P2RX7

P2X purinoceptor 7 is a protein that in humans is encoded by the P2RX7 gene.[5][6]

P2RX7
Identifiers
Aliases	P2RX7, P2X7, purinergic receptor P2X 7
External IDs	OMIM: 602566 MGI: 1339957 HomoloGene: 1925 GeneCards: P2RX7
Gene location (Human) Chr. Chromosome 12 (human)[1] Band 12q24.31 Start 121,132,819 bp[1] End 121,188,032 bp[1]
Gene location (Mouse) Chr. Chromosome 5 (mouse)[2] Band 5|5 F Start 122,643,911 bp[2] End 122,691,432 bp[2]
RNA expression pattern More reference expression data
Gene ontology Molecular function • receptor binding • ATP binding • lipopolysaccharide binding • purinergic nucleotide receptor activity • protein homodimerization activity • channel activity • GO:0001948 protein binding • ion channel activity • extracellular ATP-gated cation channel activity • signaling receptor activity Cellular component • cytoplasm • membrane • intercellular junction • synapse • integral component of membrane • neuromuscular junction • cell membrane • neuronal cell body • bleb • integral component of nuclear inner membrane • integral component of plasma membrane • presynapse • external side of plasma membrane • postsynapse Biological process • cellular response to extracellular stimulus • positive regulation of protein phosphorylation • positive regulation of calcium ion transport into cytosol • regulation of sodium ion transport • NAD transport • response to zinc ion • GO:0048554 positive regulation of catalytic activity • response to organic substance • phospholipid transfer to membrane • T cell homeostasis • positive regulation of cytolysis • protein phosphorylation • cell surface receptor signaling pathway • membrane protein ectodomain proteolysis • phospholipid translocation • positive regulation of interleukin-1 beta production • apoptotic signaling pathway • positive regulation of gamma-aminobutyric acid secretion • calcium ion transport • defense response to Gram-positive bacterium • extrinsic apoptotic signaling pathway • synaptic vesicle exocytosis • ceramide biosynthetic process • positive regulation of cytokine secretion • response to mechanical stimulus • ion transport • reactive oxygen species metabolic process • phagolysosome assembly • regulation of killing of cells of other organism • positive regulation of prostaglandin secretion • positive regulation of interleukin-6 production • inflammatory response • plasma membrane organization • positive regulation of ion transmembrane transport • positive regulation of MAPK cascade • negative regulation of bone resorption • release of sequestered calcium ion into cytosol • cell volume homeostasis • cytolysis • phospholipid scrambling • positive regulation of lymphocyte apoptotic process • positive regulation of bone mineralization • skeletal system morphogenesis • cellular response to organic cyclic compound • membrane depolarization • mitochondrion organization • positive regulation of T cell mediated cytotoxicity • bleb assembly • collagen metabolic process • negative regulation of cell volume • pore complex assembly • response to electrical stimulus • cation transport • positive regulation of ossification • cation transmembrane transport • response to fluid shear stress • response to calcium ion • response to lipopolysaccharide • activation of MAPK activity • positive regulation of mitochondrial depolarization • positive regulation of interleukin-1 beta secretion • vesicle budding from membrane • negative regulation of MAPK cascade • positive regulation of protein secretion • homeostasis of number of cells within a tissue • nociception • positive regulation of bleb assembly • response to ATP • gene expression • response to bacterium • response to organic cyclic compound • programmed cell death • positive regulation of interleukin-1 alpha secretion • protein processing • cellular response to dsRNA • T cell proliferation • positive regulation of gene expression • protein oligomerization • positive regulation of glutamate secretion • cell morphogenesis • positive regulation of cytoskeleton organization • positive regulation of apoptotic process • positive regulation of glycolytic process • response to drug • purinergic nucleotide receptor signaling pathway • blood coagulation • excitatory postsynaptic potential • protein catabolic process Sources:Amigo / QuickGO
Orthologs
Species	Human	Mouse
Entrez	5027	18439
Ensembl	ENSG00000089041	ENSMUSG00000029468
UniProt	Q99572	Q9Z1M0
RefSeq (mRNA)	NM_002562 NM_177427	NM_001038839 NM_001038845 NM_001038887 NM_001284402 NM_011027
RefSeq (protein)	NP_002553	NP_001033928 NP_001033934 NP_001033976 NP_001271331 NP_035157
Location (UCSC)	Chr 12: 121.13 – 121.19 Mb	Chr 5: 122.64 – 122.69 Mb
PubMed search	[3]	[4]
Wikidata
View/Edit Human View/Edit Mouse

