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Volumn 190, Issue , 2009, Pages 3-28

Discovery of the aquaporins and development of the field

Author keywords

[No Author keywords available]

Indexed keywords

AMMONIA; ANION; ANTIMONITE; AQUAGLYCEROPORIN; AQUAPORIN; AQUAPORIN 1; AQUAPORIN 2; AQUAPORIN 3; AQUAPORIN 4; AQUAPORIN 5; AQUAPORIN 6; AQUAPORIN 7; AQUAPORIN 8; AQUAPORIN 9; ARSENIC TRIOXIDE; CARBON DIOXIDE; GLYCEROL; HYDROGEN PEROXIDE; NITRIC OXIDE; UNCLASSIFIED DRUG; UREA; ANTIMONY; ARSENOUS ACID DERIVATIVE; WATER;

EID: 61449558400     PISSN: 01712004     EISSN: None     Source Type: Book Series    
DOI: 10.1007/978-3-540-79885-9_1     Document Type: Review
Times cited : (189)

References (162)
  • 1
    • 0023610959 scopus 로고
    • Purification and partial characterization of the Mr 30,000 integral membrane protein associated with the erythrocyte Rh(D) antigen
    • Agre P, Saboori AM, Asimos A, Smith BL (1987) Purification and partial characterization of the Mr 30,000 integral membrane protein associated with the erythrocyte Rh(D) antigen. J Biol Chem 262:17497-17503
    • (1987) J Biol Chem , vol.262 , pp. 17497-17503
    • Agre, P.1    Saboori, A.M.2    Asimos, A.3    Smith, B.L.4
  • 2
    • 0027431432 scopus 로고
    • Aquaporins, a family of membrane water channels
    • Agre P, Sasaki S, Chrispeels MJ (1993) Aquaporins, a family of membrane water channels. Am J Physiol 265:F461
    • (1993) Am J Physiol , vol.265
    • Agre, P.1    Sasaki, S.2    Chrispeels, M.J.3
  • 4
    • 2442638032 scopus 로고    scopus 로고
    • Alpha-syntrophin deletion removes the perivascular but not the endothelial pool of aquaporin-4 at the blood-brain barrier and delays the development of brain edema in an experimental model of acute hyponatremia
    • Amiry-Moghaddam M, Xue R, Haug FM, Neely JD, Bhardwaj A, Agre P, Adams ME, Froehner SC, Mori S, Ottersen OP (2004) Alpha-syntrophin deletion removes the perivascular but not the endothelial pool of aquaporin-4 at the blood-brain barrier and delays the development of brain edema in an experimental model of acute hyponatremia. FASEB J 18:542-544
    • (2004) FASEB J , vol.18 , pp. 542-544
    • Amiry-Moghaddam, M.1    Xue, R.2    Haug, F.M.3    Neely, J.D.4    Bhardwaj, A.5    Agre, P.6    Adams, M.E.7    Froehner, S.C.8    Mori, S.9    Ottersen, O.P.10
  • 7
    • 0022448651 scopus 로고
    • p-(Chloromercuri) benzenesulfonate binding by membrane proteins and the inhibition of water transport in human erythrocytes
    • Benga G, Popescu O, Pop VI, Holmes RP (1986) p-(Chloromercuri) benzenesulfonate binding by membrane proteins and the inhibition of water transport in human erythrocytes. Biochemistry 25:1535-1538
    • (1986) Biochemistry , vol.25 , pp. 1535-1538
    • Benga, G.1    Popescu, O.2    Pop, V.I.3    Holmes, R.P.4
  • 8
    • 0036847857 scopus 로고    scopus 로고
    • Selective down-regulation of aquaporin-1 in salivary glands in primary Sjögren's syndrome
    • Beroukas D, Hiscock J, Gannon BJ, Jonsson R, Gordon TP, Waterman SA (2002) Selective down-regulation of aquaporin-1 in salivary glands in primary Sjögren's syndrome. Lab Invest 82:1547-1552
    • (2002) Lab Invest , vol.82 , pp. 1547-1552
    • Beroukas, D.1    Hiscock, J.2    Gannon, B.J.3    Jonsson, R.4    Gordon, T.P.5    Waterman, S.A.6
  • 9
    • 0034118380 scopus 로고    scopus 로고
    • Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q
    • Berry V, Francis P, Kaushal S, Moore A, Bhattacharya S (2000) Missense mutations in MIP underlie autosomal dominant 'polymorphic' and lamellar cataracts linked to 12q. Nat Genet 25: 15-17
    • (2000) Nat Genet , vol.25 , pp. 15-17
    • Berry, V.1    Francis, P.2    Kaushal, S.3    Moore, A.4    Bhattacharya, S.5
  • 12
    • 1542290152 scopus 로고    scopus 로고
    • Increased seizure threshold in mice lacking aquaporin-4 water channels
    • Binder DK, Oshio K, Ma T, Verkman AS, Manley GT (2004) Increased seizure threshold in mice lacking aquaporin-4 water channels. Neuroreport 15:259-262
    • (2004) Neuroreport , vol.15 , pp. 259-262
    • Binder, D.K.1    Oshio, K.2    Ma, T.3    Verkman, A.S.4    Manley, G.T.5
  • 13
    • 33646000806 scopus 로고    scopus 로고
    • Increased seizure duration and slowed potassium kinetics in mice lacking aquaporin-4 water channels
    • Binder DK, Yao X, Zador Z, Sick TJ, Verkman AS, Manley GT (2006) Increased seizure duration and slowed potassium kinetics in mice lacking aquaporin-4 water channels. Glia 53:631-636
    • (2006) Glia , vol.53 , pp. 631-636
    • Binder, D.K.1    Yao, X.2    Zador, Z.3    Sick, T.J.4    Verkman, A.S.5    Manley, G.T.6
  • 14
    • 33747050114 scopus 로고    scopus 로고
    • Ion channel function of aquaporin-1 natively expressed in choroid plexus
    • Boassa D, Stamer WD, Yool AJ (2006) Ion channel function of aquaporin-1 natively expressed in choroid plexus. J Neurosci 26:7811-7819
    • (2006) J Neurosci , vol.26 , pp. 7811-7819
    • Boassa, D.1    Stamer, W.D.2    Yool, A.J.3
  • 15
    • 0032853219 scopus 로고    scopus 로고
    • Cellular and molecular biology of the aquaporin water channels
    • Borgnia M, Nielsen S, Engel A, Agre P (1999) Cellular and molecular biology of the aquaporin water channels. Annu Rev Biochem 68:425-458
    • (1999) Annu Rev Biochem , vol.68 , pp. 425-458
    • Borgnia, M.1    Nielsen, S.2    Engel, A.3    Agre, P.4
  • 18
    • 0033557374 scopus 로고    scopus 로고
    • Reduced water permeability and altered ultrastructure in thin descending limb of Henle in aquaporin-1 null mice
    • Chou CL, Knepper MA, Hoek AN, Brown D, Yang B, Ma T, Verkman AS (1999) Reduced water permeability and altered ultrastructure in thin descending limb of Henle in aquaporin-1 null mice. J Clin Invest 103:491-496
    • (1999) J Clin Invest , vol.103 , pp. 491-496
    • Chou, C.L.1    Knepper, M.A.2    Hoek, A.N.3    Brown, D.4    Yang, B.5    Ma, T.6    Verkman, A.S.7
  • 21
    • 0023768507 scopus 로고
