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. 2004 Jan 7;51:1–38. doi: 10.1016/S1063-5823(01)51003-0

Chapter 1 discovery of the aquaporins and their impact on basic and clinical physiology

Peter Agre 1, Mario J Borgnia 1, Masato Yasui 1, John D Neely 1, Jennifer Carbrey 1, David Kozono 1, Eric Beitz 1, Jason Hoffert 1, Virginia Leitch 1, Landon S King 1
PMCID: PMC7129575

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References

  1. Agre P. Aquaporin nomenclature workshop: Mammalian aquaporins. Biol. Cell. 1997;89:321–329. [PubMed] [Google Scholar]
  2. Agre P. Vol. 95. 1998. Aquaporin null phenotypes: The importance of classical physiology; pp. 9061–9063. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  3. Agre P., Cartron J.P., editors. Protein Blood Group Antigens of the Human Red Cell. Johns Hopkins University Press; Baltimore: 1992. [Google Scholar]
  4. Agre P., Saboori A.M., Asimos A., Smith B.L. Purification and partial characterization of the Mr 30,000 integral membrane protein associated with the erythrocyte Rh(D) antigen. J. Biol. Chem. 1987;262:17497–17503. [PubMed] [Google Scholar]
  5. Agre P., Sasaki S., Chrispeels M.J. Aquaporins, a family of membrane water channels. Am. J. Physiol. 1993;265:F461. doi: 10.1152/ajprenal.1993.265.3.F461. [DOI] [PubMed] [Google Scholar]
  6. Agre E., Lee M.D., Devidas S., Guggino W.B., Sasaki S., Uchida S., Kuwahara M., fushimi K., Marumo F., Verkman A.S., Yang B., Deen P.M.T., Mulders S.M., Kansen S.M., van Os C.H. Aquaporins and ion conductance. Science. 1997;275:1490–1492. [PubMed] [Google Scholar]
  7. Agre P., Bonhivers M., Borgnia M.J. The aquaporins, blueprints for cellular plumbing systems. J. Biol. Chem. 1998;273:14659–14662. doi: 10.1074/jbc.273.24.14659. [DOI] [PubMed] [Google Scholar]
  8. Agre P., Mathai J.C., Smith B.L., Preston G.M. Functional analyses of the aquaporin water channels. Methods Enzymol. 1998;294:550–572. doi: 10.1016/s0076-6879(99)94032-6. [DOI] [PubMed] [Google Scholar]
  9. Anthony T.L., Brooks H.L., Boassa D., Leonov S., Yanochko G.M., Regan T.W., Yool A.J. Cloned human aquaporin-1 is a cyclic GMP gated ion channel. Mol. Pharmacol. 2000;57:576–588. doi: 10.1124/mol.57.3.576. [DOI] [PubMed] [Google Scholar]
  10. Berry V., Francis P.F., Kaushal S., Moore A., Bhattacharya S. Missense mutations in MIP underlie autosomal dominant ‘polymorphic’ and lamellar cataracts linked to 12q. Nat. Genet. 2000;25:15–17. doi: 10.1038/75538. [DOI] [PubMed] [Google Scholar]
  11. Beuron F., Le Caherec F., Guillam M.T., Cavalier A., Garret A., Tassan J.L., Delamarche C., Schultz P., Mallouh V., Rolland J.P., Thomas D. Structural analysis of a MIP family protein from the digestive tract of Cicadella viridis. J. Biol. Chem. 1995;270:17414–17422. doi: 10.1074/jbc.270.29.17414. [DOI] [PubMed] [Google Scholar]
  12. Bichet D.G. Nephrogenic diabetes insipidus. Am. J. Med. 1998;105:431–442. doi: 10.1016/s0002-9343(98)00301-5. [DOI] [PubMed] [Google Scholar]
  13. Bondy C., Chin E., Smith B.L., Preston G.M., Agre P. Vol. 90. 1993. Developmental gene expression and tissue distribution of the CHIP28 water channel protein; pp. 4500–4504. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  14. Bonhivers M., Carbrey J., Gould S.J., Agre P. Aquaporins in Saccharomyces: Genetic and functional distinctions between genetic and wild-type strains. J. Biol. Chem. 1998;273:27565–27572. doi: 10.1074/jbc.273.42.27565. [DOI] [PubMed] [Google Scholar]
  15. Borgnia M., Nielsen S., Engel A., Agre P. Cellular and molecular biology of the aquaporin water channels. Annu. Rev. Biochem. 1999;68:425–458. doi: 10.1146/annurev.biochem.68.1.425. [DOI] [PubMed] [Google Scholar]
  16. Braun T., Philippsen A., Wirtz S., Borgnia M.J., Agre P., Kühlbrandt W., Engel A., Stahlberg H. Projection structure of the glycerol facilitator at 3.5 Å resolution. EMBO Rep. 2000;1:183–189. doi: 10.1093/embo-reports/kvd022. [DOI] [PMC free article] [PubMed] [Google Scholar]
  17. Bron E., Lagree V., Froger A., Rolland J.E., Hubert J.E., Delamarche C., Deschamps S., Pellerin I., Thomas D., Haase W. Oligomerization state of MIP proteins expressed in Xenopus oocyte revealed by freeze-fracture electron-microscopy analysis. J. Struct. Biol. 1999;30:287–296. doi: 10.1006/jsbi.1999.4196. [DOI] [PubMed] [Google Scholar]