The product of this gene belongs to the family of purinoceptors for ATP. Multiple alternatively spliced variants which would encode different isoforms have been identified although some fit nonsense-mediated decay criteria.[7]

The receptor is found in the central and peripheral nervous systems, in microglia, in macrophages, in uterine endometrium, and in the retina.[8][9][10][11][12][13][14] The P2X₇ receptor also serves as a pattern recognition receptor for extracellular ATP-mediated apoptotic cell death,[15][16][17] regulation of receptor trafficking,[18] mast cell degranulation,[19][20] and inflammation.[21][19][20][22]

Structure and kinetics

The P2X₇ subunits can form homomeric receptors only with a typical P2X receptor structure.[23] The P2X₇ receptor is a ligand-gated cation channel that opens in response to ATP binding and leads to cell depolarization. The P2X₇ receptor requires higher levels of ATP than other P2X receptors; however, the response can be potentiated by reducing the concentration of divalent cations such as calcium or magnesium.[8][24] Continued binding leads to increased permeability to N-methyl-D-glucamine (NMDG⁺).[24] P2X₇ receptors do not become desensitized readily and continued signaling leads to the aforementioned increased permeability and an increase in current amplitude.[24]

Pharmacology

Agonists

P2X₇ receptors respond to BzATP more readily than ATP.[24] ADP and AMP are weak agonists of P2X₇ receptors, but a brief exposure to ATP can increase their effectiveness.[24] Glutathione has been proposed to act as a P2X₇ receptor agonist when present at milimolar levels, inducing calcium transients and GABA release from retinal cells.[10][9]

Antagonists

The P2X₇ receptor current can be blocked by zinc, calcium, magnesium, and copper.[24] P2X₇ receptors are sensitive to pyridoxalphosphate-6-azophenyl-2',4'-disulphonic acid (PPADS) and relatively insensitive to suramin, but the suramin analog, NF279, is much more effective. Oxidized ATP (OxATP) and Brilliant Blue G has also been used for blocking P2X₇ in inflammation.[25][26] Other blockers include the large organic cations calmidazolium (a calmodulin antagonist) and KN-62 (a CaM kinase II antagonist).[24]

Receptor trafficking

In microglia, P2X₇ receptors are found mostly on the cell surface.[27] Conserved cysteine residues located in the carboxyl terminus seem to be important for receptor trafficking to the cell membrane.[28] These receptors are upregulated in response to peripheral nerve injury.[29]

In melanocytic cells P2X₇ gene expression may be regulated by MITF.[30]

Recruitment of pannexin

Activation of the P2X₇ receptor by ATP leads to recruitment of pannexin pores[31] which allow small molecules such as ATP to leak out of cells. This allows further activation of purinergic receptors and physiological responses such a spreading cytoplasmic waves of calcium.[32] Moreover, this could be responsible for ATP-dependent lysis of macrophages through the formation of membrane pores permeable to larger molecules.