    • Identification, purification, and characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules
    • Denker BM, Smith BL, Kuhajda FP, Agre P (1988) Identification, purification, and characterization of a novel Mr 28,000 integral membrane protein from erythrocytes and renal tubules. J Biol Chem 263:15634-15642
    • (1988) J Biol Chem , vol.263 , pp. 15634-15642
    • Denker, B.M.1    Smith, B.L.2    Kuhajda, F.P.3    Agre, P.4
  • 22
    • 0023424908 scopus 로고
    • Electron microscopic observations of reconstituted proteoliposomes with the purified major intrinsic membrane protein of eye lens fibers
    • Dunia I,Manenti S, Rousselet A, Benedetti EL (1987) Electron microscopic observations of reconstituted proteoliposomes with the purified major intrinsic membrane protein of eye lens fibers. J Cell Biol 105:1679-1689
    • (1987) J Cell Biol , vol.105 , pp. 1679-1689
    • Dunia, I.1    Manenti, S.2    Rousselet, A.3    Benedetti, E.L.4
  • 24
    • 0028020911 scopus 로고
    • Cloning and expression of AQP3, a water channel frommedullary collecting duct of rat kidney
    • Echevarria M, Windhager EE, Tate SS, Frindt G (1994) Cloning and expression of AQP3, a water channel frommedullary collecting duct of rat kidney. Proc Natl Acad Sci USA 91:10997-11001
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 10997-11001
    • Echevarria, M.1    Windhager, E.E.2    Tate, S.S.3    Frindt, G.4
  • 27
  • 28
    • 0029009408 scopus 로고
    • Immunolocalization of the mercurialinsensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes
    • Frigeri A, Gropper M, Turck CW, Verkman AS (1995) Immunolocalization of the mercurialinsensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes. Proc Natl Acad Sci USA 92:4328-4331
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 4328-4331
    • Frigeri, A.1    Gropper, M.2    Turck, C.W.3    Verkman, A.S.4
  • 31
    • 33644521546 scopus 로고    scopus 로고
    • Molecular biology of hereditary diabetes insipidus
    • Fujiwara TM, Bichet DG (2005) Molecular biology of hereditary diabetes insipidus. J Am Soc Nephrol 16:2836-2846
    • (2005) J Am Soc Nephrol , vol.16 , pp. 2836-2846
    • Fujiwara, T.M.1    Bichet, D.G.2
  • 32
    • 0027459174 scopus 로고
    • Cloning and expression of apical membrane water channel of rat kidney collecting tubule
    • Fushimi K, Uchida S, Hara Y, Hirata Y, Marumo F, Sasaki S (1993) Cloning and expression of apical membrane water channel of rat kidney collecting tubule. Nature 361:549-552
    • (1993) Nature , vol.361 , pp. 549-552
    • Fushimi, K.1    Uchida, S.2    Hara, Y.3    Hirata, Y.4    Marumo, F.5    Sasaki, S.6
  • 33
    • 0030965161 scopus 로고    scopus 로고
    • Phosphorylation of serine 256 is required for cAMPdependent regulatory exocytosis of the aquaporin-2 water channel
    • Fushimi K, Sasaki S, Marumo F (1997) Phosphorylation of serine 256 is required for cAMPdependent regulatory exocytosis of the aquaporin-2 water channel. J Biol Chem 272:14800-14804
    • (1997) J Biol Chem , vol.272 , pp. 14800-14804
    • Fushimi, K.1    Sasaki, S.2    Marumo, F.3
  • 34
    • 0035853805 scopus 로고    scopus 로고
    • The water channel aquaporin-8 is mainly intracellular in rat hepatocytes, and its plasma membrane insertion is stimulated by cyclic AMP
    • Garcia F, Kierbel A, Larocca MC, Gradilone SA, Splinter P, LaRusso NF,Marinelli RA (2001) The water channel aquaporin-8 is mainly intracellular in rat hepatocytes, and its plasma membrane insertion is stimulated by cyclic AMP. J Biol Chem 276:12147-12152
    • (2001) J Biol Chem , vol.276 , pp. 12147-12152
    • Garcia, F.1    Kierbel, A.2    Larocca, M.C.3    Gradilone, S.A.4    Splinter, P.5    LaRusso, N.F.6    Marinelli, R.A.7
  • 37
    • 0021712623 scopus 로고
    • The major intrinsic protein (MIP) of the bovine lens fiber membrane
    • Gorin MB, Yancey SB, Cline J, Revel JP, Horwitz J (1984) The major intrinsic protein (MIP) of the bovine lens fiber membrane. Cell 39:49-59
    • (1984) Cell , vol.39 , pp. 49-59
    • Gorin, M.B.1    Yancey, S.B.2    Cline, J.3    Revel, J.P.4    Horwitz, J.5
  • 41
    • 34548840252 scopus 로고    scopus 로고
    • A novel mutation in major intrinsic protein of the lens gene (MIP) underlies autosomal dominant cataract in a Chinese family
    • Gu F, Zhai H, Li D, Zhao L, Li C, Huang S, Ma X (2007) A novel mutation in major intrinsic protein of the lens gene (MIP) underlies autosomal dominant cataract in a Chinese family. Mol Vis 13:1651-1656
    • (2007) Mol Vis , vol.13 , pp. 1651-1656
    • Gu, F.1    Zhai, H.2    Li, D.3    Zhao, L.4    Li, C.5    Huang, S.6    Ma, X.7
  • 43
    • 0038132147 scopus 로고    scopus 로고
    • Glycerol replacement corrects defective skin hydration, elasticity, and barrier function in aquaporin-3-deficient mice
    • Hara M, Verkman AS (2003) Glycerol replacement corrects defective skin hydration, elasticity, and barrier function in aquaporin-3-deficient mice. Proc Natl Acad Sci USA 100:7360-7365
    • (2003) Proc Natl Acad Sci USA , vol.100 , pp. 7360-7365
    • Hara, M.1    Verkman, A.S.2
  • 44
    • 0037195795 scopus 로고    scopus 로고
    • Selectively reduced glycerol in skin of aquaporin-3-deficient mice may account for impaired skin hydration, elasticity, and barrier recovery
    • Hara M, Ma T, Verkman AS (2002) Selectively reduced glycerol in skin of aquaporin-3-deficient mice may account for impaired skin hydration, elasticity, and barrier recovery. J Biol Chem 277:46616-46621
    • (2002) J Biol Chem , vol.277 , pp. 46616-46621
    • Hara, M.1    Ma, T.2    Verkman, A.S.3
  • 45
    • 18144401213 scopus 로고    scopus 로고
    • Progressive adipocyte hypertrophy in aquaporin-7-deficient mice: Adipocyte glycerol permeability as a novel regulator of fat accumulation
    • Hara-Chikuma M, Sohara E, Rai T, Ikawa M, Okabe M, Sasaki S, Uchida S, Verkman AS (2005) Progressive adipocyte hypertrophy in aquaporin-7-deficient mice: adipocyte glycerol permeability as a novel regulator of fat accumulation. J Biol Chem 280:15493-15496
