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Gene Review

Aqp5  -  aquaporin 5

Rattus norvegicus

Synonyms: AQP-5, Aquaporin-5
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Disease relevance of Aqp5


High impact information on Aqp5


Biological context of Aqp5


Anatomical context of Aqp5

  • Under control conditions, >90% of AQP-5 was associated with the apical plasma membrane of acinar and intercalated duct cells, with only rare gold particles associated with intracellular membrane domains [11].
  • However, it remains unknown whether AQP-5 in salivary glands is subject to regulated trafficking in vivo [11].
  • However, the increased salivary secretion was associated with luminal dilation and the appearance of a markedly punctate AQP-5 labeling pattern due to clustering of AQP-5 at the microvilli (especially evident in the parotid gland) after 10 min of drug injection [11].
  • To examine this possibility, we have investigated the subcellular localization of AQP-5 in rat parotid and submandibular glands fixed in vivo under conditions of stimulated or inhibited salivary secretion [11].
  • In the human pancreas, secretion occurs mainly in the intercalated ducts, where the epithelial cells express abundant AQP1 and AQP5 at the apical membrane and AQP1 alone at the basolateral membrane [12].

Associations of Aqp5 with chemical compounds

  • Pilocarpine treatment dramatically increased saliva production but had no discernible effect on AQP-5 distribution [11].
  • No changes in the subcellular localization of AQP-5 were seen in response to epinephrine, atropine, or phentolamine treatment compared with control tissues [11].
  • Furthermore, apical, but not basolateral, application of Hg(2+) significantly reduces the transepithelial osmotic permeability, suggesting that apical AQP1 and AQP5 may contribute significantly to fluid secretion [12].
  • Pretreatment of rat parotid tissue with the NO scavenger 2-(4carboxyphenyl)-4,4,5,5-tetramethyl-imidazoline-1-oxyl-3-oxide potassium inhibited both acetylcholine (ACh)- and pilocarpine-induced increases in AQP5 in the APM [6].
  • BAPTA-AM inhibited the cGMP-induced increase in AQP5 in the APM [6].

Other interactions of Aqp5


Analytical, diagnostic and therapeutic context of Aqp5


  1. Acute renal failure leads to dysregulation of lung salt and water channels. Rabb, H., Wang, Z., Nemoto, T., Hotchkiss, J., Yokota, N., Soleimani, M. Kidney Int. (2003) [Pubmed]
  2. Subcellular distribution of aquaporin 5 in salivary glands in primary Sjögren's syndrome. Beroukas, D., Hiscock, J., Jonsson, R., Waterman, S.A., Gordon, T.P. Lancet (2001) [Pubmed]
  3. Alterations in the expression of the AQP family in cultured rat astrocytes during hypoxia and reoxygenation. Yamamoto, N., Yoneda, K., Asai, K., Sobue, K., Tada, T., Fujita, Y., Katsuya, H., Fujita, M., Aihara, N., Mase, M., Yamada, K., Miura, Y., Kato, T. Brain Res. Mol. Brain Res. (2001) [Pubmed]
  4. Effect of mild hypothermia on the expression of aquaporin family in cultured rat astrocytes under hypoxic condition. Fujita, Y., Yamamoto, N., Sobue, K., Inagaki, M., Ito, H., Arima, H., Morishima, T., Takeuchi, A., Tsuda, T., Katsuya, H., Asai, K. Neurosci. Res. (2003) [Pubmed]
  5. Molecular cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues. Raina, S., Preston, G.M., Guggino, W.B., Agre, P. J. Biol. Chem. (1995) [Pubmed]
  6. The muscarinic acetylcholine receptor-stimulated increase in aquaporin-5 levels in the apical plasma membrane in rat parotid acinar cells is coupled with activation of nitric oxide/cGMP signal transduction. Ishikawa, Y., Iida, H., Ishida, H. Mol. Pharmacol. (2002) [Pubmed]
  7. Divergent expression and localization of aquaporin 5, an exocrine-type water channel, in the submandibular gland of Sprague-Dawley rats. Murdiastuti, K., Miki, O., Yao, C., Parvin, M.N., Kosugi-Tanaka, C., Akamatsu, T., Kanamori, N., Hosoi, K. Pflugers Arch. (2002) [Pubmed]
  8. Keratinocyte growth factor modulates alveolar epithelial cell phenotype in vitro: expression of aquaporin 5. Borok, Z., Lubman, R.L., Danto, S.I., Zhang, X.L., Zabski, S.M., King, L.S., Lee, D.M., Agre, P., Crandall, E.D. Am. J. Respir. Cell Mol. Biol. (1998) [Pubmed]
  9. Subcellular redistribution of AQP5 by vasoactive intestinal polypeptide in the Brunner's gland of the rat duodenum. Parvin, M.N., Kurabuchi, S., Murdiastuti, K., Yao, C., Kosugi-Tanaka, C., Akamatsu, T., Kanamori, N., Hosoi, K. Am. J. Physiol. Gastrointest. Liver Physiol. (2005) [Pubmed]
  10. A naturally occurring point mutation in the rat aquaporin 5 gene, influencing its protein production by and secretion of water from salivary glands. Murdiastuti, K., Purwanti, N., Karabasil, M.R., Li, X., Yao, C., Akamatsu, T., Kanamori, N., Hosoi, K. Am. J. Physiol. Gastrointest. Liver Physiol. (2006) [Pubmed]
  11. Immunolocalization of AQP-5 in rat parotid and submandibular salivary glands after stimulation or inhibition of secretion in vivo. Gresz, V., Kwon, T.H., Gong, H., Agre, P., Steward, M.C., King, L.S., Nielsen, S. Am. J. Physiol. Gastrointest. Liver Physiol. (2004) [Pubmed]
  12. The role of aquaporin water channels in fluid secretion by the exocrine pancreas. Burghardt, B., Nielsen, S., Steward, M.C. J. Membr. Biol. (2006) [Pubmed]
  13. Modulation of pulmonary alveolar type II cell phenotype and communication by extracellular matrix and KGF. Isakson, B.E., Lubman, R.L., Seedorf, G.J., Boitano, S. Am. J. Physiol., Cell Physiol. (2001) [Pubmed]
  14. Involvement of aquaporin-5 water channel in osmoregulation in parotid secretory granules. Matsuki, M., Hashimoto, S., Shimono, M., Murakami, M., Fujita-Yoshigaki, J., Furuyama, S., Sugiya, H. J. Membr. Biol. (2005) [Pubmed]
  15. Polarized distribution of key membrane transport proteins in the rat submandibular gland. He, X., Tse, C.M., Donowitz, M., Alper, S.L., Gabriel, S.E., Baum, B.J. Pflugers Arch. (1997) [Pubmed]
  16. Aquaporins in rat pancreatic interlobular ducts. Ko, S.B., Naruse, S., Kitagawa, M., Ishiguro, H., Furuya, S., Mizuno, N., Wang, Y., Yoshikawa, T., Suzuki, A., Shimano, S., Hayakawa, T. Am. J. Physiol. Gastrointest. Liver Physiol. (2002) [Pubmed]
  17. Identification of AQP5 in lipid rafts and its translocation to apical membranes by activation of M3 mAChRs in interlobular ducts of rat parotid gland. Ishikawa, Y., Yuan, Z., Inoue, N., Skowronski, M.T., Nakae, Y., Shono, M., Cho, G., Yasui, M., Agre, P., Nielsen, S. Am. J. Physiol., Cell Physiol. (2005) [Pubmed]
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