New Mutations in the AQP2 Gene in Nephrogenic Diabetes Insipidus Resulting in Functional but Misrouted Water Channels

Journal of the American Society of Nephrology

Volumn 8, Issue 2, 1997, Pages 242-248

  Mulders, Sabine M ^a   Knoers, Nine V A M ^a   Van Lieburg, Angenita F ^a   Monnens, Leo A H ^a   Leumann, Ernst ^b   Wühl, Elke ^c   Schober, Edith ^d   Rijss, Johan P L ^a   Van Os, Carel H ^a   Deen, Peter M T ^a  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

^b Universitats Kinderklinik   (Switzerland)

^c UNIVERSITY OF HEIDELBERG   (Germany)

^d Univ Kinderklinik Wien   (Austria)

Author keywords

[No Author keywords available]

Indexed keywords

AQP2 PROTEIN, HUMAN; AQUAPORIN; AQUAPORIN 2; AQUAPORIN 6; ION CHANNEL;

ADOLESCENT; ADULT; ANIMAL; ARTICLE; CASE REPORT; FEMALE; GENETICS; HUMAN; IN VITRO STUDY; MALE; METABOLISM; NEPHROGENIC DIABETES INSIPIDUS; OOCYTE; POINT MUTATION; PRESCHOOL CHILD; RECESSIVE GENE; XENOPUS;

ADOLESCENT; ADULT; ANIMALS; AQUAPORIN 2; AQUAPORIN 6; AQUAPORINS; CHILD, PRESCHOOL; DIABETES INSIPIDUS, NEPHROGENIC; FEMALE; GENES, RECESSIVE; HUMANS; ION CHANNELS; MALE; OOCYTES; POINT MUTATION; XENOPUS;

EID: 0031067089     PISSN: 10466673     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Article

References (37)