  18. Calamita G., Bishai W.R., Preston G.M., Guggino W.B., Agre P. Molecular cloning and characterization of aquaporin Z: A water channel from E. coli. J. Biol. Chem. 1995;270:29063–29066. doi: 10.1074/jbc.270.49.29063. [DOI] [PubMed] [Google Scholar]
  19. Calamita G., Kempf B., Bonhivers M., Bishai W.R., Bremer E., Agre P. Vol. 95. 1998. Regulation of the E. coli. water channel gene, AgpZ; pp. 3627–3631. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  20. Chandy G., Zampighi G.A., Kreman M., Hall J.E. Comparison of the water transporting protperited of MIP and AQP1. J. Membr. Biol. 1997;159:29–39. doi: 10.1007/s002329900266. [DOI] [PubMed] [Google Scholar]
  21. Cheng A., van Hoek A.N., Yeager M., Verkman A.S., Mitra A.K. Three-dimensional organization of a human water channel. Nature. 1997;387:627–630. doi: 10.1038/42517. [DOI] [PubMed] [Google Scholar]
  22. Cowan C.A., Yokoyama N., Bioanci L.M., Henkemeyer M., Fritzsch B. EphB2 guides axons at the midline and is necessary for normal vestibular function. Neuron. 2000;26:417–430. doi: 10.1016/s0896-6273(00)81174-5. [DOI] [PubMed] [Google Scholar]
  23. Dean R.M., Rivers R.L., Zeidel M.L., Roberts D.M. Purification and functional reconstitution of soybean nodulin 26. An aquaporin with glycerol transport properties. Biochemistry. 1999;38:347–353. doi: 10.1021/bi982110c. [DOI] [PubMed] [Google Scholar]
  24. Deen P.M., Verdijk M.A., Knoers N.V. Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. Science. 1994;264:92–95. doi: 10.1126/science.8140421. [DOI] [PubMed] [Google Scholar]
  25. Denker B.M., Smith B.L., Kuhajda F.P., Agre P. Identification, purification, and characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J. Biol. Chem. 1988;263:15634–15642. [PubMed] [Google Scholar]
  26. Ecelbarger C.A., Terns J., Frindt G., Echevarria M., Marples D., Nielsen S., Knepper M.A. Aquaporin-3 water channel localization and regulation in rat kidney. Am. J. Physiol. 1995;269:F663–F672. doi: 10.1152/ajprenal.1995.269.5.F663. [DOI] [PubMed] [Google Scholar]
  27. Echevarria M., Windhager E.E., Tate S.S., Frindt G. Vol. 91. 1994. Cloning and expression of AQP3, a water channel from medullary collecting duct of rat kidney; pp. 10997–11001. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  28. Echevarria M., Windhager E.E., Frindt G. Selectivity of the renal collecting duct water channel aquaporin-3. J. Biol. Chem. 1996;271:25079–25082. doi: 10.1074/jbc.271.41.25079. [DOI] [PubMed] [Google Scholar]
  29. Ehring G.R., Zampighi G., Horwitz J., Bok D., Hall J. Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes. J. Gen. Physiol. 1990;96:631–664. doi: 10.1085/jgp.96.3.631. [DOI] [PMC free article] [PubMed] [Google Scholar]
  30. Finkelstein A. Wiley; New York: 1987. Water Movement through Lipid Bilayers, Pores, and Plasma Membranes. Theory and Reality. [Google Scholar]
  31. Fischbarg J., Kuang K., Vera J.C., Arant S., Silverstein S.C., Loike J., Rosen O.M. Vol. 87. 1990. Glucose transporters serve as water channels; pp. 3244–3247. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  32. Fotiadis D., Hasler L., Müller D.J., Stahlberg H., Kistler J., Engel A. Surface topography of lens MIP (AQP0) supports two functions. J. Mol. Biol. 2000;300:779–789. doi: 10.1006/jmbi.2000.3920. [DOI] [PubMed] [Google Scholar]
  33. Francis P., Chung J.-J., Yasui M., Berry V., Moore A., Wyatt M.K., Wistow G., Bhattacharya S.S., Agre P. Functional impairment of lens aquaporin in two families with dominantly inherited cataract. Human Mol. Genet. 2000;9:2329–2334. doi: 10.1093/oxfordjournals.hmg.a018925. [DOI] [PubMed] [Google Scholar]
  34. Frigeri A., Gropper M., Turck C.W., Verkman A.S. Vol. 92. 1995. Immunolocalization of the mercurialinsensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes; pp. 4328–4331. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  35. Frigeri A., Niechia G.P., Verbavatz J.M., Valenti G., Svelto M. Expression of aquaporin4 in gast-twitch fibers of mammalian skeletal muscle. J. Clin. Invest. 1998;102:695–703. doi: 10.1172/JCI2545. [DOI] [PMC free article] [PubMed] [Google Scholar]
  36. Frokiaer J., Nielsen S. Do aquaporins have a role in nocturnal enuresis? Scan. J. Urol. Nephrol. Suppl. 1997;183:31–32. [PubMed] [Google Scholar]
  37. Frokiaer J., Marples D., Knepper M.A. Bilateral ureteral obstruction downregulates expression of vasopressin-sensitive AQP-2 water channel in rat kidney. Am. J. Physiol. 1996;270:F657–F668. doi: 10.1152/ajprenal.1996.270.4.F657. [DOI] [PubMed] [Google Scholar]