    • (2005) J Biol Chem , vol.280 , pp. 15493-15496
    • Hara-Chikuma, M.1    Sohara, E.2    Rai, T.3    Ikawa, M.4    Okabe, M.5    Sasaki, S.6    Uchida, S.7    Verkman, A.S.8
  • 47
    • 0024121575 scopus 로고
    • Identification of specific apical membrane polypeptides associated with the antidiuretic hormone-elicited water permeability increase in the toad urinary bladder
    • Harris HW, Wade JB, Handler JS (1988) Identification of specific apical membrane polypeptides associated with the antidiuretic hormone-elicited water permeability increase in the toad urinary bladder. Proc Natl Acad Sci USA 85:1942-1946
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 1942-1946
    • Harris, H.W.1    Wade, J.B.2    Handler, J.S.3
  • 48
    • 0032546752 scopus 로고    scopus 로고
    • Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution
    • Hasler L, Walz T, Tittmann P, Gross H, Kistler J, Engel A (1998) Purified lens major intrinsic protein (MIP) forms highly ordered tetragonal two-dimensional arrays by reconstitution. J Mol Biol 279:855-864
    • (1998) J Mol Biol , vol.279 , pp. 855-864
    • Hasler, L.1    Walz, T.2    Tittmann, P.3    Gross, H.4    Kistler, J.5    Engel, A.6
  • 50
    • 34247849194 scopus 로고    scopus 로고
    • Novel role of AQP-1 in NO-dependent vasorelaxation
    • Herrera M, Garvin JL (2007) Novel role of AQP-1 in NO-dependent vasorelaxation. Am J Physiol Renal Physiol 292:F1443-F1451
    • (2007) Am J Physiol Renal Physiol , vol.292
    • Herrera, M.1    Garvin, J.L.2
  • 51
    • 33745988574 scopus 로고    scopus 로고
    • Aquaporin-1 transports NO across cell membranes
    • Herrera M, Hong NJ, Garvin JL (2006) Aquaporin-1 transports NO across cell membranes. Hypertension 48:157-164
    • (2006) Hypertension , vol.48 , pp. 157-164
    • Herrera, M.1    Hong, N.J.2    Garvin, J.L.3
  • 55
    • 0037131175 scopus 로고    scopus 로고
    • Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63
    • IkedaM, Beitz E, Kozono D, Guggino WB, Agre P, YasuiM(2002) Characterization of aquaporin-6 as a nitrate channel in mammalian cells. Requirement of pore-lining residue threonine 63. J Biol Chem 277:39873-39879
    • (2002) J Biol Chem , vol.277 , pp. 39873-39879
    • Ikeda, M.1    Beitz, E.2    Kozono, D.3    Guggino, W.B.4    Agre, P.5    Yasui, M.6
  • 56
    • 0028227129 scopus 로고
    • 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
    • Ishibashi K, Sasaki S, Fushimi K, Uchida S, Kuwahara M, Marumo F (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. Proc Natl Acad Sci USA 91:6269-6273
    • (1994) Proc Natl Acad Sci USA , vol.91 , pp. 6269-6273
    • Ishibashi, K.1    Sasaki, S.2    Fushimi, K.3    Uchida, S.4    Kuwahara, M.5    Marumo, F.6
  • 57
    • 0030860531 scopus 로고    scopus 로고
    • Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea
    • Ishibashi K, Kuwahara M, Gu Y, Kageyama Y, Tohsaka A, Suzuki F, Marumo F, Sasaki S (1997) Cloning and functional expression of a new water channel abundantly expressed in the testis permeable to water, glycerol, and urea. J Biol Chem 272:20782-20786
    • (1997) J Biol Chem , vol.272 , pp. 20782-20786
    • Ishibashi, K.1    Kuwahara, M.2    Gu, Y.3    Kageyama, Y.4    Tohsaka, A.5    Suzuki, F.6    Marumo, F.7    Sasaki, S.8
  • 58
    • 0032489241 scopus 로고    scopus 로고
    • Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol
    • Ishibashi K, Kuwahara M, Gu Y, Tanaka Y, Marumo F, Sasaki S (1998) Cloning and functional expression of a new aquaporin (AQP9) abundantly expressed in the peripheral leukocytes permeable to water and urea, but not to glycerol. Biochem Biophys Res Commun 244:268-274
    • (1998) Biochem Biophys Res Commun , vol.244 , pp. 268-274
    • Ishibashi, K.1    Kuwahara, M.2    Gu, Y.3    Tanaka, Y.4    Marumo, F.5    Sasaki, S.6
  • 59
    • 0037135227 scopus 로고    scopus 로고
    • Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin
    • Ishibashi K, Morinaga T, Kuwahara M, Sasaki S, Imai M (2002) Cloning and identification of a new member of water channel (AQP10) as an aquaglyceroporin. Biochim Biophys Acta 1576:335-340
    • (2002) Biochim Biophys Acta , vol.1576 , pp. 335-340
    • Ishibashi, K.1    Morinaga, T.2    Kuwahara, M.3    Sasaki, S.4    Imai, M.5
  • 63
    • 0028318868 scopus 로고
    • Molecular structure of the water channel through aquaporin CHIP: The hourglass model
    • Jung JS, Preston GM, Smith BL, Guggino WB, Agre P (1994) Molecular structure of the water channel through aquaporin CHIP: The hourglass model. J Biol Chem 269:14648-14654
    • (1994) J Biol Chem , vol.269 , pp. 14648-14654
    • Jung, J.S.1    Preston, G.M.2    Smith, B.L.3    Guggino, W.B.4    Agre, P.5
  • 64
    • 0033984955 scopus 로고    scopus 로고
    • Vasopressin: Induced structural changes in toad bladder luminal membrane
    • Kachadorian WA, Wade JB, DiScala VA (2000) Vasopressin: Induced structural changes in toad bladder luminal membrane. J Am Soc Nephrol 11:376-380
    • (2000) J Am Soc Nephrol , vol.11 , pp. 376-380
    • Kachadorian, W.A.1    Wade, J.B.2    DiScala, V.A.3
  • 65
    • 0034645068 scopus 로고    scopus 로고
    • The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers
    • Kamsteeg EJ, Heijnen I, van Os CH, Deen PM (2000) The subcellular localization of an aquaporin-2 tetramer depends on the stoichiometry of phosphorylated and nonphosphorylated monomers. J Cell Biol 151:919-930
    • (2000) J Cell Biol , vol.151 , pp. 919-930
    • Kamsteeg, E.J.1    Heijnen, I.2    van Os, C.H.3    Deen, P.M.4
  • 67
    • 0030772349 scopus 로고    scopus 로고
    • Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells
    • Katsura T, Gustafson CE, Ausiello DA, Brown D (1997) Protein kinase A phosphorylation is involved in regulated exocytosis of aquaporin-2 in transfected LLC-PK1 cells. Am J Physiol Renal Physiol 272:F816-F822
