartite motif-containing 63 (TRIM 63) in melanoma. The expression levels of TRIM63 and purinergic receptor P2Y1 (P2RY1) in melanoma were examined by online database. Cell counting kit-8 (CCK-8) and colony formation assay were carried out to explore the effects of TRIM63 on melanoma cells proliferation. Transwell assay was used to explore the influence of TRIM63 on melanoma cells invasion and migration. Bioinformatics, co-immunoprecipitation (co-IP) assay, ubiquitination assay, and protein stability assay were used to detect the regulatory mechanism of TRIM63 on P2RY1. TRIM63 was upregulated in melanoma samples, and a higher expression level of TRIM63 indicated a shorter overall survival of melanoma patients. Knocked down of TRIM63 obviously suppressed the proliferation, invasion, and migration abilities of melanoma cells. Mechanistically, TRIM63 was regarded as a posttranslational mediator of P2RY1, and TRIM63 was co-immunoprecipitated with P2RY1 and degraded its protein level. Notably, silencing P2RY1 alleviated melanoma cells progression by TRIM63 depletion. Collectively, these data suggested that TRIM63 contributed to melanoma cells growth and mobility by ubiquitination of P2RY1 and may be a promising candidate as a potential diagnostic and therapeutic marker for patients with melanoma. - Source: PubMed
Zhang QianqianZhu ZixuanYang HuiWang XiaoyanLiu YanxiaSong Laitao - Fibroblast-like cells (FLCs) exist in the smooth muscle layers of visceral organs, yet in many instances their functional role(s) have not been identified. FLCs express platelet-derived growth factor receptor (PDGFR) α and are a novel class of excitable cells recently described in visceral organs. Crenolanib is a benzamidine quinolone derivative originally developed as an inhibitor of PDGFR to treat certain solid tumors with PDGFRα overexpression mutations. In the present study, we used crenolanib to disrupt PDGFRα expression and signaling in the gastrointestinal (GI) tracts of mice. Intraperitoneal injections of crenolanib (100 µg/g body wt) or DMSO control vehicle were given to littermates from postpartum P1 through P15. Crenolanib-injected mice were smaller in size and weight. The gastrointestinal tracts were also shorter and appeared partially distended. qPCR revealed downregulation of key gene transcripts involved in PDGFRα cell signaling including , , and . Confocal immunofluorescence demonstrated significant decreases in PDGFRα and SK3 protein expression. c-Kit expression was slightly inhibited, but gastric, intestinal, and colonic pacemaker activity was not affected by crenolanib. Purinergic inhibitory postjunctional motor responses were greatly attenuated in the GI tracts of crenolanib-treated animals compared with vehicle-treated controls in response to electric field-evoked nerve stimulation. These data provide evidence for a functional role of PDGFRα cells in inhibitory neuroeffector motor responses throughout the gastrointestinal tract. The physiological roles of newly described PDGFRα interstitial cells in neurotransmission within the gastrointestinal (GI) tract have predominantly come from studies on isolated cells. Here we used an inhibitor of PDGFRα, crenolanib, to examine the effects of PDGFRα cells in enteric inhibitory neurotransmission. Crenolanib caused loss of PDGFRα cells and neurally evoked fast inhibitory junction potentials associated with purine neurotransmission, providing evidence for the function of PDGFRα cells within intact tissues of the GI tract. - Source: PubMed
Publication date: 2025/12/31
Hwang Sung JinSanders Kenton MWard Sean M - Hepatic stellate cells (HSC) play a crucial role in the fibrotic response of the liver when they transdifferentiate from quiescent cells (qHSC) to myofibroblast (MFB). Ca responses mediated by purinergic P2Y receptors are not fully characterized in qHSC and MFB. The objective of this study was to compare the expression of purinergic receptors with the capacity to mobilize intracellular Ca in both phenotypes, as well as to explore the potential role of these signals in HSCs activation. Isolated mouse HSC were quiescent on day 2 and became MFB on day 7 when cultured in high stiffness substrate. Both phenotypes expressed the transcripts of , , and , and exhibited a similar Ca response to UDP, UTP and Bz-ATP, indicating comparable activity in P2Y6, P2Y2 and P2X7 receptors. In contrast, transcript was detected only in MFB. Remarkably, P2Y1 receptor was identified in qHSC, an observation that had not yet been reported. Evidence of P2Y1 receptor functionality was obtained from stimulation with ADP. ADP-elicited Ca mobilization was more potent in qHSC in comparison to MFB. Interestingly, ADP stimulation worsens the transdifferentiation of qHSC to MFB after 4 or 7 days in culture, strongly suggesting the role of this purinergic receptor in HSC activation. - Source: PubMed
Publication date: 2025/11/23
Mata-Martínez EsperanzaJuárez-Mercado Ana PatriciaGonzález-Gallardo AdrianaNúñez-Ríos José DavidDíaz-Muñoz MauricioHernández-Muñoz RolandoVázquez-Cuevas Francisco G