  38. Fushimi K., Uchida S., Hara Y., Hirata Y., Marumo F., Sasai S. Cloning and expression of apical membrane water channel of rat kidney collecting tubule. Nature. 1993;361:549–552. doi: 10.1038/361549a0. [DOI] [PubMed] [Google Scholar]
  39. Gorin M.B., Yancey S.B., Cline J., Revel J.P., Horwitz J. The major intrinsic protein (MIP) of the bovine lens fiber membrane. Cell. 1984;39:49–59. doi: 10.1016/0092-8674(84)90190-9. [DOI] [PubMed] [Google Scholar]
  40. Guerrero F.D., Jones J.T., Mullet J.E. Turgor-responsive gene transcription and RNA levels increase rapidly when pea shoots are wilted. Plant Mol. Biol. 1990;15:11–26. doi: 10.1007/BF00017720. [DOI] [PubMed] [Google Scholar]
  41. Hamann S., Zeuthen T., la Cour M., Nagelhus E., Ottersen O.P., Agre P., Nielsen S. Aquaporins in complex tissues: III. Distribution of aquaporins 1–5 in human and rat eye. Am. J. Physiol. 1998;274:C1332–C1345. doi: 10.1152/ajpcell.1998.274.5.C1332. [DOI] [PubMed] [Google Scholar]
  42. Han Z., Wax M.B., Patil R.V. Regulation of aquaporin-4 water channels by phorbol ester-dependent protein phosphorylation. J. Biol. Chem. 1998;273:6001–6004. doi: 10.1074/jbc.273.11.6001. [DOI] [PubMed] [Google Scholar]
  43. Harris H.W., Hosselet C., Guay-Woodford L., Zeidel M.L. Purification and partial characterization of candidate antidiuretic hormone water channel proteins of Mr 55,000 and 53,000 from toad bladder. J. Biol. Chem. 1992;267:22115–22121. [PubMed] [Google Scholar]
  44. Hasegawa H., Ma T., Skach W., Matthay M.A., Verkman A.S. Molecular cloning of a mercurial sensitive water channel expressed in selected water-transporting tissues. J. Biol. Chem. 1994;269:5497–5500. [PubMed] [Google Scholar]
  45. Hediger M.A., Coady J.M., Ikeda T.S., Wright E.M. Expression cloning and cDNA sequencing of the Na+/glucose co-transporter. Nature. 1987;330:379–381. doi: 10.1038/330379a0. [DOI] [PubMed] [Google Scholar]
  46. Heller K.B., Lin E.C., Wilson T.H. Substrate specificity and transport properties of the glycerol facilitator of Escherichia coli. J. Bacteriol. 1980;144:274–278. doi: 10.1128/jb.144.1.274-278.1980. [DOI] [PMC free article] [PubMed] [Google Scholar]
  47. Heymann J.B., Agre P., Engel A. Progress on the structure and function of aquaporin-1. J. Struct. Biol. 1998;121:191–206. doi: 10.1006/jsbi.1997.3951. [DOI] [PubMed] [Google Scholar]
  48. Ikeda S., Nasrallah J.B., Dixit R., Preiss S., Nasrallah M.E. An aquaporin-like gene required for the Brassica self-incompatibility response. Science. 1997;276:1564–1566. doi: 10.1126/science.276.5318.1564. [DOI] [PubMed] [Google Scholar]
  49. Ishibashi K., Sasaki S., Fushimi K., Uchida S., Kuwahara M., Marumo F. Vol. 91. 1994. Molecular cloning and expression of a member of the aquaporin family with permeability to glycerol and urea in addition to water expressed at the basolateral membrane of kidney collecting duct cells; pp. 6269–6273. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  50. Ishibashi K., Kuwahara M., Gu Y., Kageyama Y., Tohsaka A., Suzuki F., Marumo F., Sasaki S. Cloning and functional expression of a new water channel abundantly expressed in testis and permeable to water, glycerol, and urea. J. Biol. Chem. 1997;272:20782–20786. doi: 10.1074/jbc.272.33.20782. [DOI] [PubMed] [Google Scholar]
  51. Jung J.S., Preston G.M., Smith B.L., Guggino W.B., Agre P. Molecular structure of the water channel through aquaporin CHIP: The hourglass model. J. Biol. Chem. 1994;269:14648–14654. [PubMed] [Google Scholar]
  52. Jung J.S., Bhat R.V., Preston G.M., Baraban J.M., Agre P. Vol. 91. 1994. Molecular characterization of an aquaporin cDNA from brain: Candidate osmoreceptor and regulator of water balance; pp. 13052–13056. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  53. Kachadorian W.A., Wade J.B., DiScala V.A. Vasopressin: Induced structural changes in toad bladder luminal membrane. J. Am. Soc. Neph. 2000;11:376–380. [PubMed] [Google Scholar]
  54. Kaldenhoff R., Grote K., Zhu J.J., Zimmermann U. Significance of plasmalemma aquaporins for water-transport in arabidopsis thaliana. Plant J. 1998;14:121–128. doi: 10.1046/j.1365-313x.1998.00111.x. [DOI] [PubMed] [Google Scholar]