    • (1997) Am J Physiol Renal Physiol , vol.272
    • Katsura, T.1    Gustafson, C.E.2    Ausiello, D.A.3    Brown, D.4
  • 68
    • 26944471697 scopus 로고    scopus 로고
    • Decreased expression of AQP2 and AQP4 water channels and Na,K-ATPase in kidney collecting duct in AQP3 null mice
    • Kim SW, Gresz V, Rojek A, Wang W, Verkman AS, Frøkiaer J, Nielsen S (2005) Decreased expression of AQP2 and AQP4 water channels and Na,K-ATPase in kidney collecting duct in AQP3 null mice. Biol Cell 97:765-778
    • (2005) Biol Cell , vol.97 , pp. 765-778
    • Kim, S.W.1    Gresz, V.2    Rojek, A.3    Wang, W.4    Verkman, A.S.5    Frøkiaer, J.6    Nielsen, S.7
  • 69
    • 0029588463 scopus 로고
    • Current concepts of brain edema. Review of laboratory investigations
    • Kimelberg HK (1995) Current concepts of brain edema. Review of laboratory investigations. J Neurosurg 83:1051-1059
    • (1995) J Neurosurg , vol.83 , pp. 1051-1059
    • Kimelberg, H.K.1
  • 70
    • 0030013048 scopus 로고    scopus 로고
    • Aquaporin-1 water channel protein in lung: Ontogeny, steroidinduced expression, and distribution in rat
    • King LS, Nielsen S, Agre P (1996) Aquaporin-1 water channel protein in lung: Ontogeny, steroidinduced expression, and distribution in rat. J Clin Invest 97:2183-2191
    • (1996) J Clin Invest , vol.97 , pp. 2183-2191
    • King, L.S.1    Nielsen, S.2    Agre, P.3
  • 71
    • 0035913207 scopus 로고    scopus 로고
    • Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1
    • King LS, Choi M, Fernandez PC, Cartron JP, Agre P (2001) Defective urinary-concentrating ability due to a complete deficiency of aquaporin-1. N Engl J Med 345:175-179
    • (2001) N Engl J Med , vol.345 , pp. 175-179
    • King, L.S.1    Choi, M.2    Fernandez, P.C.3    Cartron, J.P.4    Agre, P.5
  • 72
    • 0037154182 scopus 로고    scopus 로고
    • Decreased pulmonary vascular permeability in aquaporin-1 null humans
    • King LS, Nielsen S, Agre P, Brown RH (2002) Decreased pulmonary vascular permeability in aquaporin-1 null humans. Proc Natl Acad Sci USA 99:1059-1063
    • (2002) Proc Natl Acad Sci USA , vol.99 , pp. 1059-1063
    • King, L.S.1    Nielsen, S.2    Agre, P.3    Brown, R.H.4
  • 76
    • 0035968332 scopus 로고    scopus 로고
    • Salivary acinar cells from aquaporin 5-deficient mice have decreased membrane water permeability and altered cell volume regulation
    • Krane CM, Melvin JE, Nguyen HV, Richardson L, Towne JE, Doetschman T, Menon AG (2001b) Salivary acinar cells from aquaporin 5-deficient mice have decreased membrane water permeability and altered cell volume regulation. J Biol Chem 276:23413-23420
    • (2001) J Biol Chem , vol.276 , pp. 23413-23420
    • Krane, C.M.1    Melvin, J.E.2    Nguyen, H.V.3    Richardson, L.4    Towne, J.E.5    Doetschman, T.6    Menon, A.G.7
  • 77
    • 33745850428 scopus 로고    scopus 로고
    • Enhanced expression of multidrug resistance-associated protein 2 and reduced expression of aquaglyceroporin 3 in an arsenic-resistant human cell line
    • Lee TC, Ho IC, Lu WJ, Huang JD (2006) Enhanced expression of multidrug resistance-associated protein 2 and reduced expression of aquaglyceroporin 3 in an arsenic-resistant human cell line. J Biol Chem 281:18401-18407
    • (2006) J Biol Chem , vol.281 , pp. 18401-18407
    • Lee, T.C.1    Ho, I.C.2    Lu, W.J.3    Huang, J.D.4
  • 78
    • 13844310859 scopus 로고    scopus 로고
    • Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution
    • Liu K, Kozono D, Kato Y, Agre P, Hazama A, Yasui M (2005) Conversion of aquaporin 6 from an anion channel to a water-selective channel by a single amino acid substitution. Proc Natl Acad Sci USA 102:2192-2197
    • (2005) Proc Natl Acad Sci USA , vol.102 , pp. 2192-2197
    • Liu, K.1    Kozono, D.2    Kato, Y.3    Agre, P.4    Hazama, A.5    Yasui, M.6
  • 81
    • 0028059494 scopus 로고
    • Cloning of a water channel homolog expressed in brain meningeal cells and kidney collecting duct that functions as a stilbene-sensitive glycerol transporter
    • Ma T, Frigeri A, Hasegawa H, Verkman AS (1994) 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 269:21845-21849
    • (1994) J Biol Chem , vol.269 , pp. 21845-21849
    • Ma, T.1    Frigeri, A.2    Hasegawa, H.3    Verkman, A.S.4
  • 82
    • 0030955183 scopus 로고    scopus 로고
    • Generation and phenotype of a transgenic knockout mouse lacking the mercurial-insensitive water channel aquaporin-4
    • Ma T, Yang B, Gillespie A, Carlson EJ, Epstein CJ, Verkman AS (1997a) Generation and phenotype of a transgenic knockout mouse lacking the mercurial-insensitive water channel aquaporin-4. J Clin Invest 100:957-962
    • (1997) J Clin Invest , vol.100 , pp. 957-962
    • Ma, T.1    Yang, B.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5    Verkman, A.S.6
  • 83
    • 0031576555 scopus 로고    scopus 로고
    • Cloning of a novel water and urea-permeable aquaporin from mouse expressed strongly in colon, placenta, liver, and heart
    • Ma T, Yang B, Verkman AS (1997b) Cloning of a novel water and urea-permeable aquaporin from mouse expressed strongly in colon, placenta, liver, and heart. Biochem Biophys Res Commun 240:324-328
    • (1997) Biochem Biophys Res Commun , vol.240 , pp. 324-328
    • Ma, T.1    Yang, B.2    Verkman, A.S.3
  • 84
    • 0032549031 scopus 로고    scopus 로고
    • Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels
    • Ma T, Yang B, Gillespie A, Carlson EJ, Epstein CJ, Verkman AS (1998) Severely impaired urinary concentrating ability in transgenic mice lacking aquaporin-1 water channels. J Biol Chem 273:4296-4299
    • (1998) J Biol Chem , vol.273 , pp. 4296-4299
    • Ma, T.1    Yang, B.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5    Verkman, A.S.6
  • 85
    • 0033575326 scopus 로고    scopus 로고
    • Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels
    • Ma T, Song Y, Gillespie A, Carlson EJ, Epstein CJ, Verkman AS (1999) Defective secretion of saliva in transgenic mice lacking aquaporin-5 water channels. J Biol Chem 274:20071-20074
