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P2RX5 Membrane Protein Introduction

Introduction of P2RX5

P2X purinoceptor 5 (P2RX5) is a membrane protein encoded by human P2RX5 gene, which is mapped to chromosome 17p13.2. P2RX5 belongs to the family of ATP-gated P2X receptor cation channel proteins and it acts as a sensor for the extracellular adenosine triphosphate (ATP). Upon ATP binding, P2RX5 can be exclusively activated to mediate calcium flux, induce large pore formation, and form signaling complexes with interacting proteins and membrane lipids. P2RX5 is expressed by a wide range of mammalian cells including neurons and glial cells in the central (CNS) and peripheral (PNS) nervous systems, muscle cells, epithelial cells, endothelial cells, endocrine cells, bone cells, and immune cells.

Basic Information of P2RX5
Protein Name Adhesion G-protein coupled receptor G2
Gene Name P2RX5
Aliases P2X5, P2X5R, purinergic receptor P2X 5
Organism Homo sapiens (Human)
UniProt ID Q93086
Transmembrane Times 1
Length (aa) 422
Sequence MGQAGCKGLCLSLFDYKTEKYVIAKNKKVGLLYRLLQASILAYLVVWVFLIKKGYQDVDTSLQSAVITKVKGVAFTNTSDLGQRIWDVADYVIPAQGENVFFVVTNLIVTPNQRQNVCAENEGIPDGACSKDSDCHAGEAVTAGNGVKTGRCLRRENLARGTCEIFAWCPLETSSRPEEPFLKEAEDFTIFIKNHIRFPKFNFSKSNVMDVKDRSFLKSCHFGPKNHYCPIFRLGSVIRWAGSDFQDIALEGGVIGINIEWNCDLDKAASECHPHYSFSRLDNKLSKSVSSGYNFRFARYYRDAAGVEFRTLMKAYGIRFDVMVNGKGAFFCDLVLIYLIKKREFYRDKKYEEVRGLEDSSQEAEDEASGLGLSEQLTSGPGLLGMPEQQELQEPPEAKRGSSSQKGNGSVCPQLLEPHRST

Function of P2RX5 Membrane Protein

P2RX5 functions as a ligand-gated ion channel to regulate the selective permeability to cations, which is essential for various cellular functions, including proliferation and apoptosis, especially in bone remodeling and bone homeostasis. Additionally, P2RX5 is involved in the activation of the inflammasome, in the optimal inflammasome-induced IL-1β production by osteoclasts, and in osteoclast maturation and hyper-multinucleation. P2RX5 deficiency has been found to inhibit local osteoclast differentiation and activation, suggesting that P2RX5 may a potential therapeutic target in the context of periodontal disease and other selectively inhibiting inflammatory bone loss. Besides, there are many biological processes involving P2RX5, such as blood coagulation, nervous system development, regulation of calcium ion transport into the cytosol, regulation of calcium-mediated signaling, etc. P2RX5 is associated with Cystinosis disease.

A simple schematic representation of a ligand-gated ion channel. Fig.1 A simple schematic representation of a ligand-gated ion channel.

Application of P2RX5 Membrane Protein in Literature

  1. Kim H., et al. The purinergic receptor P2X5 regulates inflammasome activity and hyper-multinucleation of murine osteoclasts. Sci Rep. 2017, 7(1): 196. PubMed ID: 28298636

    This article demonstrates that P2RX5 is indispensable for IL-1β production by osteoclasts and inflammasome activation mediated by ATP and that P2X5-deficient maturation in osteoclast is rescued in vitro by addition of exogenous IL-1β.

  2. Wang W., et al. Effects of Adenosine Triphosphate on Proliferation and Odontoblastic Differentiation of Human Dental Pulp Cells. J Endod. 2016, 42(10): 1483-9. PubMed ID: 27576209

    This article demonstrates that all P2Y receptor subtypes and the purinoceptors P2X3, P2X4, P2X5, and P2X7 can be detected in human dental pulp cells.

  3. Meng M., et al. P2X2 and P2X5 Receptors Mediate Bladder Hyperesthesia in ICC in Female Overactive Bladder. Cell Biochem Biophys. 2015, 72(2): 375-83. PubMed ID: 25561285

    This article suggests that P2RX2 and P2RX5 may play a role in mediating bladder hyperesthesia in interstitial cells of Caja in the female overactive bladder.

  4. Yang L.P., et al. The Relationship Study between Expressions of P2X5 Receptor and Deficiency-cold Syndrome/Deficiency-heat Syndrome at Various Ambient Temperatures. Zhongguo Zhong Xi Yi Jie He Za Zhi. 2015, 35(5): 559-62. PubMed ID: 26159019

    This article confirms that the P2RX5 expression level is different in different syndrome groups at different ambient temperatures.

  5. Abramowski P., et al. A truncation variant of the cation channel P2RX5 is upregulated during T cell activation. PLoS One. 2014, 9(9): e104692. PubMed ID: 25181038

    This article indicates a functional role of the human P2RX5 truncation variant in T cell activation and immunoregulation.

P2RX5 Preparation Options

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