  55. King L.S., Nielsen S., Agre P. Aquaporin-1 water channel protein in lung: Ontogeny, steroid-induced expression, and distribution in rat. J. Clin. Invest. 1996;97:2183–2191. doi: 10.1172/JCI118659. [DOI] [PMC free article] [PubMed] [Google Scholar]
  56. King L.S., Nielsen S., Agre P. Aquaporins in complex tissues: I. Developmental patterns in respiratory tract and glandular tissue of rat. Am. J. Physiol. 1997;273:C1541–C1548. doi: 10.1152/ajpcell.1997.273.5.C1541. [DOI] [PubMed] [Google Scholar]
  57. Koyama Y., Yamamoto T., Kondo D., Funaki H., Yaoita E., Kawasaki K., Sato H., Hatakeyama K., Kihara I. Molecular cloning of a new aquaporin from rat pancreas and liver. J. Biol. Chem. 1997;272:30329–30333. doi: 10.1074/jbc.272.48.30329. [DOI] [PubMed] [Google Scholar]
  58. Kushmerick C., Rice S.J., Baldo G.J., Haspel H.C., Mathias R.T. Ion, water, and neutral solute transport in Xenopus oocytes expressing frog lens MIP. Exo. Eye Res. 1995;61:351–362. doi: 10.1016/s0014-4835(05)80129-0. [DOI] [PubMed] [Google Scholar]
  59. Kuwahara M., Gu Y., Ishibashi K., Marumo F., Sasaki S. Mercury-sensitive residues and pore site in AQP3 water channel. Biochemistry. 1997;36:13973–13978. doi: 10.1021/bi9711442. [DOI] [PubMed] [Google Scholar]
  60. Lagrée V., Froger A., Deschamps S., Pellerin I., Delamarche C., Bonnec G., Gouranton J., Thomas D., Hubert J.F. Oligomerization state of water channels and glycerol facilitators: Involvement of loop E. J. Biol. Chem. 1998;273:33949–33953. doi: 10.1074/jbc.273.51.33949. [DOI] [PubMed] [Google Scholar]
  61. Lagrée V., Froger A., Deschamps S., Hubert J.F., Delamarche C., Bonnec G., Thomas D., Gouranton J., Pellerin I. Switch from an aquaporin to a glycerol channel by two amino acids substitution. J. Biol. Chem. 1999;274:6817–6819. doi: 10.1074/jbc.274.11.6817. [DOI] [PubMed] [Google Scholar]
  62. Laizé V., Gobin R., Rousselet G., Badier C., Hohmann S., Ripoche P., Tacnet F. Molecular and functional study of AQY1 from Saccharomyces cerevisiae. Role of the C-terminal domain. Biochem. Biophys. Res. Commun. 1999;257:139–144. doi: 10.1006/bbrc.1999.0425. [DOI] [PubMed] [Google Scholar]
  63. Laizé V., Tacnet F., Ripoche P., Hohmann S. Polymorphism of yeast aquaporins. Yeast. 2000;16:897–903. doi: 10.1002/1097-0061(200007)16:10<897::AID-YEA583>3.0.CO;2-T. [DOI] [PubMed] [Google Scholar]
  64. Lee M.D., King L.S., Agre P. The aquaporin family of water channel proteins in clinical medicine. Medicine. 1997;76:141–156. doi: 10.1097/00005792-199705000-00001. [DOI] [PubMed] [Google Scholar]
  65. Li H., Lee S., Jap B.K. Molecular design of aquaporin-1 water channel as revealed by electron crystallography. Nature Struct. Biol. 1997;4:263–265. doi: 10.1038/nsb0497-263. [DOI] [PubMed] [Google Scholar]
  66. Lu M., Lee M.D., Smith B.L., Jung J.S., Agre P., Verdijk M.A.J., Merkx G., Rijss J.P.L., Deen P. Vol. 93. 1996. The human aquaporin-4 gene: Definition of the locus encoding two water channel polypeptides in brain; pp. 10908–10912. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  67. Ma T., Frigeri A., Hasegawa H., Verkman A.S. Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter. J. Biol. Chem. 1994;269:21845–21849. [PubMed] [Google Scholar]
  68. Ma T., Yang B., Kuo W.L., Verkman A.S. cDNA cloning and gene structure of a novel water channel expressed exclusively in human kidney: Evidence for a gene cluster of aquaporins at chromosome locus 12q13. Genomics. 1995;35:543–550. doi: 10.1006/geno.1996.0396. [DOI] [PubMed] [Google Scholar]
  69. Ma T., Song Y., Gillespie A., Carlson E.J., Epstein C.J., Verkman A.S. Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels. J. Biol. Chem. 1999;274:20071–20074. doi: 10.1074/jbc.274.29.20071. [DOI] [PubMed] [Google Scholar]
  70. Macey R.I. Transport of water and urea in red blood cells. Am. J. Physiol. 1984;246:C195–C203. doi: 10.1152/ajpcell.1984.246.3.C195. [DOI] [PubMed] [Google Scholar]
  71. Manley G.T., Fujimura M., Ma T., Feliz F., Bollen A., Chan P., Verkman A.S. Aquaporin-4 deletion in mice reduces brain edema following acute water intoxication and ischemic stroke. Nature Med. 2000;6:159–163. doi: 10.1038/72256. [DOI] [PubMed] [Google Scholar]
  72. Marples D., Christensen S., Christensen E.L., Ottosen P.D., Nielsen S. Lithium-induced downregulation of aquaporin-2 water channel expression in rat kidney medulla. J. Clin. Invest. 1995;95:1838–1845. doi: 10.1172/JCI117863. [DOI] [PMC free article] [PubMed] [Google Scholar]