Clinical significance

Neuropathic pain

Microglial P2X₇ receptors are thought to be involved in neuropathic pain because blockade or deletion of P2X₇ receptors results in decreased responses to pain, as demonstrated in vivo.[33][34] Moreover, P2X₇ receptor signaling increases the release of proinflammatory molecules such as IL-1β, IL-6, and TNF-α.[35][36][37] In addition, P2X₇ receptors have been linked to increases in proinflammatory cytokines such as CXCL2 and CCL3.[38][39] P2X₇ receptors are also linked to P2X₄ receptors, which are also associated with neuropathic pain mediated by microglia.[27]

Osteoporosis

Mutations in this gene have been associated to low lumbar spine bone mineral density and accelerated bone loss in post-menopausal women.[40]

Diabetes

The ATP/P2X7R pathway may trigger T-cell attacks on the pancreas, rendering it unable to produce insulin. This autoimmune response may be an early mechanism by which the onset of diabetes is caused.[41][42]

Researches

Possible link to hepatic fibrosis

One study in mice showed that blockade of P2X7 receptors attenuates onset of liver fibrosis.[43]

See also

• Purinergic receptor
• P2X receptor

References

1. GRCh38: Ensembl release 89: ENSG00000089041 - Ensembl, May 2017
2. GRCm38: Ensembl release 89: ENSMUSG00000029468 - Ensembl, May 2017
3. "Human PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
4. "Mouse PubMed Reference:". National Center for Biotechnology Information, U.S. National Library of Medicine.
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6. Buell GN, Talabot F, Gos A, Lorenz J, Lai E, Morris MA, Antonarakis SE (Feb 1999). "Gene structure and chromosomal localization of the human P2X7 receptor". Receptors & Channels. 5 (6): 347–54. PMID 9826911.
7. "Entrez Gene: P2RX7 purinergic receptor P2X, ligand-gated ion channel, 7".
8. Faria RX, Freitas HR, Reis RA (June 2017). "P2X7 receptor large pore signaling in avian Müller glial cells". Journal of Bioenergetics and Biomembranes. 49 (3): 215–229. doi:10.1007/s10863-017-9717-9. PMID 28573491. S2CID 4122579.
9. Freitas HR, Reis RA (February 2017). "7R activation on Müller glia". Neurogenesis. 4 (1): e1283188. doi:10.1080/23262133.2017.1283188. PMC 5305167. PMID 28229088.
10. Freitas HR, Ferraz G, Ferreira GC, Ribeiro-Resende VT, Chiarini LB, do Nascimento JL, et al. (April 2016). "Glutathione-Induced Calcium Shifts in Chick Retinal Glial Cells". PLOS ONE. 11 (4): e0153677. Bibcode:2016PLoSO..1153677F. doi:10.1371/journal.pone.0153677. PMC 4831842. PMID 27078878.
11. Deuchars SA, Atkinson L, Brooke RE, Musa H, Milligan CJ, Batten TF, et al. (September 2001). "Neuronal P2X7 receptors are targeted to presynaptic terminals in the central and peripheral nervous systems". The Journal of Neuroscience. 21 (18): 7143–52. doi:10.1523/JNEUROSCI.21-18-07143.2001. PMC 6762981. PMID 11549725.
12. Collo G, Neidhart S, Kawashima E, Kosco-Vilbois M, North RA, Buell G (September 1997). "Tissue distribution of the P2X7 receptor". Neuropharmacology. 36 (9): 1277–83. doi:10.1016/S0028-3908(97)00140-8. PMID 9364482. S2CID 21491471.
13. Slater NM, Barden JA, Murphy CR (June 2000). "Distributional changes of purinergic receptor subtypes (P2X 1-7) in uterine epithelial cells during early pregnancy". The Histochemical Journal. 32 (6): 365–72. doi:10.1023/A:1004017714702. PMID 10943851. S2CID 40282870.
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21. Gonzaga DT, Ferreira LB, Moreira Maramaldo Costa TE, von Ranke NL, Anastácio Furtado Pacheco P, Sposito Simões AP, et al. (October 2017). "1-Aryl-1H- and 2-aryl-2H-1,2,3-triazole derivatives blockade P2X7 receptor in vitro and inflammatory response in vivo". European Journal of Medicinal Chemistry. 139: 698–717. doi:10.1016/j.ejmech.2017.08.034. PMID 28858765.
22. Russo MV, McGavern DB (October 2015). "Immune Surveillance of the CNS following Infection and Injury". Trends in Immunology. 36 (10): 637–650. doi:10.1016/j.it.2015.08.002. PMC 4592776. PMID 26431941.
