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Aquaporin 2




Aquaporin 2 (collecting duct)
Identifiers
Symbol(s) AQP2; AQP-CD; MGC34501; WCH-CD
External IDs OMIM: 107777 MGI: 1096865 Homologene: 20137
RNA expression pattern

More reference expression data

Orthologs
Human Mouse
Entrez 359 11827
Ensembl ENSG00000167580 ENSMUSG00000023013
Uniprot P41181 Q3UQD4
Refseq NM_000486 (mRNA)
NP_000477 (protein) 		NM_009699 (mRNA)
NP_033829 (protein)
Location Chr 12: 48.63 - 48.64 Mb Chr 15: 99.41 - 99.41 Mb
Pubmed search [1] [2]

AQP2 is found in the apical cell membranes of the kidney's collecting duct principal cells and in intracellular vesicles located throughout the cell.

Contents

Regulation

It is the only aquaporin regulated by vasopressin.[1]

This aquaporin is regulated in two ways by the peptide hormone vasopressin:

  • short-term regulation (minutes) through trafficking of AQP2 vesicles to the apical region where they fuse with the apical plasma membrane
  • long-term regulation (days) through an increase in AQP2 gene expression.

Clinical significance

Mutations in this channel are associated with nephrogenic diabetes insipidus, which can be either autosomal dominant or recessive.

Lithium, which is often used to treat bipolar disorder, can cause acquired diabetes insipidus by decreasing the expression of the AQP2 gene. This can result in debilitating increases in the rate of urine production.

The expression of the AQP2 gene is increased during conditions associated with water retention such as pregnancy and congestive heart failure.

References

  1. ^ Dibas AI, Mia AJ, Yorio T (1998). "Aquaporins (water channels): role in vasopressin-activated water transport". Proc. Soc. Exp. Biol. Med. 219 (3): 183–99. PMID 9824541.

Further reading

  • Bichet DG (2006). "Nephrogenic diabetes insipidus.". Advances in chronic kidney disease 13 (2): 96-104. doi:10.1053/j.ackd.2006.01.006. PMID 16580609.
  • Robben JH, Knoers NV, Deen PM (2006). "Cell biological aspects of the vasopressin type-2 receptor and aquaporin 2 water channel in nephrogenic diabetes insipidus.". Am. J. Physiol. Renal Physiol. 291 (2): F257-70. doi:10.1152/ajprenal.00491.2005. PMID 16825342.
  • Sasaki S, Fushimi K, Saito H, et al. (1994). "Cloning, characterization, and chromosomal mapping of human aquaporin of collecting duct.". J. Clin. Invest. 93 (3): 1250-6. PMID 7510718.
  • Deen PM, Weghuis DO, Sinke RJ, et al. (1994). "Assignment of the human gene for the water channel of renal collecting duct Aquaporin 2 (AQP2) to chromosome 12 region q12-->q13.". Cytogenet. Cell Genet. 66 (4): 260-2. PMID 7512890.
  • Uchida S, Sasaki S, Fushimi K, Marumo F (1994). "Isolation of human aquaporin-CD gene.". J. Biol. Chem. 269 (38): 23451-5. PMID 7522228.
  • van Lieburg AF, Verdijk MA, Knoers VV, et al. (1994). "Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene.". Am. J. Hum. Genet. 55 (4): 648-52. PMID 7524315.
  • Saito F, Sasaki S, Chepelinsky AB, et al. (1994). "Human AQP2 and MIP genes, two members of the MIP family, map within chromosome band 12q13 on the basis of two-color FISH.". Cytogenet. Cell Genet. 68 (1-2): 45-8. PMID 7525161.
  • Nielsen S, Chou CL, Marples D, et al. (1995). "Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane.". Proc. Natl. Acad. Sci. U.S.A. 92 (4): 1013-7. PMID 7532304.
  • 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.
  • Deen PM, Verdijk MA, Knoers NV, et al. (1994). "Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine.". Science 264 (5155): 92-5. PMID 8140421.
  • Oksche A, Möller A, Dickson J, et al. (1996). "Two novel mutations in the aquaporin-2 and the vasopressin V2 receptor genes in patients with congenital nephrogenic diabetes insipidus.". Hum. Genet. 98 (5): 587-9. PMID 8882880.
  • Mulders SM, Knoers NV, Van Lieburg AF, et al. (1997). "New mutations in the AQP2 gene in nephrogenic diabetes insipidus resulting in functional but misrouted water channels.". J. Am. Soc. Nephrol. 8 (2): 242-8. PMID 9048343.
  • Ma T, Yang B, Umenishi F, Verkman AS (1997). "Closely spaced tandem arrangement of AQP2, AQP5, and AQP6 genes in a 27-kilobase segment at chromosome locus 12q13.". Genomics 43 (3): 387-9. doi:10.1006/geno.1997.4836. PMID 9268644.
  • Canfield MC, Tamarappoo BK, Moses AM, et al. (1998). "Identification and characterization of aquaporin-2 water channel mutations causing nephrogenic diabetes insipidus with partial vasopressin response.". Hum. Mol. Genet. 6 (11): 1865-71. PMID 9302264.
  • 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.
  • Vargas-Poussou R, Forestier L, Dautzenberg MD, et al. (1998). "Mutations in the vasopressin V2 receptor and aquaporin-2 genes in 12 families with congenital nephrogenic diabetes insipidus.". J. Am. Soc. Nephrol. 8 (12): 1855-62. PMID 9402087.
  • Kuwahara M (1998). "Aquaporin-2, a vasopressin-sensitive water channel, and nephrogenic diabetes insipidus.". Intern. Med. 37 (2): 215-7. PMID 9550615.
  • Mulders SM, Bichet DG, Rijss JP, et al. (1998). "An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex.". J. Clin. Invest. 102 (1): 57-66. PMID 9649557.
  • Goji K, Kuwahara M, Gu Y, et al. (1998). "Novel mutations in aquaporin-2 gene in female siblings with nephrogenic diabetes insipidus: evidence of disrupted water channel function.". J. Clin. Endocrinol. Metab. 83 (9): 3205-9. PMID 9745427.
  • Saito T, Ishikawa S, Ito T, et al. (1999). "Urinary excretion of aquaporin-2 water channel differentiates psychogenic polydipsia from central diabetes insipidus.". J. Clin. Endocrinol. Metab. 84 (6): 2235-7. PMID 10372737.