  73. Marples D., Frokiaer J., Dorup J., Knepper M.A., Nielsen S. Hypokalemia-induced downregulation of aquaporin-2 water channel expression in rat kidney medulla and cortex. J. Clin. Invest. 1996;97:1960–1968. doi: 10.1172/JCI118628. [DOI] [PMC free article] [PubMed] [Google Scholar]
  74. Mathai J.C., Mor S., Smith B.L., Preston G.M., Mohandas N., Collins M., van Zijl P.C.M., Zeidel M.L., Agre P. Functional analysis of aquaporin-1 deficient red cells: the Colton-null phenotype. J. Biol. Chem. 1996;271:1309–1313. doi: 10.1074/jbc.271.3.1309. [DOI] [PubMed] [Google Scholar]
  75. Maunsbach A.B., Marples D., Chin E., Ning G., Bondy C., Agre P., Nielsen S. Aquaporin-1 water channel expression in human kidney. J. Am. Soc. Nephrol. 1997;8:1–14. doi: 10.1681/ASN.V811. [DOI] [PubMed] [Google Scholar]
  76. Maurel C. Aquaporins and water permeability of plant membranes. Annu. Rev. Plant Physiol. Plant Mol. Biol. 1997;48:399–429. doi: 10.1146/annurev.arplant.48.1.399. [DOI] [PubMed] [Google Scholar]
  77. Maurel C., Reizer J., Schroeder J.L., Chrispeels M.J. The vacuolar membrane protein gamma-TIP creates water specific channels in Xenopus oocytes. EMBO J. 1993;12:2241–2247. doi: 10.1002/j.1460-2075.1993.tb05877.x. [DOI] [PMC free article] [PubMed] [Google Scholar]
  78. maurel C., Reizer J., Schroeder J.I., Chrispeels M.J., Saier M.H.J. Functional characterization of the Escherichia coli glycerol facilitator, G1pF, in Xenopus oocytes. J. Biol. Chem. 1994;269:11869–11872. [PubMed] [Google Scholar]
  79. Mitsuoka K., Murata K., Walz T., Hirai T., Agre P., Heymann B., Engel A., Fujiyoshi Y. The structure of aquaporin-1 at 4.5 Å resolution reveals short α-helices in the center of the monomer. J. Struct. Biol. 1999;128:34–43. doi: 10.1006/jsbi.1999.4177. [DOI] [PubMed] [Google Scholar]
  80. Moon C., King L.S., Agre P. AQP1 expression in erythroleukemia cells: Genetic Regulation of glucocorticoid and chemical induction. Am. J. Physiol. 1997;273:C1562–C1570. doi: 10.1152/ajpcell.1997.273.5.C1562. [DOI] [PubMed] [Google Scholar]
  81. Mulders S.M., Preston G.M., Deen P.M.T., Guggino W.B., van Os C.H., Agre P. Water channel properties of major intrinsic protein of lens. J. Biol. Chem. 1995;270:9010–9016. doi: 10.1074/jbc.270.15.9010. [DOI] [PubMed] [Google Scholar]
  82. Mulders S.M., Bichet D.G., Rijss J.P., Kamsteeg E.J., Arthus M.F., Lonergan M., Fujiwara M., Morgan K., Leijendekker R., van der Sluijs P., van Os C.H., Deen P.M.T. An aquaporin-2 water channel mutant which causes autosomal dominant nephrogenic diabetes insipidus is retained in the Golgi complex. J. Clin. Invest. 1998;102:57–66. doi: 10.1172/JCI2605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  83. Murata K., Mitsuoka K., Hirai T., Walz T., Agre P., Heymann J.B., Engel A., Fujiyoshi Y. Structural determinants of water permeation through aqua porin-1. Nature. 2000;407:599–605. doi: 10.1038/35036519. [DOI] [PubMed] [Google Scholar]
  84. Nagelhus E.A., Veruki M.L., Torp R., Haug F.M., Nielsen S., Agre P., Ottersen O.P. Aquaporin-4 water channel protein in the rat retina and optic nerve: Polarized expression in Müller cells and fibrous astrocytes. J. Neurosci. 1998;18:2506–2519. doi: 10.1523/JNEUROSCI.18-07-02506.1998. [DOI] [PMC free article] [PubMed] [Google Scholar]
  85. Nakhoul N.L., Davis B.A., Romero M.F., Boron W.F. Effect of expressing the water channel aquaporin-1 on the CO2 permeability. Am. J. Physiol. 1998;274:C543–C548. doi: 10.1152/ajpcell.1998.274.2.C543. [DOI] [PubMed] [Google Scholar]
  86. Neely J.D., Christensen B.M., Nielsen S., Agre P. Heterotetrameric composition of aquaporin-4 water channels. Biochemistry. 1999;38:11156–11163. doi: 10.1021/bi990941s. [DOI] [PubMed] [Google Scholar]
  87. Nemeth-Cahalan K.L., Hall J.E. pH and calcium regulate the water permeability of aquaporin 0. J. Biol. Chem. 2000;275:6777–6782. doi: 10.1074/jbc.275.10.6777. [DOI] [PubMed] [Google Scholar]
  88. Nielsen S., Agre P. The aquaporin family of water channels in kidney. Kidney Int. 1995;48:1057–1068. doi: 10.1038/ki.1995.389. [DOI] [PubMed] [Google Scholar]
  89. Nielsen S., Smith B.L., Christensen E.I., Knepper M., Agre P. CHIP28 water channels are localized in constitutively water-permeable segments of the nephron. J. Cell Biol. 1993;120:371–383. doi: 10.1083/jcb.120.2.371. [DOI] [PMC free article] [PubMed] [Google Scholar]
