P2RX4

Purinergic receptor P2X, ligand-gated ion channel, 4
Identifiers
Symbols	P2RX4 ; P2X4; P2X4R
External IDs	Template:OMIM5 Template:MGI HomoloGene: 1923
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO
RNA expression pattern
File:PBB GE P2RX4 204088 at tn.png
More reference expression data
Orthologs
Template:GNF Ortholog box
Species	Human	Mouse
Entrez	n/a	n/a
Ensembl	n/a	n/a
UniProt	n/a	n/a
RefSeq (mRNA)	n/a	n/a
RefSeq (protein)	n/a	n/a
Location (UCSC)	n/a	n/a
PubMed search	n/a	n/a

Purinergic receptor P2X, ligand-gated ion channel, 4, also known as P2RX4, is a human gene.

The product of this gene belongs to the family of purinoceptors for ATP. This receptor functions as a ligand-gated ion channel with high calcium permeability. The main pharmacological distinction between the members of the purinoceptor family is the relative sensitivity to the antagonists suramin and PPADS. The product of this gene has the lowest sensitivity for these antagonists. Multiple alternatively spliced transcript variants have been identified for this gene although their full-length natures have not been determined.

See also

• P2X receptor

Further reading

• North RA (2002). "Molecular physiology of P2X receptors". Physiol. Rev. 82 (4): 1013–67. doi:10.1152/physrev.00015.2002. PMID 12270951.
• Maruyama K, Sugano S (1994). "Oligo-capping: a simple method to replace the cap structure of eukaryotic mRNAs with oligoribonucleotides". Gene. 138 (1–2): 171–4. PMID 8125298.
• Garcia-Guzman M, Soto F, Gomez-Hernandez JM; et al. (1997). "Characterization of recombinant human P2X4 receptor reveals pharmacological differences to the rat homologue". Mol. Pharmacol. 51 (1): 109–18. PMID 9016352.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Garcia-Guzman M, Stühmer W, Soto F (1997). "Molecular characterization and pharmacological properties of the human P2X3 purinoceptor". Brain Res. Mol. Brain Res. 47 (1–2): 59–66. PMID 9221902.CS1 maint: Multiple names: authors list (link)
• Suzuki Y, Yoshitomo-Nakagawa K, Maruyama K; et al. (1997). "Construction and characterization of a full length-enriched and a 5'-end-enriched cDNA library". Gene. 200 (1–2): 149–56. PMID 9373149.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Korenaga R, Yamamoto K, Ohura N; et al. (2001). "Sp1-mediated downregulation of P2X4 receptor gene transcription in endothelial cells exposed to shear stress". Am. J. Physiol. Heart Circ. Physiol. 280 (5): H2214–21. PMID 11299224.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Glass R, Loesch A, Bodin P, Burnstock G (2002). "P2X4 and P2X6 receptors associate with VE-cadherin in human endothelial cells". Cell. Mol. Life Sci. 59 (5): 870–81. PMID 12088286.CS1 maint: Multiple names: authors list (link)
• Strausberg RL, Feingold EA, Grouse LH; et al. (2003). "Generation and initial analysis of more than 15,000 full-length human and mouse cDNA sequences". Proc. Natl. Acad. Sci. U.S.A. 99 (26): 16899–903. doi:10.1073/pnas.242603899. PMID 12477932.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yamamoto K, Sokabe T, Ohura N; et al. (2003). "Endogenously released ATP mediates shear stress-induced Ca2+ influx into pulmonary artery endothelial cells". Am. J. Physiol. Heart Circ. Physiol. 285 (2): H793–803. doi:10.1152/ajpheart.01155.2002. PMID 12714321.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Yeung D, Kharidia R, Brown SC, Górecki DC (2004). "Enhanced expression of the P2X4 receptor in Duchenne muscular dystrophy correlates with macrophage invasion". Neurobiol. Dis. 15 (2): 212–20. doi:10.1016/j.nbd.2003.10.014. PMID 15006691.CS1 maint: Multiple names: authors list (link)
• Yang A, Sonin D, Jones L; et al. (2004). "A beneficial role of cardiac P2X4 receptors in heart failure: rescue of the calsequestrin overexpression model of cardiomyopathy". Am. J. Physiol. Heart Circ. Physiol. 287 (3): H1096–103. doi:10.1152/ajpheart.00079.2004. PMID 15130891.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Brown DA, Bruce JI, Straub SV, Yule DI (2004). "cAMP potentiates ATP-evoked calcium signaling in human parotid acinar cells". J. Biol. Chem. 279 (38): 39485–94. doi:10.1074/jbc.M406201200. PMID 15262999.CS1 maint: Multiple names: authors list (link)
• Fountain SJ, North RA (2006). "A C-terminal lysine that controls human P2X4 receptor desensitization". J. Biol. Chem. 281 (22): 15044–9. doi:10.1074/jbc.M600442200. PMID 16533808.
• Jelínková I, Yan Z, Liang Z; et al. (2006). "Identification of P2X4 receptor-specific residues contributing to the ivermectin effects on channel deactivation". Biochem. Biophys. Res. Commun. 349 (2): 619–25. doi:10.1016/j.bbrc.2006.08.084. PMID 16949036.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Solini A, Santini E, Chimenti D; et al. (2007). "Multiple P2X receptors are involved in the modulation of apoptosis in human mesangial cells: evidence for a role of P2X4". Am. J. Physiol. Renal Physiol. 292 (5): F1537–47. doi:10.1152/ajprenal.00440.2006. PMID 17264311.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

External links

• P2RX4+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.