    • (1999) J Biol Chem , vol.274 , pp. 20071-20074
    • Ma, T.1    Song, Y.2    Gillespie, A.3    Carlson, E.J.4    Epstein, C.J.5    Verkman, A.S.6
  • 87
    • 0037053303 scopus 로고    scopus 로고
    • Impaired stratum corneum hydration in mice lacking epidermal water channel aquaporin-3
    • Ma T, Hara M, Sougrat R, Verbavatz JM, Verkman AS (2002) Impaired stratum corneum hydration in mice lacking epidermal water channel aquaporin-3. J Biol Chem 277:17147-17153
    • (2002) J Biol Chem , vol.277 , pp. 17147-17153
    • Ma, T.1    Hara, M.2    Sougrat, R.3    Verbavatz, J.M.4    Verkman, A.S.5
  • 88
    • 0021251173 scopus 로고
    • Transport of water and urea in red blood cells
    • Macey RI (1984) Transport of water and urea in red blood cells. Am J Physiol 246:C195-C203
    • (1984) Am J Physiol , vol.246
    • Macey, R.I.1
  • 91
    • 0031011414 scopus 로고    scopus 로고
    • Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane
    • Marinelli RA, Pham L, Agre P, LaRusso NF (1997) Secretin promotes osmotic water transport in rat cholangiocytes by increasing aquaporin-1 water channels in plasma membrane. J Biol Chem 272:12984-12988
    • (1997) J Biol Chem , vol.272 , pp. 12984-12988
    • Marinelli, R.A.1    Pham, L.2    Agre, P.3    LaRusso, N.F.4
  • 94
    • 0026348012 scopus 로고
    • Cell to cell communication and pH in the frog lens
    • Mathias RT, Riquelme G, Rae JL (1991) Cell to cell communication and pH in the frog lens. J Gen Physiol 98:1085-1103
    • (1991) J Gen Physiol , vol.98 , pp. 1085-1103
    • Mathias, R.T.1    Riquelme, G.2    Rae, J.L.3
  • 95
    • 0032868691 scopus 로고    scopus 로고
    • Water channel protein AQP3 is present in epithelia exposed to the environment of possible water loss
    • Matsuzaki T, Suzuki T, Koyama H, Tanaka S, Takata K (1999) Water channel protein AQP3 is present in epithelia exposed to the environment of possible water loss. J Histochem Cytochem 47:1275-1286
    • (1999) J Histochem Cytochem , vol.47 , pp. 1275-1286
    • Matsuzaki, T.1    Suzuki, T.2    Koyama, H.3    Tanaka, S.4    Takata, K.5
  • 96
    • 0033844419 scopus 로고    scopus 로고
    • Tear secretion by lacrimal glands in transgenic mice lacking water channels AQP1, AQP3, AQP4 and AQP5
    • Moore M, Ma T, Yang B, Verkman AS (2000) Tear secretion by lacrimal glands in transgenic mice lacking water channels AQP1, AQP3, AQP4 and AQP5. Exp Eye Res 70:557-562
    • (2000) Exp Eye Res , vol.70 , pp. 557-562
    • Moore, M.1    Ma, T.2    Yang, B.3    Verkman, A.S.4
  • 99
    • 0031888726 scopus 로고    scopus 로고
    • Effect of expressing the water channel aquaporin-1 on the CO2 permeability of Xenopus oocytes
    • Nakhoul NL, Davis BA, Romero MF, Boron WF (1998) Effect of expressing the water channel aquaporin-1 on the CO2 permeability of Xenopus oocytes. Am J Physiol 274:C543-C548
    • (1998) Am J Physiol , vol.274
    • Nakhoul, N.L.1    Davis, B.A.2    Romero, M.F.3    Boron, W.F.4
  • 101
    • 0041721625 scopus 로고    scopus 로고
    • pH and calcium regulate the water permeability of aquaporin O
    • Nemeth-Cahalan KL, Hall JE (2000) pH and calcium regulate the water permeability of aquaporin O. J Biol Chem 275:6777-6782
    • (2000) J Biol Chem , vol.275 , pp. 6777-6782
    • Nemeth-Cahalan, K.L.1    Hall, J.E.2
  • 102
    • 35649011018 scopus 로고    scopus 로고
    • Zinc modulation of water permeability reveals that Aquaporin 0 functions as a cooperative tetramer
    • Nemeth-Cahalan KL, Kalman K, Froger A, Hall JE (2007) Zinc modulation of water permeability reveals that Aquaporin 0 functions as a cooperative tetramer. J Gen Physiol 130:457-464
    • (2007) J Gen Physiol , vol.130 , pp. 457-464
    • Nemeth-Cahalan, K.L.1    Kalman, K.2    Froger, A.3    Hall, J.E.4
  • 104
    • 0027306170 scopus 로고
    • Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia
    • Nielsen S, Smith BL, Christensen EI, Agre P (1993b) Distribution of the aquaporin CHIP in secretory and resorptive epithelia and capillary endothelia. Proc Natl Acad Sci USA 90:7275-7279
    • (1993) Proc Natl Acad Sci USA , vol.90 , pp. 7275-7279
    • Nielsen, S.1    Smith, B.L.2    Christensen, E.I.3    Agre, P.4
  • 105
    • 0027475944 scopus 로고
    • CHIP28 water channels are localized in constitutively water-permeable segments of the nephron
    • Nielsen S, Smith BL, Christensen EI, Knepper MA, Agre P (1993c) CHIP28 water channels are localized in constitutively water-permeable segments of the nephron. J Cell Biol 120:371-383
    • (1993) J Cell Biol , vol.120 , pp. 371-383
    • Nielsen, S.1    Smith, B.L.2    Christensen, E.I.3    Knepper, M.A.4    Agre, P.5
  • 106
    • 0028889112 scopus 로고
    • Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane
    • Nielsen S, Chou CL, Marples D, Christensen EI, Kishore BK, Knepper MA (1995a) Vasopressin increases water permeability of kidney collecting duct by inducing translocation of aquaporin-CD water channels to plasma membrane. Proc Natl Acad Sci USA 92:1013-1017
    • (1995) Proc Natl Acad Sci USA , vol.92 , pp. 1013-1017
    • Nielsen, S.1    Chou, C.L.2    Marples, D.3    Christensen, E.I.4    Kishore, B.K.5    Knepper, M.A.6
  • 107
    • 0029045996 scopus 로고
    • Aquaporin CHIP water channels in short and long loop descending thin limb and in descending vasa recta in rat kidney
    • Nielsen S, Pallone TL, Smith B, Christensen EI, Agre P, Maunsbach AB (1995b) Aquaporin CHIP water channels in short and long loop descending thin limb and in descending vasa recta in rat kidney. Am J Physiol 268:F1023-F1037
    • (1995) Am J Physiol , vol.268
    • Nielsen, S.1    Pallone, T.L.2    Smith, B.3    Christensen, E.I.4    Agre, P.5    Maunsbach, A.B.6
  • 108
    • 0030657804 scopus 로고    scopus 로고
    • Aquaporins in complex tissues. II. Subcellular distribution in respiratory and glandular tissues of rat
