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P2Y purinoceptor 10 (P2Y10) is a member of the P2Y family of G protein-coupled receptors (GPCRs), encoded in humans by the P2RY10 gene. This receptor is characterized by seven transmembrane domains typical of GPCRs and is activated mainly by lysophosphatidic acid and sphingosine-1-phosphate, as well as possibly by purine and pyrimidine nucleotides. On activation, P2Y10 mediates intracellular signaling events such as mobilization of inositol trisphosphate-sensitive calcium stores, activation of inward membrane currents, and stimulation of diacylglyceride-dependent protein kinases. Expression is observed at low levels in blood leukocytes with upregulation during differentiation along the monocytic pathway. P2Y10 is considered a therapeutic target due to its roles in immune signaling and potential involvement in inflammatory and gastrointestinal processes, though no approved drugs yet specifically target this receptor. It is primarily studied in the context of research on purinergic signaling, immune cell regulation, and as a deorphanized GPCR for specific lysolipid mediators. No direct clinical biomarker or safety data is established, and it remains a focus of investigative drug development rather than established therapy or diagnosis.
Agonism at P2Y10 leads to activation of G protein signaling, causing mobilization of inositol-1,4,5-triphosphate-sensitive Ca²⁺ stores, activation of inward plasma membrane currents, and stimulation of diacylglyceride-dependent protein kinases. Functions as a receptor for lysophosphatidic acid and sphingosine-1-phosphate, modulating downstream signaling cascades
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