  90. Nielsen S., Smith B.L., Christensen E.I., Agre P. Vol. 90. 1993. Distribution of aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia; pp. 7275–7279. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  91. Nielsen S., Chou C.L., Marples D., Christensen E.I., Kishore B.K., Knepper M.A. Vol. 92. 1995. Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane; pp. 1013–1017. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  92. Nielsen S., Pallone T., Smith B.L., Christensen E.I., Agre P., maunsbach A. Aquaporin-1 water channels in short and long loop descending thin limbs and in descending vasa recta in rat kidney. Am. J. Physiol. Renal. 1995;37:F1023–F1037. doi: 10.1152/ajprenal.1995.268.6.F1023. [DOI] [PubMed] [Google Scholar]
  93. Nielsen S., King L.S., Mønster Christensen B., Agre P. Aquaporins in complex tissues: II. Subcellular distribution in respiratory and glandular tissues of rat. Am. J. Physiol. 1997;273:C1549–C1561. doi: 10.1152/ajpcell.1997.273.5.C1549. [DOI] [PubMed] [Google Scholar]
  94. Nielsen S., Nagelhus E.A., Amiry-Moghaddam M., Bourque C., Agre P., Ottersen O.P. Specialized membrane domains for water transport in glial cells: High resolution immunogold cytochemistry of aquaporin-4 in rat brain. J. Neurosci. 1997;17:171–180. doi: 10.1523/JNEUROSCI.17-01-00171.1997. [DOI] [PMC free article] [PubMed] [Google Scholar]
  95. Nielsen S., Terris J., Andersen D. Vol. 94. 1997. Congestive heart failure in rats is associated with increased expression and targeting of aquaporin-2 water channel in collecting duct; pp. 5450–5455. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  96. Ohara M., Martin P.Y., Xu D.L., St. John J., Pattison T.A., Kim J.K., Schrier R.W. Upregulation of aquaporin 2 water channel expression in pregnant rats. J. Clin. Invest. 1998;101:1076–1083. doi: 10.1172/JCI649. [DOI] [PMC free article] [PubMed] [Google Scholar]
  97. Opperman C.H., Taylor C.G., Conkling M.A. Root-knot nematode-directed expression of a plant root-specific gene. Science. 1994;263:221–223. doi: 10.1126/science.263.5144.221. [DOI] [PubMed] [Google Scholar]
  98. Pallone T., Kishore B.K., Nielsen S., Agre P., Knepper M.A. A selective pathway mediates NaCl induced water flux across descending vasa recta. Am. J. Physiol. Renal. 1997;272:F587–F596. doi: 10.1152/ajprenal.1997.272.5.F587. [DOI] [PubMed] [Google Scholar]
  99. Preston G.M., Agre P. Vol. 88. 1991. Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family; pp. 11110–11114. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  100. Preston G.M., Carroll T., Guggino W.B., Agre P. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science. 1992;256:385–387. doi: 10.1126/science.256.5055.385. [DOI] [PubMed] [Google Scholar]
  101. Preston G.M., Jung J.S., Guggino W.B., Agre P. The mercury-sensitive residue at cysteine-189 in the CHIP28 water channel. J. Biol. Chem. 1993;268:17–20. [PubMed] [Google Scholar]
  102. Preston G.M., Jung J.S., Guggino W.B., Agre P. Membrane topology of Aquaporin CHIP: Analysis of functional epitope-scanning mutants by vectorial proteolysis. J. Biol. Chem. 1994;269:1668–1673. [PubMed] [Google Scholar]
  103. Preston G.M., Smith B.L., Zeidel M.L., Moulds J.J., Agre P. Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. Science. 1994;265:1585–1587. doi: 10.1126/science.7521540. [DOI] [PubMed] [Google Scholar]
  104. Raina S., Preston G.M., Guggino W.B., Agre P. Molecular cloning and characterization of an aquaporin cDNA from salivary, lacrimal, and respiratory tissues. J. Biol. Chem. 1995;270:1508–1512. doi: 10.1074/jbc.270.4.1908. [DOI] [PubMed] [Google Scholar]
  105. Ramón Y., Cajal S. MIT Press; Cambridge, MA: 1897. Advice for a Young Investigator. 1999. [Google Scholar]
  106. Rao Y., Jan L.Y., Jan Y.N. Similarity of the product of the Drosophila neurogenic gene big brain and transmembrane channel proteins. Nature. 1990;345:163–167. doi: 10.1038/345163a0. [DOI] [PubMed] [Google Scholar]
  107. Rash J., Yasumura T., Hudson C.S., Agre P., Nielsen S. Vol. 95. 1998. Direct immunogold labeling of aquaporin-4 in square arrays of astroglial and ependymal cell membranes from rat brain and spinal cord; pp. 11981–11986. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  108. Reizer J., Reizer A., Saier M.H. The MIP family of integral membrane channel proteins: Sequence comparisons, evolutionary relationships, reconstructed pathway of evolution, and proposed functional differentiation of the two repeated halves of the proteins. Crit. Rev. Biochem. Mol. Biol. 1993;28:235–257. doi: 10.3109/10409239309086796. [DOI] [PubMed] [Google Scholar]
