Comparison of the water transporting properties of MIP and AQP1

Journal of Membrane Biology

Volumn 159, Issue 1, 1997, Pages 29-39

  Chandy, G ^a,c   Zampighi, G A ^b   Kreman, M ^b   Hall, J E ^a  

^a UNIVERSITY OF CALIFORNIA   (United States)

^b UNIVERSITY OF CALIFORNIA   (United States)

^c UNIVERSITY OF CALIFORNIA   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

AQUAPORIN; LENS PROTEIN; MEMBRANE PROTEIN;

ANIMAL CELL; ARTICLE; CONTROLLED STUDY; ELECTRON MICROSCOPY; GENE EXPRESSION; GENE TRANSFER; MUTANT; NONHUMAN; OOCYTE; WATER PERMEABILITY; WATER TRANSPORT; XENOPUS LAEVIS;

ANIMALS; AQUAPORIN 1; AQUAPORINS; CALORIMETRY; CELL MEMBRANE; CELL MEMBRANE PERMEABILITY; EYE PROTEINS; FEMALE; FREEZE FRACTURING; ION CHANNELS; MEMBRANE GLYCOPROTEINS; MICROSCOPY, ELECTRON; MUTAGENESIS; OOCYTES; SEQUENCE DELETION; THERMODYNAMICS; WATER; XENOPUS LAEVIS;

ANIMALIA; XENOPUS LAEVIS;

EID: 0030883373     PISSN: 00222631     EISSN: None     Source Type: Journal    
DOI: 10.1007/s002329900266     Document Type: Article

References (60)