v • d • e
Membrane transport protein: ion channels
Ca2+: Calcium channelVoltage-dependent calcium channel (L-type/Cavα(1.1, 1.2, 1.3, 1.4), N-type, P-type/Cavα(2.1), Q-type, R-type, T-type, β-subunits (β1, β2, β4), γ-subunits (γ2) • Inositol triphosphate receptor • Ryanodine receptor • Cation channels of sperm • Two-pore channel
Na+: Sodium channelNavα (1.1, 1.2, 1.4, 1.5, 1.7, 1.9) • Navβ (1, 3, 4) • Epithelial sodium channel
K+: Potassium channelVoltage-gated (Kvα (1.1, 1.2, 1.3, 1.4, 1.5, 2.1, 4.2, 4.3, 7.1, 7.2, 7.3, 7.4, 10.1, 11.1/hERG) • Kvβ (1, 2), Shaker gene, KCNE1) • Calcium-activated (BK channel, SK channel, SK3) • Inward-rectifier Kir (1.1, 2.1, 2.2, 2.3, 3.1, 3.2, 3.4, 4.1, 4.2, 6.1, 6.2)) • Tandem pore domain K2P (1, 2, 3, 4, 6, 9)
Cl-: Chloride channelCystic fibrosis transmembrane conductance regulator
PorinAquaporin (1, 2, 3, 4) • Voltage-dependent anion channel (1)
Cations: TRPTRPA (1) • TRPC (1, 2, 3, 4, 4AP, 5, 6, 7) • TRPM (1, 2, 3, 4, 5, 6, 7, 8) • TRPML (Mucolipin-1) • TRPP (1, 2)• TRPV (1, 2, 3, 4, 5, 6)
Other/generalVoltage-gated ion channel • Ligand-gated ion channel • Cyclic nucleotide-gated ion channel (α1, α3, β3, H1, H2, H4) • Stretch-activated ion channel
 
This article is licensed under the GNU Free Documentation License. It uses material from the Wikipedia article "Aquaporin_2". A list of authors is available in Wikipedia.
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