    • Nielsen S, King LS, Christensen BM, Agre P (1997a) Aquaporins in complex tissues. II. Subcellular distribution in respiratory and glandular tissues of rat. Am J Physiol 273:C1549-C1561
    • (1997) Am J Physiol , vol.273
    • Nielsen, S.1    King, L.S.2    Christensen, B.M.3    Agre, P.4
  • 109
    • 0031022918 scopus 로고    scopus 로고
    • Specialized membrane domains for water transport in glial cells: High-resolution immunogold cytochemistry of aquaporin-4 in rat brain
    • Nielsen S, Nagelhus EA, Amiry-Moghaddam M, Bourque C, Agre P, Ottersen OP (1997b) Specialized membrane domains for water transport in glial cells: high-resolution immunogold cytochemistry of aquaporin-4 in rat brain. J Neurosci 17:171-180
    • (1997) J Neurosci , vol.17 , pp. 171-180
    • Nielsen, S.1    Nagelhus, E.A.2    Amiry-Moghaddam, M.3    Bourque, C.4    Agre, P.5    Ottersen, O.P.6
  • 110
    • 11244254968 scopus 로고    scopus 로고
    • Reduced cerebrospinal fluid production and intracranial pressure in mice lacking choroid plexus water channel Aquaporin-1
    • Oshio K, Watanabe H, Song Y, Verkman AS, Manley GT (2005) Reduced cerebrospinal fluid production and intracranial pressure in mice lacking choroid plexus water channel Aquaporin-1. FASEB J 19:76-78
    • (2005) FASEB J , vol.19 , pp. 76-78
    • Oshio, K.1    Watanabe, H.2    Song, Y.3    Verkman, A.S.4    Manley, G.T.5
  • 111
    • 0033955098 scopus 로고    scopus 로고
    • Requirement of aquaporin-1 for NaCl-driven water transport across descending vasa recta
    • Pallone TL, Edwards A, Ma T, Silldorff EP, Verkman AS (2000) Requirement of aquaporin-1 for NaCl-driven water transport across descending vasa recta. J Clin Invest 105:215-222
    • (2000) J Clin Invest , vol.105 , pp. 215-222
    • Pallone, T.L.1    Edwards, A.2    Ma, T.3    Silldorff, E.P.4    Verkman, A.S.5
  • 112
    • 17144383572 scopus 로고    scopus 로고
    • Aquaporin-4 gene disruption in mice reduces brain swelling and mortality in pneumococcal meningitis
    • Papadopoulos MC, Verkman AS (2005) Aquaporin-4 gene disruption in mice reduces brain swelling and mortality in pneumococcal meningitis. J Biol Chem 280:13906-13912
    • (2005) J Biol Chem , vol.280 , pp. 13906-13912
    • Papadopoulos, M.C.1    Verkman, A.S.2
  • 114
    • 4644314913 scopus 로고    scopus 로고
    • Aquaporin-4 facilitates reabsorption of excess fluid in vasogenic brain edema
    • Papadopoulos MC, Manley GT, Krishna S, Verkman AS (2004) Aquaporin-4 facilitates reabsorption of excess fluid in vasogenic brain edema. FASEB J 18:1291-1293
    • (2004) FASEB J , vol.18 , pp. 1291-1293
    • Papadopoulos, M.C.1    Manley, G.T.2    Krishna, S.3    Verkman, A.S.4
  • 115
    • 20644433762 scopus 로고    scopus 로고
    • Reconstituted aquaporin 1 water channels transport CO2 across membranes
    • Prasad GV, Coury LA, Finn F, Zeidel ML (1998) Reconstituted aquaporin 1 water channels transport CO2 across membranes. J Biol Chem 273:33123-33126
    • (1998) J Biol Chem , vol.273 , pp. 33123-33126
    • Prasad, G.V.1    Coury, L.A.2    Finn, F.3    Zeidel, M.L.4
  • 116
    • 0026332210 scopus 로고
    • Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family
    • Preston GM, Agre P (1991) Isolation of the cDNA for erythrocyte integral membrane protein of 28 kilodaltons: Member of an ancient channel family. Proc Natl Acad Sci USA 88:11110-11114
    • (1991) Proc Natl Acad Sci USA , vol.88 , pp. 11110-11114
    • Preston, G.M.1    Agre, P.2
  • 117
    • 0026503030 scopus 로고    scopus 로고
    • Preston GM, Carroll T, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256:385-387
    • Preston GM, Carroll T, Guggino WB, Agre P (1992) Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256:385-387
  • 118
    • 33847768229 scopus 로고    scopus 로고
    • Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei
    • Promeneur D, Liu Y, Maciel J, Agre P, King LS, Kumar N (2007) Aquaglyceroporin PbAQP during intraerythrocytic development of the malaria parasite Plasmodium berghei. Proc Natl Acad Sci USA 104:2211-2216
    • (2007) Proc Natl Acad Sci USA , vol.104 , pp. 2211-2216
    • Promeneur, D.1    Liu, Y.2    Maciel, J.3    Agre, P.4    King, L.S.5    Kumar, N.6
  • 119
    • 0032578454 scopus 로고    scopus 로고
    • Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord
    • Rash JE, Yasumura T, Hudson CS, Agre P, Nielsen S (1998) Direct immunogold labeling of aquaporin-4 in square arrays of astrocyte and ependymocyte plasma membranes in rat brain and spinal cord. Proc Natl Acad Sci USA 95:11981-11986
    • (1998) Proc Natl Acad Sci USA , vol.95 , pp. 11981-11986
    • Rash, J.E.1    Yasumura, T.2    Hudson, C.S.3    Agre, P.4    Nielsen, S.5
  • 120
    • 33645809329 scopus 로고    scopus 로고
    • Severe urinary concentrating defect in renal collecting duct-selective AQP2 conditional-knockout mice
    • Rojek A, Füchtbauer EM, Kwon TH, Frøkiaer J, Nielsen S (2006) Severe urinary concentrating defect in renal collecting duct-selective AQP2 conditional-knockout mice. Proc Natl Acad Sci USA 103:6037-6042
    • (2006) Proc Natl Acad Sci USA , vol.103 , pp. 6037-6042
    • Rojek, A.1    Füchtbauer, E.M.2    Kwon, T.H.3    Frøkiaer, J.4    Nielsen, S.5
  • 122
    • 17144379334 scopus 로고    scopus 로고
    • Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption
    • Saadoun S, Papadopoulos MC, Hara-Chikuma M, Verkman AS (2005a) Impairment of angiogenesis and cell migration by targeted aquaporin-1 gene disruption. Nature 434:786-792
    • (2005) Nature , vol.434 , pp. 786-792
    • Saadoun, S.1    Papadopoulos, M.C.2    Hara-Chikuma, M.3    Verkman, A.S.4
  • 124
    • 0024024829 scopus 로고
    • Polymorphism in the Mr 32,000 Rh protein purified from Rh(D)-positive and -negative erythrocytes
    • Saboori AM, Smith BL, Agre P (1988) Polymorphism in the Mr 32,000 Rh protein purified from Rh(D)-positive and -negative erythrocytes. Proc Natl Acad Sci USA 85:4042-4045.