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26. Peng W, Cotrina ML, Han X, Yu H, Bekar L, Blum L, et al. (July 2009). "Systemic administration of an antagonist of the ATP-sensitive receptor P2X7 improves recovery after spinal cord injury". Proceedings of the National Academy of Sciences of the United States of America. 106 (30): 12489–93. doi:10.1073/pnas.0902531106. PMC 2718350. PMID 19666625.
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28. Jindrichova M, Kuzyk P, Li S, Stojilkovic SS, Zemkova H (June 2012). "Conserved ectodomain cysteines are essential for rat P2X7 receptor trafficking". Purinergic Signalling. 8 (2): 317–25. doi:10.1007/s11302-012-9291-x. PMC 3350585. PMID 22286664.
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31. Iglesias R, Locovei S, Roque A, Alberto AP, Dahl G, Spray DC, Scemes E (September 2008). "P2X7 receptor-Pannexin1 complex: pharmacology and signaling". American Journal of Physiology. Cell Physiology. 295 (3): C752-60. doi:10.1152/ajpcell.00228.2008. PMC 2544446. PMID 18596211.
32. Boison D, Chen JF, Fredholm BB (July 2010). "Adenosine signaling and function in glial cells". Cell Death and Differentiation. 17 (7): 1071–82. doi:10.1038/cdd.2009.131. PMC 2885470. PMID 19763139.
33. {{cite journal | vauthors = Honore P, Donnelly-Roberts D, Namovic MT, Hsieh G, Zhu CZ, Mikusa JP, Hernandez G, Zhong C, Gauvin DM, Chandran P, Harris R, Medrano AP, Carroll W, Marsh K, Sullivan JP, Faltynek CR, Jarvis MF | s2cid = 11352013 | display-authors = 6 | title = A-740003 [N-(1-{[(cyanoimino)(5-quinolinylamino) methyl]amino}-2,2-dimethylpropyl)-2-(3,4-dimethoxyphenyl)acetamide], a novel and selective P2X7 receptor antagonist, dose-dependently reduces neuropathic pain in the rat | journal = The Journal of Pharmacology and Experimental Therapeutics | volume = 319 | issue = 3 | pages = 1376–85 | date = December 2006 | pmid = 16982702 | doi = 10.1124/jpet.106.111559 }}
34. Chessell IP, Hatcher JP, Bountra C, Michel AD, Hughes JP, Green P, et al. (April 2005). "Disruption of the P2X7 purinoceptor gene abolishes chronic inflammatory and neuropathic pain". Pain. 114 (3): 386–96. doi:10.1016/j.pain.2005.01.002. PMID 15777864. S2CID 21486673.
35. Clark AK, Staniland AA, Marchand F, Kaan TK, McMahon SB, Malcangio M (January 2010). "P2X7-dependent release of interleukin-1beta and nociception in the spinal cord following lipopolysaccharide". The Journal of Neuroscience. 30 (2): 573–82. doi:10.1523/JNEUROSCI.3295-09.2010. PMC 2880485. PMID 20071520.
36. Shigemoto-Mogami Y, Koizumi S, Tsuda M, Ohsawa K, Kohsaka S, Inoue K (September 2001). "Mechanisms underlying extracellular ATP-evoked interleukin-6 release in mouse microglial cell line, MG-5". Journal of Neurochemistry. 78 (6): 1339–49. doi:10.1046/j.1471-4159.2001.00514.x. PMID 11579142.
37. Hide I, Tanaka M, Inoue A, Nakajima K, Kohsaka S, Inoue K, Nakata Y (September 2000). "Extracellular ATP triggers tumor necrosis factor-alpha release from rat microglia". Journal of Neurochemistry. 75 (3): 965–72. doi:10.1046/j.1471-4159.2000.0750965.x. PMID 10936177.
38. Shiratori M, Tozaki-Saitoh H, Yoshitake M, Tsuda M, Inoue K (August 2010). "P2X7 receptor activation induces CXCL2 production in microglia through NFAT and PKC/MAPK pathways". Journal of Neurochemistry. 114 (3): 810–9. doi:10.1111/j.1471-4159.2010.06809.x. PMID 20477948.
39. Kataoka A, Tozaki-Saitoh H, Koga Y, Tsuda M, Inoue K (January 2009). "Activation of P2X7 receptors induces CCL3 production in microglial cells through transcription factor NFAT". Journal of Neurochemistry. 108 (1): 115–25. doi:10.1111/j.1471-4159.2008.05744.x. PMID 19014371.
40. Gartland A, Skarratt KK, Hocking LJ, Parsons C, Stokes L, Jørgensen NR, et al. (May 2012). "Polymorphisms in the P2X7 receptor gene are associated with low lumbar spine bone mineral density and accelerated bone loss in post-menopausal women". European Journal of Human Genetics. 20 (5): 559–64. doi:10.1038/ejhg.2011.245. PMC 3330223. PMID 22234152.
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Further reading

