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Gene Review

Aqp2  -  aquaporin 2

Mus musculus

Synonyms: ADH water channel, AQP-2, AQP-CD, Aquaporin-2, Aquaporin-CD, ...
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Disease relevance of Aqp2


High impact information on Aqp2

  • Western blot analysis and immunoelectron microscopic studies showed that the loss of functional V2Rs had no significant effect on the basal expression levels of aquaporin-2 and the bumetanide-sensitive Na-K-2Cl cotransporter (BSC-1) [5].
  • The C-T change led to the substitution of a Ser (S256) by a Leu in the cytoplasmic tail of the Aqp2 protein, preventing its phosphorylation at S256 and the subsequent accumulation of Aqp2 on the apical membrane of the collecting duct principal cells [6].
  • Here, we describe the identification of a single base pair change in aquaporin-2 (Aqp2) in cph mutants through genetic linkage mapping [6].
  • The interference with normal trafficking of Aqp2 by this mutation resulted in a severe urine concentration defect. cph homozygotes demonstrated polydipsia and produced a copious amount of hypotonic urine [6].
  • Immunofluorescence of collecting duct cells in the AD-NDI mouse revealed that the mutant AQP2 was missorted to the basolateral instead of apical plasma membrane [4].

Chemical compound and disease context of Aqp2


Biological context of Aqp2

  • Sequence comparison of the Aqp2 cDNA with a 5.5-kb mouse genomic DNA indicated three introns (lengths 2.4, 0.9, and 0.6 kb) separating four exons with boundaries at amino acids 120, 175, and 202 [8].
  • This study has revealed the genetic basis for the classical cph mutation and has provided direct genetic evidence that S256 in Aqp2 is indispensable for the apical accumulation, but not the general glycosylation or membrane association, of Aqp2 [6].
  • AQP2 is the vasopressin-regulated water channel that is important in hereditary and acquired diseases affecting urine-concentrating ability [9].
  • During normal water intake, urinary osmolality (Uosm), plasma Na concentration, urine volume, and renal aquaporin-2 (AQP2) levels were unchanged, but plasma AVP concentration was reduced in CD ET-1 KO animals [10].
  • METHODS: Various fragments of the 5'-flanking region of the murine AQP-2 gene up to -9.5 kb were cloned into a luciferase (Luc) reporter plasmid, and they were transiently transfected into Madin-Darby canine kidney cells [11].

Anatomical context of Aqp2

  • Expression in Xenopus oocytes indicated that Aqp2 encoded a mercurial-sensitive, water-selective channel [8].
  • STUDY DESIGN: A systematic immunohistochemical study of Aqp2 protein expression was performed on embryonic mouse inner ears ranging from embryonic day 10 (otocyst stage) to embryonic day 18 (just before birth) [12].
  • During early cochlear duct formation (embryonic days 12 and 13), expression of Aqp2 is homogeneous; later, it becomes restricted to specific regions of the endolymphatic compartment (embryonic days 15 and 18) [12].
  • Endolymphatic duct and sac and stria vascularis expression of Aqp2 was noted to occur fairly late during development but demonstrated a distinct pattern of immunolabeling [12].
  • Previous in vitro experiments using renal cell lines suggest recessive Aqp2 mutations result in improper trafficking of the mutant water pore [2].

Associations of Aqp2 with chemical compounds


Other interactions of Aqp2


Analytical, diagnostic and therapeutic context of Aqp2

  • Northern blot analysis showed a single 1.7-kb Aqp2 transcript expressed only in kidney (medulla > cortex); transcript expression was increased approximately 20-fold in 48-h water-deprived mice [8].
  • Genomic Southern blot analysis revealed a single-copy Aqp2 gene [8].
  • Along the collecting duct, the induction and subapical to plasma membrane translocation of the aquaporin-2 water channel in WD EP(1)(-/-) mice appeared equivalent to that of WD WT mice as determined by quantitative RT-PCR and immunohistochemistry [17].
  • Combined RNase protection assay, Western blot, and immunofluorescence analyses revealed that physiological concentrations of AVP added to the basal side, but not to the apical side, of cells grown on filters induced both AQP2 mRNA and apical protein expression [15].
  • Chromatin immunoprecipitation assays demonstrated that the endogenous AQP-2 promoter was occupied by TAp73 in a developmentally regulated manner [16].