    • (1988) Proc Natl Acad Sci USA , vol.85 , pp. 4042-4045
    • Saboori, A.M.1    Smith, B.L.2    Agre, P.3
  • 125
    • 0030953720 scopus 로고    scopus 로고
    • Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli
    • Sanders OI, Rensing C, Kuroda M, Mitra B, Rosen BP (1997) Antimonite is accumulated by the glycerol facilitator GlpF in Escherichia coli. J Bacteriol 179:3365-3367
    • (1997) J Bacteriol , vol.179 , pp. 3365-3367
    • Sanders, O.I.1    Rensing, C.2    Kuroda, M.3    Mitra, B.4    Rosen, B.P.5
  • 126
    • 34247104106 scopus 로고    scopus 로고
    • Fast and selective ammonia transport by aquaporin-8
    • Saparov SM, Liu K, Agre P, Pohl P (2007) Fast and selective ammonia transport by aquaporin-8. J Biol Chem 282:5296-5301
    • (2007) J Biol Chem , vol.282 , pp. 5296-5301
    • Saparov, S.M.1    Liu, K.2    Agre, P.3    Pohl, P.4
  • 129
    • 0030031158 scopus 로고    scopus 로고
    • Mutations in the founder of the MIP gene family underlie cataract development in the mouse
    • Shiels A, Bassnett S (1996) Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Nature 12:212-215
    • (1996) Nature , vol.12 , pp. 212-215
    • Shiels, A.1    Bassnett, S.2
  • 130
    • 0025922827 scopus 로고
    • Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins
    • Smith BL, Agre P (1991) Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit oligomer similar to channel proteins. J Biol Chem 266:6407-6415
    • (1991) J Biol Chem , vol.266 , pp. 6407-6415
    • Smith, B.L.1    Agre, P.2
  • 131
    • 0014285021 scopus 로고
    • Characterization of biological membranes by equivalent pores
    • Solomon AK (1968) Characterization of biological membranes by equivalent pores. J Gen Physiol 51:S335-S364
    • (1968) J Gen Physiol , vol.51
    • Solomon, A.K.1
  • 132
    • 0035798592 scopus 로고    scopus 로고
    • Aquaporin-5 dependent fluid secretion in airway submucosal glands
    • Song Y, Verkman AS (2001) Aquaporin-5 dependent fluid secretion in airway submucosal glands. J Biol Chem 276:41288-41292
    • (2001) J Biol Chem , vol.276 , pp. 41288-41292
    • Song, Y.1    Verkman, A.S.2
  • 133
    • 0036623643 scopus 로고    scopus 로고
    • Localization of aquaporin-5 in sweat glands and functional analysis using knockout mice
    • Song Y, Sonawane N, Verkman AS (2002) Localization of aquaporin-5 in sweat glands and functional analysis using knockout mice. J Physiol 541:561-568
    • (2002) J Physiol , vol.541 , pp. 561-568
    • Song, Y.1    Sonawane, N.2    Verkman, A.S.3
  • 134
    • 0034745705 scopus 로고    scopus 로고
    • Abnormal distribution of aquaporin-5 water channel protein in salivary glands from Sjögren's syndrome patients
    • Steinfeld S, Cogan E, King LS, Agre P, Kiss R, Delporte C (2001) Abnormal distribution of aquaporin-5 water channel protein in salivary glands from Sjögren's syndrome patients. Lab Invest 81:143-148
    • (2001) Lab Invest , vol.81 , pp. 143-148
    • Steinfeld, S.1    Cogan, E.2    King, L.S.3    Agre, P.4    Kiss, R.5    Delporte, C.6
  • 135
    • 0035924329 scopus 로고    scopus 로고
    • Structural basis of water-specific transport through the AQP1 water channel
    • Sui H, Han BG, Lee JK, Walian P, Jap BK (2001) Structural basis of water-specific transport through the AQP1 water channel. Nature 414:872-878
    • (2001) Nature , vol.414 , pp. 872-878
    • Sui, H.1    Han, B.G.2    Lee, J.K.3    Walian, P.4    Jap, B.K.5
  • 138
    • 0035799116 scopus 로고    scopus 로고
    • Defective cellular trafficking of lacrimal gland aquaporin-5 in Sjögren's syndrome
    • Tsubota K, Hirai S, King LS, Agre P, Ishida N (2001) Defective cellular trafficking of lacrimal gland aquaporin-5 in Sjögren's syndrome. Lancet 357:688-689
    • (2001) Lancet , vol.357 , pp. 688-689
    • Tsubota, K.1    Hirai, S.2    King, L.S.3    Agre, P.4    Ishida, N.5
  • 141
    • 0013819880 scopus 로고
    • Transport of electrolytes and water across epithelia
    • Ussing HH (1965) Transport of electrolytes and water across epithelia. Harvey Lect 59:1-30
    • (1965) Harvey Lect , vol.59 , pp. 1-30
    • Ussing, H.H.1
  • 143
    • 0025945806 scopus 로고
    • Functional unit of 30-kDa for proximal tubule water channels as revealed by radiation inactivation
    • van Hoek AN, Hom ML, Luthjens LH, de Jong MD, Dempster JA, van Os CH (1991) Functional unit of 30-kDa for proximal tubule water channels as revealed by radiation inactivation. J Biol Chem 266:16633-16635
    • (1991) J Biol Chem , vol.266 , pp. 16633-16635
    • van Hoek, A.N.1    Hom, M.L.2    Luthjens, L.H.3    de Jong, M.D.4    Dempster, J.A.5    van Os, C.H.6
  • 144
    • 58149205292 scopus 로고
    • Aquaporins: Water selective channels in biological membranes
    • van Os CH, Deen PMT, Dempster JA (1994) Aquaporins: water selective channels in biological membranes. Biochim Biophys Acta 1197:291-309
    • (1994) Biochim Biophys Acta , vol.1197 , pp. 291-309
    • van Os, C.H.1    Deen, P.M.T.2    Dempster, J.A.3
  • 147
    • 0024381165 scopus 로고
    • Phospholipid metabolism in Plasmodiuminfected erythrocytes: Guidelines for further studies using radioactive precursor incorporation
