Aquaporin 1

Aquaporin 1 (Colton blood group)
Identifiers
Symbols	AQP1 ; AQP-CHIP; CHIP28; CO; MGC26324
External IDs	Template:OMIM5 Template:MGI HomoloGene: 68051
Gene ontology Molecular function Template:GNF GO Template:GNF GO Template:GNF GO Cellular component Template:GNF GO Template:GNF GO Template:GNF GO Template:GNF GO Biological process Template:GNF GO Template:GNF GO Template:GNF GO
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

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Editor-In-Chief: C. Michael Gibson, M.S., M.D. [1]

Overview

AQP1 is a widely expressed water channel, whose physiological function has been most thoroughly characterized in the kidney.

It is found in the basolateral and apical plasma membranes of the proximal tubules, the descending limb of the loop of Henle, and in the descending portion of the vasa recta.

Additionally, it is found in red blood cells, vascular endothelium, the gastrointestinal tract, sweat glands, and lungs.

It is not regulated by vasopressin (ADH).

Aquaporins are a family of small integral membrane proteins related to the major intrinsic protein (MIP or AQP0). This gene encodes an aquaporin which functions as a molecular water channel protein. It is a homotetramer with 6 bilayer spanning domains and N-glycosylation sites. The protein physically resembles channel proteins and is abundant in erythrocytes and renal tubes. The gene encoding this aquaporin is a possible candidate for disorders involving imbalance in ocular fluid movement.

See also

• Aquaporin
• Colton antigen system

Further reading

• Knepper MA (1994). "The aquaporin family of molecular water channels". Proc. Natl. Acad. Sci. U.S.A. 91 (14): 6255–8. PMID 7517546.
• Borgnia M, Nielsen S, Engel A, Agre P (2000). "Cellular and molecular biology of the aquaporin water channels". Annu. Rev. Biochem. 68: 425–58. doi:10.1146/annurev.biochem.68.1.425. PMID 10872456.CS1 maint: Multiple names: authors list (link)
• Horster M (2001). "Embryonic epithelial membrane transporters". Am. J. Physiol. Renal Physiol. 279 (6): F982–96. PMID 11097616.
• Yool AJ, Weinstein AM (2002). "New roles for old holes: ion channel function in aquaporin-1". News Physiol. Sci. 17: 68–72. PMID 11909995.
• Mitra AK, Ren G, Reddy VS; et al. (2002). "The architecture of a water-selective pore in the lipid bilayer visualized by electron crystallography in vitreous ice". Novartis Found. Symp. 245: 33–46, discussion 46-50, 165–8. PMID 12027013.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Ripoche P, Goossens D, Devuyst O; et al. (2006). "Role of RhAG and AQP1 in NH3 and CO2 gas transport in red cell ghosts: a stopped-flow analysis". Transfusion clinique et biologique : journal de la Société française de transfusion sanguine. 13 (1–2): 117–22. doi:10.1016/j.tracli.2006.03.004. PMID 16574458.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Preston GM, Carroll TP, Guggino WB, Agre P (1992). "Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein". Science. 256 (5055): 385–7. PMID 1373524.CS1 maint: Multiple names: authors list (link)
• Preston GM, Agre P (1992). "Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: member of an ancient channel family". Proc. Natl. Acad. Sci. U.S.A. 88 (24): 11110–4. PMID 1722319.
• Smith BL, Agre P (1991). "Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins". J. Biol. Chem. 266 (10): 6407–15. PMID 2007592.
• Denker BM, Smith BL, Kuhajda FP, Agre P (1988). "Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules". J. Biol. Chem. 263 (30): 15634–42. PMID 3049610.CS1 maint: Multiple names: authors list (link)
• Zelinski T, Kaita H, Lewis M; et al. (1988). "The Colton blood group locus. A linkage analysis". Transfusion. 28 (5): 435–8. PMID 3166547.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Preston GM, Jung JS, Guggino WB, Agre P (1994). "Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis". J. Biol. Chem. 269 (3): 1668–73. PMID 7507481.CS1 maint: Multiple names: authors list (link)
• Skach WR, Shi LB, Calayag MC; et al. (1994). "Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum". J. Cell Biol. 125 (4): 803–15. PMID 7514605.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Li X, Yu H, Koide SS (1994). "The water channel gene in human uterus". Biochem. Mol. Biol. Int. 32 (2): 371–7. PMID 7517253.CS1 maint: Multiple names: authors list (link)
• Walz T, Smith BL, Agre P, Engel A (1994). "The three-dimensional structure of human erythrocyte aquaporin CHIP". EMBO J. 13 (13): 2985–93. PMID 7518771.CS1 maint: Multiple names: authors list (link)
• Preston GM, Smith BL, Zeidel ML; et al. (1994). "Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels". Science. 265 (5178): 1585–7. PMID 7521540.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Smith BL, Preston GM, Spring FA; et al. (1994). "Human red cell aquaporin CHIP. I. Molecular characterization of ABH and Colton blood group antigens". J. Clin. Invest. 94 (3): 1043–9. PMID 7521882.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• van Hoek AN, Wiener MC, Verbavatz JM; et al. (1995). "Purification and structure-function analysis of native, PNGase F-treated, and endo-beta-galactosidase-treated CHIP28 water channels". Biochemistry. 34 (7): 2212–9. PMID 7532004.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)
• Keen TJ, Inglehearn CF, Patel RJ; et al. (1995). "Localization of the aquaporin 1 (AQP1) gene within a YAC contig containing the polymorphic markers D7S632 and D7S526". Genomics. 25 (2): 599–600. PMID 7540589.CS1 maint: Explicit use of et al. (link) CS1 maint: Multiple names: authors list (link)

External links

• Aquaporin+1 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.