1. Aerts, T., Xia, J., Siegers, H., de Block, J., Clauwaert, J. 1990. Hydrodynamic characterization of the major intrinsic protein from the bovine lens fiber membranes. J. Biol. Chem. 265:8675-8680
2. Agre, P., Preston, G.M., Smith, B.L., Jung, J.S., Raina, S., Moon, C., Guggino, W.B., Nielsen, S. 1993. Aquaporin CHIP: the archetypal molecular water channel. Am. J. Physiol. 265:F463-76
3. Alcala, J., Cenedella, R.J., Katar, M. 1985. Limited proteolysis of MP26 in lens fiber plasma membranes of the U18666A-induced cataract in rats. Curr. Eye Res. 4:1001-1005
4. Alcala, J., Lieska, N., Maisel, H. 1975. Protein composition of bovine lens cortical fiber cell membranes. Exp. Eye Res. 21:591-595
5. Alcala, J., Unakar, N.J., Katar, M., Tsui, J.Y. 1986. Limited proteolysis of MP26 in lens fiber plasma membranes of the galactose-induced cataract in the rat. Curr. Eye Res. 5:697-703
6. Alcala, J., Unakar, N., Katar, M., Tsui, J. 1990. Reversal of the limited proteolysis of MP26 during the reversal and prevention of the galactose cataract in rat lenses. Curr. Eye Res. 9:225-232
7. Bloemendal, H., Zweers, A., Vermorken, F., Dunia, I., Benedetti, E.L. 1972. The plasma membranes of the eye lens fibres. Biochemical and structural characterization. Cell Diff. 1:91-106
8. David, L.L., Takemoto, L.J., Anderson, R.S., Shearer, T.R. 1988. Proteolytic changes in main intrinsic polypeptide (MIP26) from membranes in selenite cataract. Curr. Eye Res. 7:411-417
9. Dick, E.G., Dick, D.A.T. 1970. The effect of surface microvilli on the water permeability of single toad oocytes. J. Cell Sci. 6:451-476
10. Ehring, G.R., Lagos, N., Zampighi, G.A., Hall, J.E. 1991. Phosphorylation modulates the voltage dependence of channels reconstituted from the major intrinsic protein of lens fiber membranes. J. Membrane Biol. 126:75-88
11. Ehring, G.R., Zampighi, G.A., Horwitz, J., Bok, D., Hall, J.E. 1990. Properties of channels reconstituted from the major intrinsic protein of lens fiber membranes. J. Gen. Physiol. 96:631-664
12. Fettiplace, R., Haydon, D.A. 1980. Water permeability of lipid membranes. Physiol. Rev. 60:510-550
13. Finkelstein, A. 1987. Water Movement through Lipid Bilayers. Pores, and Plasma Membranes. Theory and Reality, 228 4. New York. Distinguished Lecture Series of the Society of General Physiologists
14. Fortin, M.G., Morrison, N.A., Verma, D.P. 1987. Nodulin-26, a peribacteroid membrane nodulin is expressed independently of the development of the peribacteroid compartment. Nucleic Acids Res. 15:813-824
15. Girsch, S.J., Peracchia, C. 1985. Lens cell-to-cell channel protein: I. Self-assembly into liposomes and permeability regulation by calmodulin. J. Membrane Biol. 83:217-225
16. Gooden, M., Rintoul, D., Takehana, M., Takemoto, L. 1985. Major intrinsic polypeptide (MIP26K) from lens membrane: Reconstitution into vesicles and inhibition of channel forming activity by peptide antiserum. Biochem. Biophys. Res. Comm. 128:993-999
17. Gooden, M.M., Takemoto, L.J., Rintoul, D.A. 1985. Reconstitution of MIP26 from single human lenses into artificial membranes. I. Differences in pH sensitivity of cataractous vs. normal human lens fiber cell proteins. Curr. Eye Res. 4:1107-1115
18. Gorin, M.B., Yancey, S.B., Cline, J., Revel, J.P., Horwitz, J. 1984. The major intrinsic protein (MIP) of the bovine lens fiber membrane: characterization and structure based on cDNA cloning. Cell. 39:49-59.
19. +/ glucose cotransporter expression by protein kinases in Xenopus laevis oocytes. J. Biol. Chem. 271:14740-14746
20. Ho, S.N., Hunt, H.D., Horton, R.M., Pullen, J.K., Pease, L.R. 1989. Site-directed mutagenesis by overlap extension using the polymerase chain reaction. Gene. 77:51-9
21. Isom, L.L., Ragsdale, D.S., De Jongh, K.S., Westenbroek, R.E., Reber, R.F., Scheuer, T., Catterall, W.A. 1995. Structure and function of the beta 2 subunit of brain sodium channels, a transmembrane glycoprotein with a CAM motif. Cell. 83:433-442
22. Jap, B.K., Li, H. 1995. Structure of the osmo-regulated H2O-channel. AQP-CHIP, in projection at 3.5 A resolution. J. Mol. Biol. 251:413-420
23. Kushmerick, C., Rice, S.J., Baldo, G.J., Haspel, H.C., Mathias, R.T. 1995. Ion, water and neutral solute transport in Xenopus oocytes expressing frog lens MIP. Exp. Eye Res. 61:351-362
24. Laemmli, U.K. 1970. Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature. 227:680-685
25. Lampe, P.D., Johnson, R.G. 1990. Amino acid sequence of the in vivo phosphorylation sites in the main intrinsic protein (MIP) of lens membrane. Eur. J. Biochem. 194:541-547
26. Lo, W.K., Kuck, J.F.R. 1990. Alterations of urea-insoluble membrane traction, MP26, of Emory mouse lenses in aging and cataractogenesis. Ophthalmic Res. 22:82-88
27. +/glucose cotransporter. PNAS. 93:13367-13370
28. Lucké, B., McCutcheon, M. 1932. The living cell as an osmotic system and its permeability to water. Physiol. Rev. 12:68-139
29. Maisel, H. 1985. The Ocular lens: structure, function, and pathology. 1-479 New York
30. Mitra, A.K., Yeager, M., Van Hoek, A.N., Wiener, M.C., Verkman, A.S. 1994. Projection structure of the CHIP28 water channel in lipid bilayer membranes at 12-A resolution. Biochemistry 33:12735-12740
31. Mulders, S.M., Preston, G.M., Deen, P.M., Guggino, W.B., Van Os, C.H., Agre, P. 1995. Water channel properties of major intrinsic protein of lens. J. Biol. Chem. 270:9010-9016