    • Vial HJ, Ancelin ML, Thuet MJ, Philippot JR (1989) Phospholipid metabolism in Plasmodiuminfected erythrocytes: guidelines for further studies using radioactive precursor incorporation. Parasitology 98:351-357
    • (1989) Parasitology , vol.98 , pp. 351-357
    • Vial, H.J.1    Ancelin, M.L.2    Thuet, M.J.3    Philippot, J.R.4
  • 148
    • 0019732284 scopus 로고
    • ADH action: Evidence for a membrane shuttle mechanism
    • Wade JB, Stetson DL, Lewis SA (1981) ADH action: Evidence for a membrane shuttle mechanism. Ann NY Acad Sci 372:106-117
    • (1981) Ann NY Acad Sci , vol.372 , pp. 106-117
    • Wade, J.B.1    Stetson, D.L.2    Lewis, S.A.3
  • 150
    • 0034723202 scopus 로고    scopus 로고
    • Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes
    • Yang B, Fukuda N, van Hoek A, Matthay MA, Ma T, Verkman AS (2000) Carbon dioxide permeability of aquaporin-1 measured in erythrocytes and lung of aquaporin-1 null mice and in reconstituted proteoliposomes. J Biol Chem 275:2686-2692
    • (2000) J Biol Chem , vol.275 , pp. 2686-2692
    • Yang, B.1    Fukuda, N.2    van Hoek, A.3    Matthay, M.A.4    Ma, T.5    Verkman, A.S.6
  • 151
    • 0035951776 scopus 로고    scopus 로고
    • Neonatal mortality in an aquaporin-2 knock-in mouse model of recessive nephrogenic diabetes insipidus
    • Yang B, Gillespie A, Carlson EJ, Epstein CJ, Verkman AS (2001) Neonatal mortality in an aquaporin-2 knock-in mouse model of recessive nephrogenic diabetes insipidus. J Biol Chem 276:2775-2779
    • (2001) J Biol Chem , vol.276 , pp. 2775-2779
    • Yang, B.1    Gillespie, A.2    Carlson, E.J.3    Epstein, C.J.4    Verkman, A.S.5
  • 152
    • 33748430962 scopus 로고    scopus 로고
    • Evidence from knockout mice against physiologically significant aquaporin 8-facilitated ammonia transport
    • Yang B, Zhao D, Solenov E, Verkman AS (2006) Evidence from knockout mice against physiologically significant aquaporin 8-facilitated ammonia transport. Am J Physiol Cell Physiol 291:C417-C423
    • (2006) Am J Physiol Cell Physiol , vol.291
    • Yang, B.1    Zhao, D.2    Solenov, E.3    Verkman, A.S.4
  • 153
  • 154
    • 0033545980 scopus 로고    scopus 로고
    • Aquaporin 6: An intracellular vesicle water channel protein in renal epithelia
    • YasuiM, Kwon TH, KnepperMA, Nielsen S, Agre P (1999b) Aquaporin 6: an intracellular vesicle water channel protein in renal epithelia. Proc Natl Acad Sci USA 96:5808-5813
    • (1999) Proc Natl Acad Sci USA , vol.96 , pp. 5808-5813
    • Yasui, M.1    Kwon, T.H.2    Knepper, M.A.3    Nielsen, S.4    Agre, P.5
  • 155
    • 0026806764 scopus 로고
    • Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein
    • Zeidel ML, Ambudkar SV, Smith BL, Agre P (1992) Reconstitution of functional water channels in liposomes containing purified red cell CHIP28 protein. Biochemistry 31:7436-7440
    • (1992) Biochemistry , vol.31 , pp. 7436-7440
    • Zeidel, M.L.1    Ambudkar, S.V.2    Smith, B.L.3    Agre, P.4
  • 156
    • 0028314729 scopus 로고
    • Ultrastructure, pharmacologic inhibition, and transport-selectivity of aquaporin CHIP in proteoliposomes
    • Zeidel ML, Nielsen S, Smith BL, Ambudkar SV, Maunsbach AB, Agre P (1994) Ultrastructure, pharmacologic inhibition, and transport-selectivity of aquaporin CHIP in proteoliposomes. Biochemistry 33:1606-1615
    • (1994) Biochemistry , vol.33 , pp. 1606-1615
    • Zeidel, M.L.1    Nielsen, S.2    Smith, B.L.3    Ambudkar, S.V.4    Maunsbach, A.B.5    Agre, P.6
  • 157
    • 0042531571 scopus 로고    scopus 로고
    • Nickel and extracellular acidification inhibit the water permeability of human aquaporin-3 in lung epithelial cells
    • Zelenina M, Bondar AA, Zelenin S, Aperia A (2003) Nickel and extracellular acidification inhibit the water permeability of human aquaporin-3 in lung epithelial cells. J Biol Chem 278:30037-30043
    • (2003) J Biol Chem , vol.278 , pp. 30037-30043
    • Zelenina, M.1    Bondar, A.A.2    Zelenin, S.3    Aperia, A.4
  • 158
    • 10644251690 scopus 로고    scopus 로고
    • Copper inhibits the water and glycerol permeability of aquaporin-3
    • Zelenina M, Tritto S, Bondar AA, Zelenin S, Aperia A (2004) Copper inhibits the water and glycerol permeability of aquaporin-3. J Biol Chem 279:51939-51943
    • (2004) J Biol Chem , vol.279 , pp. 51939-51943
    • Zelenina, M.1    Tritto, S.2    Bondar, A.A.3    Zelenin, S.4    Aperia, A.5
  • 161
    • 0036016542 scopus 로고    scopus 로고
    • Aquaporin deletion in mice reduces intraocular pressure and aqueous fluid production
    • Zhang D, Vetrivel L, Verkman AS (2002) Aquaporin deletion in mice reduces intraocular pressure and aqueous fluid production. J Gen Physiol 119:561-569
    • (2002) J Gen Physiol , vol.119 , pp. 561-569
    • Zhang, D.1    Vetrivel, L.2    Verkman, A.S.3
  • 162
    • 0025181046 scopus 로고
    • Expression of mRNA coding for kidney and red cell water channels in Xenopus oocytes
    • Zhang R, Logee KA, Verkman AS (1990) Expression of mRNA coding for kidney and red cell water channels in Xenopus oocytes. J Biol Chem 265:15375-15378
    • (1990) J Biol Chem , vol.265 , pp. 15375-15378
    • Zhang, R.1    Logee, K.A.2    Verkman, A.S.3


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