  109. Roberts S.K., Yano M., Ueno Y., Pham L., Alpini G., Agre P., LaRusso N. Vol. 91. 1994. Cholangiocytes express aquaporin CHIP and transport water via a channel-mediated mechanism; pp. 13009–13013. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  110. Sabolic I., Valenti G., Verbavatz J.M., van Hoek A.N., Verkman A.S., Ausiello D.A., Brown D. Localization of the CHIP28 water channel in rat kidney. Am. J. Physiol. 1992;263:C1225–C1233. doi: 10.1152/ajpcell.1992.263.6.C1225. [DOI] [PubMed] [Google Scholar]
  111. Saboori A.M., Smith B.L., Agre P. Vol. 85. 1988. Polymorphism in the Mr 32,000 Rh protein purified from Rh(D)-positive and -negative erythrocytes; pp. 4042–4045. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  112. shiels A., Bassnett S. Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Nat. Genet. 1996;12:212–215. doi: 10.1038/ng0296-212. [DOI] [PubMed] [Google Scholar]
  113. Skach W.R., Shi L.B., Calayag M.C., Frigeri A., Lingappa V.R., Verkman A.S. Biogenesis and transmembrane topology of the CHIP28 water channel at the endoplasmic reticulum. J. Cell Biol. 1994;125:803–815. doi: 10.1083/jcb.125.4.803. [DOI] [PMC free article] [PubMed] [Google Scholar]
  114. Smith B.L., Agre P. Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J. Biol. Chem. 1991;266:6407–6415. [PubMed] [Google Scholar]
  115. Smith B.L., Baumgarten R., Nielsen S., Raben D.M., Zeidel M.L., Agre P. Concurrent expression of crythroid and renal aquaporin CHIP and appearance of water channel activity in perinatal rats. J. Clin. Invest. 1993;92:2035–2041. doi: 10.1172/JCI116798. [DOI] [PMC free article] [PubMed] [Google Scholar]
  116. Smith B.L., Preston G.M., Spring F.A., Anstee D.J., Agre P. Human red cell aquaporin CHIP: I. Molecular characterization of ABH and Colton blood group antigens. J. Clin. Invest. 1994;94:1043–1049. doi: 10.1172/JCI117418. [DOI] [PMC free article] [PubMed] [Google Scholar]
  117. Smith H.W. Oxford University Press; New York: 1937. The Physiology of the Kidney. [Google Scholar]
  118. Solomon A.K. Characterization of biological membranes by equivalent pores. J. Gen. Physiol. 1968;51:S335–S364. [PMC free article] [PubMed] [Google Scholar]
  119. Solomon A.K. Water channels across the red blood cell and other biological membranes. Methods Enzymol. 1989;173:192–222. doi: 10.1016/s0076-6879(89)73013-5. [DOI] [PubMed] [Google Scholar]
  120. Solomon A.K., Chasan B., Dix J.A., Lukacovic M.F., Toon M.R., Verkman A.S. The aqueous pore in the red cell membrane. Ann. NY Acad. Sci. 1983;414:97–124. doi: 10.1111/j.1749-6632.1983.tb31678.x. [DOI] [PubMed] [Google Scholar]
  121. Steinfeld S., Cogan E., King L.S., Agre P., Kiss R., Delporte C. Defective cellular trafficking of aquaporin-5 water channel protein in Sjögren's syndrome lacrimal glands. Lab Invest. 2001 doi: 10.1038/labinvest.3780221. (in press) [DOI] [PubMed] [Google Scholar]
  122. Terris J., Ecelbarger C.A., Marples D., Knepper M.A., Nielsen S. Distribution of aquaporin-4 water channel espression within rat kidney. Am. J. Physiol. 1995;269:F775–F785. doi: 10.1152/ajprenal.1995.269.6.F775. [DOI] [PubMed] [Google Scholar]
  123. Tsubota K., Hirai S.I., King L.S., Agre P., Ishida N., Mita S. Defective cellular trafficking of aquaporin-5 water channel protein in Sjögren's syndrome lacrimal glands. The Lancet. 2001 doi: 10.1016/S0140-6736(00)04140-4. (in press) [DOI] [PubMed] [Google Scholar]
  124. Tsukaguchi H., Shayakul C., Berger U.V., Mackenzie B., Devidas S., Guggino W.M., van Hoek A.N., Hediger M.A. Molecular characterization of a broad selectivity neutral solute channel. J. Biol. Chem. 1998;273:24737–24743. doi: 10.1074/jbc.273.38.24737. [DOI] [PubMed] [Google Scholar]
  125. Umenishi F., Carter E.P., Yang B., Oliver B., Matthay M.A., Verkman A.S. Sharp increase in rat lung water channel expression in the perinatal period. am. J. Resp. Cell Mol. Biol. 1996;15:673–679. doi: 10.1165/ajrcmb.15.5.8918374. [DOI] [PubMed] [Google Scholar]
  126. Ussing H.H. Transport of electrolytes and water across epithelia. Harvey Lect. 1965;59:1–30. [PubMed] [Google Scholar]