32. Nielsen, S., Smith, B.L., Christensen, E.I., Knepper, M.A., Agre, P. 1993. CHIP28 water channels are localized in constitutively water-permeable segments of the nephron. J. Cell Biol. 120:371-383
33. Preston, G.M., 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
34. Preston, G.M., Carroll, T.P., Guggino, W.B., Agre, P. 1992. Appearance of water channels in Xenopus oocytes expressing red cell CHIP28 protein. Science 256:385-387
35. Roy, D., Spector, A., Farnsworth, P.N. 1979. Human lens membrane: Comparison of major intrinsic polypeptides from young and old lenses isolated by a new methodology. Exp. Eye Res. 28:353-358
36. Sanger, F., Nicklen, S., Coulson, A.R. 1977. DNA sequencing with chain-terminating inhibitors. Proc. Natl. Acad. Sci. USA 74:5463-5467
37. Scaglione, B.A., Rintoul, D.A. 1989. A fluorescence-quenching assay for measuring permeability of reconstituted lens MIP26. Invest. Ophthalmol. Vis. Sci. 30:961-966
38. Shen, L., Shrager, P., Girseh, S.J., Donaldson, P.J., Peracchia, C. 1991. Channel reconstitution in liposomes and planar bilayers with HPLC-purified MIP26 of bovine lens. J. Membrane Biol. 124:21-32
39. Shi, L.B., Skach, W.R., Verkman, A.S. 1994. Functional independence of monomeric CHIP28 water channels revealed by expression of wild-type mutant heterodimers. J. Biol. Chem. 269:10417-10422
40. Shiels, A., Bassnett, S. 1996. Mutations in the founder of the MIP gene family underlie cataract development in the mouse. Nature Genetics 12:212-215
41. Smith, B.L., Agre, P. 1991. Erythrocyte Mr 28,000 transmembrane protein exists as a multisubunit of oligomer similar to channel proteins. J. Biol. Chem. 266:6507-6415
42. Smith, C.P., Chater, K.F. 1988. Structure and regulation of controlling sequences for the Streptomyces coelicolor glycerol operon. J. Mol. Biol. 204:569-580
43. Tanaka, M., Russell, P., Smith, S., Uga, S., Kuwabara, T., Kinoshita, J.H. 1980. Membrane alterations during cataract development in the Nakano mouse lens. Invest. Ophthalmol. Vis. Sci. 19:619-629
44. Van Aelst, L., Hohmann, S., Zimmermann, F.K., Jans, A.W., Thevelein, J.M. 1991. A yeast homologue of the bovine lens fibre MIP gene family complements the growth defect of a Saccharomyces cerevisiae mutant on fermentable sugars but not its defect in glucose-induced RAS-mediated cAMP signalling. EMBO. J. 10:2095-2104
45. Van Hoek, A.N., Verkman, A.S. 1992. Functional reconstitution of the isolated erythrocyte water channel CHIP28. J. Biol. Chem. 267:18267-18269
46. Verbavatz, J.M., Brown, D., Sabolic, I., Valenti, G., Ausiello, D.A., Van Hoek, A.N., Ma, T., Verkman, A.S. 1993. Tetrameric assembly of CHIP28 water channels in liposomes and cell membranes: a freeze-fracture study. J. Cell Biol. 123:605-618
47. Walz, T., Smith, B.L., Agre, P., Engel, A. 1994a. The three-dimensional structure of human erythrocyte aquaporin CHIP. Embo. J. 13:2985-2993
48. Walz, T., Smith, B.L., Zeidel, M.L., Engel, A., Agre, P. 1994b. Biologically active two-dimensional crystals of aquaporin CHIP. J. Biol. Chem. 269:1583-1586
49. Weaver, C.D., Shomer, N.H., Louis, C.F., Roberts, D.M. 1994. Nodulin 26, a nodule-specific symbiosome membrane protein from soybean, is an ion channel. J. Biol. Chem. 269:17858-17862
50. Yool, A.J., Stamer, W.D., Regan, J.W. 1996. Forskolin stimulation of water and cation permeability in Aquaporin1 water channels. Science 273:1216-1218
51. Zampighi, G.A., Hall, J.E., Ehring, G.R., Simon, S.A. 1989. The structural organization and protein composition of lens fiber junctions. J. Cell Biol. 108:2255-2275
52. Zampighi, G.A., Hall., J.E., Kreman, M. 1985a. Purified lens junctional protein forms channels in planar lipid films. Proc. Natl. Acad. Sci. USA 82:8468-8472
53. Zampighi, G.A., Hall, J.E., Kreman, M. 1985b. Purified lens junctional protein forms channels in planar lipid films. Proc. Natl. Acad. Sci USA 82:8468-8472
54. Zampighi, G.A., Kreman, M., Boorer, K.J., Loo, D.D.F., Bezanilla, F., Chandy, G., Hall, J.E., Wright, E.M. 1995. A method for determining the unitary functional capacity of cloned channels and transporters expressed in Xenopus laevis oocytes. J. Membrane Biol. 148:65-68
55. Zampighi, G., Kreman, M., Ramon, F., Moreno, A.L., Simon, S.A. 1988. Structural characteristics of gap junctions. I. Channel number in coupled and uncoupled conditions. J. Cell Biol. 106:1667-1678
56. Zampighi, G., Simon, S.A., Robertson, J.D., McIntosh, T.J., Costello, M.J. 1982. On the structural organization of isolated bovine lens fiber junctions. J. Cell Biol. 93:175-189
57. Zeidel, M.L., Neilsen, S., Smith, B.L., Ambudkar, S.V., Maunsbach, A.B., Agre, P. 1994. Ultrastructure, pharmacologic inhibition, and transport selectivity of aquaporin channel-forming integral protein in proteoliposomes. Biochemistry 33:1606-1615
58. Zhang, R., Alper, S.L., Thorens, B., Verkman, A.S. 1991. Evidence from oocyte expression that the erythrocyte water channel is distinct from band 3 and the glucose transporter. J. Clin. Invest. 88:1553-1558
59. Zhang, R.B., Skach, W., Hasegawa, H., Vanhoek, A.N., Verkman, A.S. 1993. Cloning, functional analysis and cell localization of a kidney proximal tubule water transporter homologous to Chip28. J. Cell Biol. 120:359-369
60. Zhang, R.B., Verkman, A.S. 1991. Water and urea permeability properties of Xenopus oocytes: expression of mRNA from toad urinary bladder. Am. J. Physiol. 260:C26-34