1. Preston GM, Carroll TP, Guggino WB, Agre P: Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256: 385-387, 1992
2. Fushimi K, Uchida S, Hara Y, Hirata Y, Marumo F, Sasaki S: Cloning and expression of apical membrane water channel of rat kidney collecting tubule. Nature (Lond) 361: 549-552, 1993,
3. Echevarria M, Windhager EE, Tate SS, Frindt G: Cloning and expression of AQP3, a water channel from the medullary collecting duct of rat kidney. Proc Natl Acad Sci USA 91: 10997-11001, 1994
4. Ishibashi K, Sasaki S, Fushimi K, Uchida S, Kuwahara M, Saito H, Furukawa T, Nakajima K, Yamaguchi Y, Gojobori T, Marumo F: 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
5. Ma T, Frigeri A, Hasegawa H, Verkman AS: 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
6. Jung JS, Bhat RV, Preston GM, Guggino WB, Baraban JM, Agre P: Molecular characterization of an aquaporin cDNA from brain: Candidate osmoreceptor and regulator of water balance. Proc Natl Acad Sci USA 91: 13052-13056, 1994
7. Nielsen S, Smith BL, Christensen EI, Knepper MA, Agre P: CHIP28 water channels are localized in constitutively water-permeable segments of the nephron. J Cell Biol 120: 371-383, 1993
8. Katsura T, Verbavatz JM, Farinas J, Ma TH, Ausiello DA, Verkman AS, Brown D: Constitutive and regulated membrane expression of aquaporin 1 and aquaporin 2 water channels in stably transfected LLC-PK1 epithelial cells. Proc Natl Acad Sci USA 92: 7212-7216, 1995
9. Marples D, Knepper MA, Christensen EI, Nielsen S: Redistribution of aquaporin-2 water channels induced by vasopressin in rat kidney inner medullary collecting duct. Am J Physiol 38: C655-C664, 1995
10. Nielsen S, Chou CL, Marples D, Christensen EI, Kishore BK, Knepper MA: 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
11. Sabolic I, Katsura T, Verbavatz JM, Brown D: The AQP2 water channel: Effect of vasopressin treatment, microtubule disruption, and distribution in neonatal rats. J Membr Biol 143: 165-175, 1995
12. Yamamoto T, Sasaki S, Fushimi K, Ishibashi K, Yaoita E, Kawasaki K, Marumo F, Kihara I: Vasopressin increases AQP-CD water channel in apical membrane of collecting duct cells in Brattleboro rats. Am J Physiol 268: C1546-C1551, 1995
13. Frigeri A, Gropper MA, Turck CW, Verkman AS: Immunolocalization of the mercurial-insensitive water channel and glycerol intrinsic protein in epithelial cell plasma membranes. Proc Natl Acad Sci USA 92: 4328-4331, 1995
14. Preston GM, Smith BL, Zeidel ML, Moulds JJ, Agre P: Mutations in aquaporin-1 in phenotypically normal humans without functional CHIP water channels. Science 265: 1585-1587, 1994
15. Deen PMT, Verdijk MA, Knoers NVAM, Wieringa B, Monncns LAH, van Os CH, van Oost BA: Requirement of human renal water channel aquaporin-2 for vasopressin-dependent concentration of urine. Science 264: 92-95, 1994
16. van Lieburg AF, Verdijk MA, Knoers VVAM, van Essen AJ, Proesmans W, Mallmann R, Monnens LAH, van Oost BA, van Os CH, Deen PMT: Patients with autosomal nephrogenic diabetes insipidus homozygous for mutations in the aquaporin 2 water-channel gene. Am J Hum Genet 55: 648-652, 1994
17. Deen PM, Croes H, van Aubel RA, Ginsel LA, van Os CH: Water channels encoded by mutant aquaporin-2 genes in nephrogenic diabetes insipidus are impaired in their cellular routing. J Clin Invest 95: 2291-2296, 1995
18. Hattori M, Sakaki Y: Dideoxy sequencing method using denatured plasmid templates. Anal Biochem 152: 232-238, 1986
19. Chomczynski P, Sacchi N: Single-step method of RNA isolation by acid guanidinium thiocyanate-phenol-chloroform extraction. Anal Biochem 162: 156-159, 1987
20. Deen PM, Dempster JA, Wieringa B, van Os CH: Isolation of a cDNA for rat CHIP28 water channel: High mRNA expression in kidney cortex and inner medulla. Biochem Biophys Res Commun 188: 1267-1273, 1992
21. Feinberg AP, Vogelstein B: A technique for radiolabeling DNA restriction endonuclease fragments to high specific activity. Anal Biochem 132: 6-13, 1983
22. Destree OH, Bendig MM, De Laaf RT, Koster JG: Organization of Xenopus histone gene variants within clusters and their transcriptional expression. Biochim Biophys Acta 782: 132-141, 1984
23. Wall DA, Patel S: Isolation of plasma membrane complexes from Xenopus oocytes. J Membr Biol 107: 189-201, 1989
24. Laemmli UK: Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature (Lond) 227: 680-685, 1970
25. McLean IW, Nakane PK: Periodate-lysine-paraformaldehyde fixative. A new fixation for immunoelectron microscopy. J Histochem Cytochem 22: 1077-1083, 1974
26. Reizer J, Reizer A, Saier MHJ: 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 28: 235-257, 1993
27. Knoers NVAM, van Os CH: Molecular and cellular defects in nephrogenic diabetes insipidus. Curr Opin Nephrol Hypertens 1996, in press.
28. Deen PM, Weghuis DO, Sinke RJ, Geurts van Kessel A, Wieringa B, van Os CH: Assignment of the human gene for the water channel of renal collecting duct Aquaporin 2 (AQP2) to chromosome 12 region q12→q13. Cytogenet Cell Genet 66: 260-262, 1994
29. Bonifacino JS, Lippincott Schwartz J: Degradation of proteins within the endoplasmic reticulum. Curr Opin Cell Biol 3: 592-600, 1991
30. Halban PA, Irminger JC: Sorting and processing of secretory proteins. Biochem J 299: 1-18, 1994
31. Hammond C, Helenius A: Quality control in the secretory pathway. Curr Opin Cell Biol 7: 523-529, 1995
32. Jung JS, Preston GM, Smith BL, Guggino WB, Agre P: Molecular structure of the water channel through aquaporin CHIP. The hourglass model. J Biol Chem 269: 14648-14654, 1994
33. Preston GM, Jung JS, Guggino WB, Agre P: Membrane topology of aquaporin CHIP. Analysis of functional epitope-scanning mutants by vectorial proteolysis. J Biol Chem 269: 1668-1673, 1994
34. Bai LQ, Fushimi K, Sasaki S, Marumo F: Structure of aquaporin-2 vasopressin water channel. J Biol Chem 271: 5171-5176, 1996
35. Denning GM, Anderson MP, Amara JF, Marshall J, Smith AE, Welsh MJ: Processing of mutant cystic fibrosis transmembrane conductance regulator is temperature-sensitive. Nature (Lond) 358: 761-764, 1992
36. Bross P, Andresen BS, Winter V, Kräutle F, Jensen TG, Nandy A, Kolvraa S, Ghisla S, Bolund I, Gregersen N: Co-overexpression of bacterial GroESL chaperonins partly overcomes non-productive folding and tetramer assembly of E. coli-expressed human medium-chain acyl-CoA dehydrogenase (MCAD) carrying the prevalent disease-causing K304E mutation. Biochim Biophys Acta 1182: 264-274, 1993
37. Thomas PJ, Qu BH, Pedersen PL: Defective protein folding as a basis of human disease. Trends Biochem Sci 20: 456-459, 1995