• Gartland A, Buckley KA, Hipskind RA, Bowler WB, Gallagher JA (2003). "P2 receptors in bone--modulation of osteoclast formation and activity via P2X7 activation". Critical Reviews in Eukaryotic Gene Expression. 13 (2–4): 237–42. doi:10.1615/CritRevEukaryotGeneExpr.v13.i24.150. PMID 14696970.
• Gartland A, Buckley KA, Bowler WB, Gallagher JA (October 2003). "Blockade of the pore-forming P2X7 receptor inhibits formation of multinucleated human osteoclasts in vitro". Calcified Tissue International. 73 (4): 361–9. doi:10.1007/s00223-002-2098-y. PMID 12874700. S2CID 23793221.
• Bowler WB, Buckley KA, Gartland A, Hipskind RA, Bilbe G, Gallagher JA (May 2001). "Extracellular nucleotide signaling: a mechanism for integrating local and systemic responses in the activation of bone remodeling". Bone. 28 (5): 507–12. doi:10.1016/S8756-3282(01)00430-6. PMID 11344050.
• Gartland A, Hipskind RA, Gallagher JA, Bowler WB (May 2001). "Expression of a P2X7 receptor by a subpopulation of human osteoblasts". Journal of Bone and Mineral Research. 16 (5): 846–56. doi:10.1359/jbmr.2001.16.5.846. PMID 11341329.
• Gartland A, Buckley KA, Hipskind RA, Perry MJ, Tobias JH, Buell G, et al. (2003). "Multinucleated osteoclast formation in vivo and in vitro by P2X7 receptor-deficient mice". Critical Reviews in Eukaryotic Gene Expression. 13 (2–4): 243–53. doi:10.1615/CritRevEukaryotGeneExpr.v13.i24.160. PMID 14696971.
• Maruyama K, Sugano S (January 1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. doi:10.1016/0378-1119(94)90802-8. PMID 8125298.
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K, Suyama A, Sugano S (October 1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. doi:10.1016/S0378-1119(97)00411-3. PMID 9373149.
• Gu BJ, Zhang W, Worthington RA, Sluyter R, Dao-Ung P, Petrou S, et al. (April 2001). "A Glu-496 to Ala polymorphism leads to loss of function of the human P2X7 receptor". The Journal of Biological Chemistry. 276 (14): 11135–42. doi:10.1074/jbc.M010353200. PMID 11150303.
• Kim M, Jiang LH, Wilson HL, North RA, Surprenant A (November 2001). "Proteomic and functional evidence for a P2X7 receptor signalling complex". The EMBO Journal. 20 (22): 6347–58. doi:10.1093/emboj/20.22.6347. PMC 125721. PMID 11707406.
• Worthington RA, Smart ML, Gu BJ, Williams DA, Petrou S, Wiley JS, Barden JA (February 2002). "Point mutations confer loss of ATP-induced human P2X(7) receptor function". FEBS Letters. 512 (1–3): 43–6. doi:10.1016/S0014-5793(01)03311-7. PMID 11852049.
• Wiley JS, Dao-Ung LP, Gu BJ, Sluyter R, Shemon AN, Li C, et al. (March 2002). "A loss-of-function polymorphic mutation in the cytolytic P2X7 receptor gene and chronic lymphocytic leukaemia: a molecular study". Lancet. 359 (9312): 1114–9. doi:10.1016/S0140-6736(02)08156-4. PMID 11943260. S2CID 6019286.
