Ask about this productRelated genes to: P2ry1 Blocking Peptide
- 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 Blocking Peptide
Related articles to: P2ry1 Blocking Peptide
- Children with heart disease face competing risks of thrombosis and bleeding. Antiplatelet agents are widely used, but clinical effectiveness and safety may vary with pharmacogenomic variants. We evaluated bleeding and thromboembolic outcomes and explored pharmacogenomic associations in a pediatric cardiac cohort. - Source: PubMed
Publication date: 2026/07/25
Esteso PaulSiegel BryanKim HyunMorin CarolinePace ElizabethMaschietto NicolaVanderpluym ChristinaEmani SitaramRoberts Amy ENewburger Jane WQuiat DanielMorton Sarah UMoynihan Katie M - 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 (P2ry1) and P2Y (P2ry6) 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 Ca²⁺ 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: 2026/06/17
Süß Lena MariePetzendorfer AnnaTran Minh LinhFirmke BettinaSüß AnjaWarth RichardBroeker Katharina Anna-ElisabethForst Anna-Lena - Extracellular adenosine triphosphate (ATP) and diphosphate (ADP) act as key signalling molecules in the central nervous system (CNS) and regulate neuroinflammatory responses through purinergic receptors. Although astrocytes and neurons undergo profound changes in signalling and metabolism during inflammation, the contribution of specific purinergic pathways to inflammation-induced neurodegeneration remains unclear. Here we show that the ADP/ATP-activated Gq-coupled receptor P2Y drives astrocyte-mediated neurotoxicity in experimental autoimmune encephalomyelitis (EAE), a model of multiple sclerosis (MS). Using plasma membrane-targeted luciferase reporter mice, we demonstrate that extracellular ATP levels are increased during acute EAE. This was accompanied by elevated astrocytic P2ry1 expression, which is also observed in inflammatory MS lesions. In vivo, pharmacological inhibition or astrocyte-specific deletion of P2Y reduced disease severity, astrocytosis, and neuronal loss, whereas neuron-specific deletion exerted only modest effects. Mechanistically, astrocytic P2Y signalling promoted cytokine-induced ERK activation, inflammatory gene expression, and metabolic reprogramming in vitro. In contrast to supernatants from stimulated P2Y-deficient astrocyte culture, supernatants derived from stimulated P2Y-proficient astrocytes reduced neuronal viability, demonstrating neurotoxic effects mediated by astrocyte-derived factors. In contrast, neuronal P2Y signalling primarily contributed to oxidative stress and mitochondrial dysfunction. Together, these findings identify astrocytic P2Y as a key regulator of neuroinflammatory damage and a potential therapeutic target. - Source: PubMed
Publication date: 2026/06/13
Schubert CharlotteLopes Fonseca RicardoHadjilaou AlexandrosVieira VanessaDegenhardt KarolineSeemann Anna LenaHakimy AliceSonner Jana KLudewig PeterMagnus TimSchneider MarionMüller Christa EHirnet DanielaFriese Manuel A - Intracellular Ca transients drive key developmental and physiological processes, yet their role in oncogenesis remains incompletely understood. In glioblastoma (GBM), an aggressive brain malignancy, tumor cellular networks exhibit self-sustaining Ca transients that promote tumor growth through unclear mechanisms. Using patient-derived GBM models, we show that these transients depend primarily on intracellular Ca stores and extend to the nucleus to drive tumorigenesis. A neuromodulator screen identified extracellular purines ATP and ADP as potent inducers of both nuclear and cytosolic Ca transients via activation of metabotropic purinergic P2RY1 receptors, whose knockdown attenuates tumorigenicity and . Mechanistically, Ca transients promote tumorigenesis via the nuclear Ca/calmodulin-dependent kinase CAMK4, which regulates transcriptional and epigenetic programs, as well as ribosomal DNA transcription. From the therapeutic perspective, pharmacologic P2RY1 inhibition suppresses tumor growth and . Collectively, these findings reveal a pharmacologically targetable oncogenic mechanism in GBM and possibly other malignancies. - Source: PubMed
Publication date: 2026/05/14
Wang ShuaiRichter JennaKim Claire DRonnen RebeccaCai JuliaSong YunfeiHaddock SaraStoessel Mark BDada HannahGross SuzanneGuerrero AdlerKarnavas TheodorisStephan GabrieleBelizaire GregBonanni LukeGolub DanielleSabio JonathanSchwarz HannaJiang AlbertMaleeha NawshinGhosh AnuvaYung MadelynnGrossman-Glover EricTang JocelynGherghina LauraDonovan AlexLeonard AndreaChiriboga LuisJones DrewSong Soomin CMazzoni EstebanVincent TheresaSchneider Robert JZagzag DavidMiura YukiBasu JayeetaBrand Andrea HPlacantonakis Dimitris G - 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