TRPV5
Transient receptor potential cation channel subfamily V member 5 is a protein that in humans is encoded by the TRPV5 gene.[5][6][7]
TRPV5 is mainly expressed in kidney epithelial cells, where it plays an important role in the reabsorption of Ca2+.[8] Genetic deletion of TRPV5 in mice leads to Ca2+ loss in the urine, and consequentual hyperparathyroidism, and bone loss.[9]
Function
This gene is a member of the transient receptor family and the TRPV subfamily. The calcium-selective channel, TRPV5, encoded by this gene has 6 transmembrane-spanning domains, multiple potential phosphorylation sites, an N-linked glycosylation site, and 5 ANK repeats. This protein forms homotetramers or heterotetramers and is activated by a low internal calcium level.[10]
Interactions
See also
References
- 1 2 3 ENSG00000127412 GRCh38: Ensembl release 89: ENSG00000274348, ENSG00000127412 - Ensembl, May 2017
- 1 2 3 GRCm38: Ensembl release 89: ENSMUSG00000036899 - Ensembl, May 2017
- ↑ "Human PubMed Reference:".
- ↑ "Mouse PubMed Reference:".
- ↑ Müller D, Hoenderop JG, Merkx GF, van Os CH, Bindels RJ (Sep 2000). "Gene structure and chromosomal mapping of human epithelial calcium channel". Biochem. Biophys. Res. Commun. 275 (1): 47–52. doi:10.1006/bbrc.2000.3227. PMID 10944439.
- ↑ Müller D, Hoenderop JG, Meij IC, van den Heuvel LP, Knoers NV, den Hollander AI, Eggert P, García-Nieto V, Claverie-Martín F, Bindels RJ (Nov 2000). "Molecular cloning, tissue distribution, and chromosomal mapping of the human epithelial Ca2+ channel (ECAC1)". Genomics. 67 (1): 48–53. doi:10.1006/geno.2000.6203. PMID 10945469.
- ↑ Clapham DE, Julius D, Montell C, Schultz G (Dec 2005). "International Union of Pharmacology. XLIX. Nomenclature and structure-function relationships of transient receptor potential channels". Pharmacol. Rev. 57 (4): 427–50. doi:10.1124/pr.57.4.6. PMID 16382100.
- ↑ Hoenderop JG, Nilius B, Bindels RJ (2002). "Molecular mechanism of active Ca2+ reabsorption in the distal nephron". Annu. Rev. Physiol. 64: 529–49. doi:10.1146/annurev.physiol.64.081501.155921. PMID 11826278.
- ↑ Hoenderop JG, van Leeuwen JP, van der Eerden BC, Kersten FF, van der Kemp AW, Mérillat AM, Waarsing JH, Rossier BC, Vallon V, Hummler E, Bindels RJ (2003). "Renal Ca2+ wasting, hyperabsorption, and reduced bone thickness in mice lacking TRPV5". J. Clin. Invest. 112 (12): 1906–14. doi:10.1172/JCI19826. PMC 297001. PMID 14679186.
- ↑ "Entrez Gene: TRPV5 transient receptor potential cation channel, subfamily V, member 5".
- ↑ van de Graaf SF, Hoenderop JG, Gkika D, Lamers D, Prenen J, Rescher U, Gerke V, Staub O, Nilius B, Bindels RJ (Apr 2003). "Functional expression of the epithelial Ca(2+) channels (TRPV5 and TRPV6) requires association of the S100A10-annexin 2 complex". EMBO J. 22 (7): 1478–87. doi:10.1093/emboj/cdg162. PMC 152906. PMID 12660155.
Further reading
- Vennekens R, Droogmans G, Nilius B (2001). "Functional properties of the epithelial Ca2+ channel, ECaC". Gen. Physiol. Biophys. 20 (3): 239–53. PMID 11765215.
- Heiner I, Eisfeld J, Lückhoff A (2004). "Role and regulation of TRP channels in neutrophil granulocytes". Cell Calcium. 33 (5–6): 533–40. doi:10.1016/S0143-4160(03)00058-7. PMID 12765698.
- Nijenhuis T, Hoenderop JG, Bindels RJ (2005). "TRPV5 and TRPV6 in Ca(2+) (re)absorption: regulating Ca(2+) entry at the gate". Pflügers Arch. 451 (1): 181–92. doi:10.1007/s00424-005-1430-6. PMID 16044309.
- Mensenkamp AR, Hoenderop JG, Bindels RJ (2007). "TRPV5, the gateway to Ca2+ homeostasis". Handb Exp Pharmacol. Handbook of Experimental Pharmacology. 179 (179): 207–20. doi:10.1007/978-3-540-34891-7_12. ISBN 978-3-540-34889-4. PMID 17217059.
- Schoeber JP, Hoenderop JG, Bindels RJ (2007). "Concerted action of associated proteins in the regulation of TRPV5 and TRPV6". Biochem. Soc. Trans. 35 (Pt 1): 115–9. doi:10.1042/BST0350115. PMID 17233615.
External links
- TRPV5+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.