• Wilson HL, Wilson SA, Surprenant A, North RA (September 2002). "Epithelial membrane proteins induce membrane blebbing and interact with the P2X7 receptor C terminus". The Journal of Biological Chemistry. 277 (37): 34017–23. doi:10.1074/jbc.M205120200. PMID 12107182.
• Atkinson L, Milligan CJ, Buckley NJ, Deuchars J (November 2002). "An ATP-gated ion channel at the cell nucleus". Nature. 420 (6911): 42. doi:10.1038/420042a. PMID 12422208. S2CID 4313025.
• Sluyter R, Wiley JS (December 2002). "Extracellular adenosine 5'-triphosphate induces a loss of CD23 from human dendritic cells via activation of P2X7 receptors". International Immunology. 14 (12): 1415–21. doi:10.1093/intimm/dxf111. PMID 12456589.
• Strausberg RL, Feingold EA, Grouse LH, Derge JG, Klausner RD, Collins FS, et al. (December 2002). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proceedings of the National Academy of Sciences of the United States of America. 99 (26): 16899–903. Bibcode:2002PNAS...9916899M. doi:10.1073/pnas.242603899. PMC 139241. PMID 12477932.
• Wiley JS, Dao-Ung LP, Li C, Shemon AN, Gu BJ, Smart ML, et al. (May 2003). "An Ile-568 to Asn polymorphism prevents normal trafficking and function of the human P2X7 receptor". The Journal of Biological Chemistry. 278 (19): 17108–13. doi:10.1074/jbc.M212759200. PMID 12586825.
• Barden JA, Sluyter R, Gu BJ, Wiley JS (March 2003). "Specific detection of non-functional human P2X(7) receptors in HEK293 cells and B-lymphocytes". FEBS Letters. 538 (1–3): 159–62. doi:10.1016/S0014-5793(03)00172-8. PMID 12633871.
• Verhoef PA, Estacion M, Schilling W, Dubyak GR (June 2003). "P2X7 receptor-dependent blebbing and the activation of Rho-effector kinases, caspases, and IL-1 beta release". Journal of Immunology. 170 (11): 5728–38. doi:10.4049/jimmunol.170.11.5728. PMID 12759456.
• Greig AV, Linge C, Terenghi G, McGrouther DA, Burnstock G (June 2003). "Purinergic receptors are part of a functional signaling system for proliferation and differentiation of human epidermal keratinocytes". The Journal of Investigative Dermatology. 120 (6): 1007–15. doi:10.1046/j.1523-1747.2003.12261.x. PMID 12787128.
• Denlinger LC, Sommer JA, Parker K, Gudipaty L, Fisette PL, Watters JW, et al. (August 2003). "Mutation of a dibasic amino acid motif within the C terminus of the P2X7 nucleotide receptor results in trafficking defects and impaired function". Journal of Immunology. 171 (3): 1304–11. doi:10.4049/jimmunol.171.3.1304. PMID 12874219.

External links

• P2RX7+protein,+human at the US National Library of Medicine Medical Subject Headings (MeSH)

This article incorporates text from the United States National Library of Medicine, which is in the public domain.