Encyclopedia of Signaling Molecules

2018 Edition
| Editors: Sangdun Choi

Aquaporin

  • Roderick Nigel Finn
  • Joan Cerdà
Reference work entry
First Online:
DOI: https://doi.org/10.1007/978-3-319-67199-4_101692
How to cite

Synonyms

 AQP-CD, WCH-CD: aquaporin, water channel of the collecting duct;  AQP-CHIP;  CHIP28: Channel-forming integral protein, 28kD;  Integral membrane protein;  MIP: major intrinsic protein

Historical Background

Water transport across cell membranes is an essential requirement for the biochemistry of life, yet it took more than two centuries of observations and research before transmembrane water channels termed aquaporins were discovered. For much of this time, it was assumed that water transport occurred either via simple diffusion or in certain instances was powered by active processes. As early as the eighteenth century, it was noted that adult frogs and toads absorb water across their ventral skin when dehydrated and placed in water. A century and a quarter later, it was discovered that the increased absorption of water across the skin could be enhanced by the injection of neurohypophysial extract (pituitrin), which was known to have antidiuretic effects in mammals. These...

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References

  1. Abascal F, Irisarri I, Zardoya R. Diversity and evolution of membrane intrinsic proteins. Biochim Biophys Acta. 2014;1840:1468–81.PubMedCrossRefGoogle Scholar
  2. Agre P, Sasaki S, Chrispeels MJ. Aquaporins: a family of water channel proteins. Am J Phys. 1993;265:F461.Google Scholar
  3. Anderberg HI, Danielsen JÅH, Johanson U. Algal MIPs, high diversity and conserved motifs. BMC Evol Biol. 2011;11:110.PubMedPubMedCentralCrossRefGoogle Scholar
  4. Benga G, Popescu O, Pop VI, Holmes RE. p-(Ch1oromercuri) benzenesulfonate binding by membrane proteins and the inhibition of water transport in human erythrocytes. Biochemistry. 1986;25:1535–8.PubMedCrossRefGoogle Scholar
  5. Benoit JB, Hansen IA, Szuter EM, Drake LL, Burnett DL, Attardo GM. Emerging roles of aquaporins in relation to the physiology of blood-feeding arthropods. J Comp Physiol. 2014;184B:811–25.CrossRefGoogle Scholar
  6. Bienert GP, Chaumont F. Aquaporin-facilitated transmembrane diffusion of hydrogen peroxide. Biochim Biophys Acta. 2014;1840:1596–604.PubMedCrossRefGoogle Scholar
  7. Cerdà J, Zapater C, Chauvigné F, Finn RN. Water homeostasis in the fish oocyte: New insights into the role and molecular regulation of a teleost-specific aquaporin. Fish Physiol Biochem. 2013;39: 19–27.PubMedCrossRefGoogle Scholar
  8. Chauvigné F, Boj M, Finn RN, Cerdà J. Mitochondrial aquaporin-8-mediated hydrogen peroxide transport is essential for teleost spermatozoon motility. Sci Rep. 2015;5:7789.PubMedPubMedCentralCrossRefGoogle Scholar
  9. Danielson JÅH, Johanson U. Unexpected complexity of the aquaporin gene family in the moss Physcomitrella patens. BMC Plant Biol. 2008;8:45.PubMedPubMedCentralCrossRefGoogle Scholar
  10. Denker BM, Smith BL, Kuhajda FP, Agre P. Identification, purification, and partial characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J Biol Chem. 1988;263:15634–42.PubMedPubMedCentralGoogle Scholar
  11. Finn RN, Cerdà J. Aquaporin evolution in fishes. Front Physiol. 2011;2:44.PubMedPubMedCentralCrossRefGoogle Scholar
  12. Finn RN, Cerdà J. Evolution and functional diversity of aquaporins. Biol Bull. 2015;229:6–23.PubMedCrossRefGoogle Scholar