  1. Mouse model of inducible nephrogenic diabetes insipidus produced by floxed aquaporin-2 gene deletion. Yang, B., Zhao, D., Qian, L., Verkman, A.S. Am. J. Physiol. Renal Physiol. (2006) [Pubmed]
  2. Diabetes insipidus in mice with a mutation in aquaporin-2. Lloyd, D.J., Hall, F.W., Tarantino, L.M., Gekakis, N. PLoS Genet. (2005) [Pubmed]
  3. Physiology and pathophysiology of renal aquaporins. Kwon, T.H., Hager, H., Nejsum, L.N., Andersen, M.L., Frøkiaer, J., Nielsen, S. Semin. Nephrol. (2001) [Pubmed]
  4. Pathogenesis and treatment of autosomal-dominant nephrogenic diabetes insipidus caused by an aquaporin 2 mutation. Sohara, E., Rai, T., Yang, S.S., Uchida, K., Nitta, K., Horita, S., Ohno, M., Harada, A., Sasaki, S., Uchida, S. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  5. Generation and phenotype of mice harboring a nonsense mutation in the V2 vasopressin receptor gene. Yun, J., Schöneberg, T., Liu, J., Schulz, A., Ecelbarger, C.A., Promeneur, D., Nielsen, S., Sheng, H., Grinberg, A., Deng, C., Wess, J. J. Clin. Invest. (2000) [Pubmed]
  6. Congenital progressive hydronephrosis (cph) is caused by an S256L mutation in aquaporin-2 that affects its phosphorylation and apical membrane accumulation. McDill, B.W., Li, S.Z., Kovach, P.A., Ding, L., Chen, F. Proc. Natl. Acad. Sci. U.S.A. (2006) [Pubmed]
  7. A mouse model to test the in vivo efficacy of chemical chaperones. Bai, C., Biwersi, J., Verkman, A.S., Matthay, M.A. Journal of pharmacological and toxicological methods. (1998) [Pubmed]
  8. cDNA and genomic cloning of mouse aquaporin-2: functional analysis of an orthologous mutant causing nephrogenic diabetes insipidus. Yang, B., Ma, T., Xu, Z., Verkman, A.S. Genomics (1999) [Pubmed]
  9. Lessons on renal physiology from transgenic mice lacking aquaporin water channels. Verkman, A.S. J. Am. Soc. Nephrol. (1999) [Pubmed]
  10. Collecting duct-specific knockout of endothelin-1 alters vasopressin regulation of urine osmolality. Ge, Y., Ahn, D., Stricklett, P.K., Hughes, A.K., Yanagisawa, M., Verbalis, J.G., Kohan, D.E. Am. J. Physiol. Renal Physiol. (2005) [Pubmed]
  11. Hypertonicity regulates the aquaporin-2 promoter independently of arginine vasopressin. Kasono, K., Saito, T., Saito, T., Tamemoto, H., Yanagidate, C., Uchida, S., Kawakami, M., Sasaki, S., Ishikawa, S.E. Nephrol. Dial. Transplant. (2005) [Pubmed]
  12. Developmental expression of aquaporin 2 in the mouse inner ear. Merves, M., Bobbitt, B., Parker, K., Kishore, B.K., Choo, D. Laryngoscope (2000) [Pubmed]
  13. Posttranscriptional control of aquaporin-2 abundance by vasopressin in renal collecting duct principal cells. Hasler, U., Nielsen, S., Féraille, E., Martin, P.Y. Am. J. Physiol. Renal Physiol. (2006) [Pubmed]
  14. Dual influence of aldosterone on AQP2 expression in cultured renal collecting duct principal cells. Hasler, U., Mordasini, D., Bianchi, M., Vandewalle, A., Féraille, E., Martin, P.Y. J. Biol. Chem. (2003) [Pubmed]
  15. Long term regulation of aquaporin-2 expression in vasopressin-responsive renal collecting duct principal cells. Hasler, U., Mordasini, D., Bens, M., Bianchi, M., Cluzeaud, F., Rousselot, M., Vandewalle, A., Feraille, E., Martin, P.Y. J. Biol. Chem. (2002) [Pubmed]
  16. Spatiotemporal switch from DeltaNp73 to TAp73 isoforms during nephrogenesis: impact on differentiation gene expression. Saifudeen, Z., Diavolitsis, V., Stefkova, J., Dipp, S., Fan, H., El-Dahr, S.S. J. Biol. Chem. (2005) [Pubmed]
  17. Urine concentrating defect in prostaglandin EP1-deficient mice. Kennedy, C.R., Xiong, H., Rahal, S., Vanderluit, J., Slack, R.S., Zhang, Y., Guan, Y., Breyer, M.D., Hébert, R.L. Am. J. Physiol. Renal Physiol. (2007) [Pubmed]
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