  127. van Hoek A.N., Verkman A.S. Functional reconstitution of the isolated erythrocyte water channel. J. Biol. Chem. 1992;267:18267–18269. [PubMed] [Google Scholar]
  128. van Hoek A.N., Hom M.L., Luthjens L.H., de Jong M.D., Dempster J.A., van Os C.H. Functional unit of 30-kDa for proximal tubule water channels as revealed by radiation inactivation. J. Biol. Chem. 1991;266:16633–16635. [PubMed] [Google Scholar]
  129. Van Lieburg A.F., Verkijk M.A., Knoers V.V., van Essen A.J., Proesmans W., Malhnann R., Monnens L.A., van Oost B.A., van Os C.H., Deen P.M. Patients with amosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin-2 water-channel gene. Am. J. Hum. Genet. 1994;55:648–652. [PMC free article] [PubMed] [Google Scholar]
  130. Verbavatz J.M., Brown D., Sabolic I., Valenti G., Ausiello D.A., van Hoek A.N., Ma T., Verkman A.S. Tetrameric assembly of CHIP28 water channels in liposomes and cell membranes: A freeze-fracture study. J. Cell Biol. 1993;123:605–618. doi: 10.1083/jcb.123.3.605. [DOI] [PMC free article] [PubMed] [Google Scholar]
  131. Verkman A.S. Water channels in cell membranes. Ann. Rev Physiol. 1992;54:73–108. doi: 10.1146/annurev.ph.54.030192.000525. [DOI] [PubMed] [Google Scholar]
  132. Wade J.B., Stetson D.L., Lewis S.A. ADH action: Evidence for a membrane shuttle mechanism. Ann. NY. Acad. Sci. 1981;372:106–117. doi: 10.1111/j.1749-6632.1981.tb15464.x. [DOI] [PubMed] [Google Scholar]
  133. Walz T., Smith B.L., Zeidel M.L., Engel A., Agre P. Biologically active two-dimensional crystals of Aquaporin CHIP. J. Biol. Chem. 1994;269:1583–1586. [PubMed] [Google Scholar]
  134. Walz T., Hirai T., Murata K., Heymann J.B., Mitsuoka K., fujiyoshi Y., Smith B.L., Agre P., Engel A. Three-dimensional structure of aquaporin-1. Nature. 1997;387:624–627. doi: 10.1038/42512. [DOI] [PubMed] [Google Scholar]
  135. Wistow G.J., Pisano M.M., Chepelinsky A.B. Tandem sequence repeats in transmembrane channel proteins. Trends Biochem. Sci. 1991;165:170–171. doi: 10.1016/0968-0004(91)90065-4. [DOI] [PubMed] [Google Scholar]
  136. Xu D.L., Martin P.Y., Ohara M. Upregulation of aquaporin-2 water channel expression in chronic heart failure rat. J. Clin. Invest. 1997;99:1500–1505. doi: 10.1172/JCI119312. [DOI] [PMC free article] [PubMed] [Google Scholar]
  137. Yang B.X., Brown D., Verkman A.S. The mercurial insensitive water channel (AQP4) forms orthogonal arrays in stably transfected Chinese hamster ovary cells. J. Biol. Chem. 1996;271:4577–4581. [PubMed] [Google Scholar]
  138. Yang B., Fukuda N., van Hoek A., Matthay M.A., Ma T., Verkman A.S. Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and kidney of mice and in reconstituted proteoliposomes. J. Biol. Chem. 2000;275:2686–2692. doi: 10.1074/jbc.275.4.2686. [DOI] [PubMed] [Google Scholar]
  139. Yasui M., Kwon T.H., Knepper M.A., Nielsen S., Agre P. Vol. 96. 1999. Aquaporin-6: An intracellular vesicle water channel protein; pp. 5808–5813. (Proc. Natl. Acad. Sci. USA). [DOI] [PMC free article] [PubMed] [Google Scholar]
  140. Yasui M., Hazama A., Kwon T.H., Nielsen S., Guggino W.B., Agre P. Rapid gating and anion permeability of an intracellular aquaporin. Nature. 1999;402:184–187. doi: 10.1038/46045. [DOI] [PubMed] [Google Scholar]
  141. Yool A.J., Starner W.D., Regan J.W. Forskolin stimulation of water and cation permeability in aquaporin-1 water channels. Science. 1996;273:1216–1218. doi: 10.1126/science.273.5279.1216. [DOI] [PubMed] [Google Scholar]
  142. Zeidel M.L., Ambudkar S.V., Smith B.L., Agre P. Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry. 1992;31:7436–7440. doi: 10.1021/bi00148a002. [DOI] [PubMed] [Google Scholar]
  143. Zeidel M.L., Nielsen S., Smith B.L., Ambudkar S.V., Maunsbach A.B., Agre P. Ultrastructure, pharmacologic inhibition, and transport-selectivity of aquaporin CHIP in proteoliposomes. Biochemistry. 1994;33:1606–1615. doi: 10.1021/bi00172a042. [DOI] [PubMed] [Google Scholar]
  144. Zelinkski T., Kaita H., Gibson T., Coghlan G., Philipps S., Lewis M. Linkage between the Colton blood group locus and ASSP11 on chromosome 7. Genomics. 1990;6:623–625. doi: 10.1016/0888-7543(90)90496-h. [DOI] [PubMed] [Google Scholar]
  145. Zhang R., Logee K.A., Verkman A.S. Expression of mRNA coding for kidney and red cell water channels in Xenopus oocytes. J. Biol. Chem. 1990;265:15375–15378. [PubMed] [Google Scholar]

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