  13. Finn RN, Chauvigné F, Hlidberg JB, Cutler C, Cerdà J. The lineage-specific evolution of aquaporin gene clusters facilitated tetrapod terrestrial adaptation. PLoS One. 2014;9(11):e113686.PubMedPubMedCentralCrossRefGoogle Scholar
  14. Finn RN, Chauvigné F, Stavang JA, Belles X, Cerdà J. Insect glycerol transporters evolved by functional co-option and gene replacement. Nature Commun. 2015;6:7814.CrossRefGoogle Scholar
  15. Gorin MB, Yancey SB, Cline J, Revel JP, Horwitz J. The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning. Cell. 1984;39:49–59.PubMedCrossRefGoogle Scholar
  16. Heller H. The effect of neurohypophysial extracts on the water balance of lower vertebrates. Biol Rev. 1945;20:147–58.PubMedCrossRefGoogle Scholar
  17. Hevesy GV, Hofer V, Krogh A. The permeability of the skin of frogs to water as determined by D20 and H2O. Skand Arch Physiol. 1935;72:199–214.CrossRefGoogle Scholar
  18. Koefoed-Johnsen V, Ussing HH. The contributions of diffusion and flow to the passage of D2O through living membranes. Acta Physiol Scand. 1953;28:60–76.PubMedCrossRefGoogle Scholar
  19. Macey RL, Farmer REL. Inhibition of water and solute permeability in human red cells. Biochim Biophys Acta. 1970;211:104–6.PubMedCrossRefGoogle Scholar
  20. Maurel C, Boursiac Y, Luu DT, Santoni V, Shazad Z, Verdoucq L. Aquaporins in plants. Physiol Rev. 2015;95:1321–58.PubMedCrossRefGoogle Scholar
  21. Paganelli CV, Solomon AK. The rate of exchange of tritriated water across the human red cell membrane. J Gen Physiol. 1957;41:259–77.PubMedPubMedCentralCrossRefGoogle Scholar
  22. Pao GM, Wu LF, Johnson KD, Höfte H, Chrispeels MJ, Sweet G, Sandal NN, Saier Jr MH. Evolution of the MIP family of integral membrane transport proteins. Mol Microbiol. 1991;5:33–7.PubMedCrossRefGoogle Scholar
  23. Preston GM, Carroll TP, Guggino WB, Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 1992;256:385–7.PubMedCrossRefGoogle Scholar
  24. Sjöhamn J, Hedfalk K. Unraveling aquaporin interaction partners. Biochim Biophys Acta. 2014;1840:1614–23.PubMedCrossRefGoogle Scholar
  25. Suzuki M, Shibata Y, Ogushi Y, Okada R. Molecular machinery for vasotocin-dependent transepithelial water movement in amphibians: aquaporins and evolution. Biol Bull. 2015;229:109–19.PubMedCrossRefGoogle Scholar
  26. Törnroth-Horsefield S, Hedfalk K, Fisher G, Lindkvist-Petersson K, Neutze R. Structural mechanism of plant aquaporin gating. FEBS Lett. 2010;584:2580–8.PubMedCrossRefGoogle Scholar
  27. Verkman AS, Anderson MO, Papadopoulis MC. Aquaporins: important but elusive drug targets. Nat Rev Drug Discov. 2014;13:259–77.PubMedPubMedCentralCrossRefGoogle Scholar
  28. Wspalz T, Fujiyoshi Y, Engel A. The AQP structure and functional implications. In: Beitz E, (ed). Aquaporins. Handb Exp Pharmacol. 2009; 190:31–56.Google Scholar

Copyright information

© Springer International Publishing AG 2018

Authors and Affiliations

  1. 1.Department of Biology, Bergen High Technology CentreUniversity of BergenBergenNorway
  2. 2.Institute of Marine ResearchBergenNorway
  3. 3.Institut de Recerca i Tecnologia Agroalimentàries (IRTA)Consejo Superior de Investigaciones Científicas (CSIC)BarcelonaSpain
  4. 4.Institut de Recerca i Tecnologia Agroalimentàries (IRTA)-Institut de Ciéncies del MarConsejo Superior de Investigaciones Científicas (CSIC)BarcelonaSpain