The protein P2Y2 is a G-protein coupled metabotropic receptor that belongs to a larger family consisting of several receptor subtypes that each has a different pharmacological selectivity for various adenosine and uridine nucleotides. (This selectivity overlaps in some cases). The P2Y2 receptor is responsive to both adenosine and uridine nucleotides and thus a receptor for both ATP and UTP. P2Y2 plays a role in the activation of a phosphatidylinositol-calcium second messenger cascade system which regulates a wide range of physiological and pathological cell processes. For example, P2Y2 appears to control cell cycling in endometrial carcinoma cells, and act as a morphogen receptor for potentiating neurotrophin signaling in neuronal development and regeneration. P2Y2 is localized to the cell membrane and is widely expressed in mammals, as it can be found in the spleen, testis, kidney, liver, lung, heart, bone, and brain. Three transcript variants (variants 1, 2, and 3) encoding the same protein have been identified for this gene.
Immunohistochemistry-Paraffin: P2Y2 Antibody [NB110-39032] - IHC analysis of P2Y2 in mouse brain.
In a 2012 review, University of Missouri researchers overviewed the existing literature to highlight the contributions of P2Y2 and its relative P2X7 on neuroinflammatory and neuroprotective processes in the central nervous system (CNS) (1). A follow-up review from the same group specifically focused on P2Y2’s neuroprotective role in the CNS and glial cells (2). In that publication they review cell-specific and tissue-integrated functions of P2Y2 as an intrinsic means of preventing and attenuating neurodegenerative diseases (such as Alzheimer’s) that result from chronic inflammation. A review from Di Virgilio examines the role of purine signaling and the role that its complex network cascade plays in creating and modulating the tumor microenvironment (3). Mounting evidence indicates that both adenosine and adenosine triphosphate are key players in host-tumor interactions and directly affect tumor cell growth. Furthermore, purinergic receptor polymorphic variations appear to play a role in human bone turnover and remodeling as summarized by Wesselius’ group from the Netherlands (4). It appears that purinergic receptors are fundamental for key bone cellular functions such as formation, resorption, cytokine release, and mineral deposition.
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