Aquaporin 1

Aquaporin 1

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).

section_title =
summary_text = 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. [cite web | title = Entrez Gene: AQP1 aquaporin 1 (Colton blood group)| url =| accessdate = ]

ee also

* Aquaporin
* Colton antigen system


Further reading

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

External links


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