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Science 17 April 1992:
Vol. 256. no. 5055, pp. 385 - 387
DOI: 10.1126/science.256.5055.385
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Articles

Appearance of Water Channels in Xenopus Oocytes Expressing Red Cell CHIP28 Protein

Gregory M. Preston 1, Tiziana Piazza Carroll 2, William B. Guggino 2, and Peter Agre 1

1 Departments of Medicine and Cell Biology/Anatomy, Johns Hopkins University School of Medicine, Baltimore, MD 21205
2 Department of Physiology, Johns Hopkins University School of Medicine, Baltimore, MD 21205.

Water rapidly crosses the plasma membrane of red blood cells (RBCs) and renal tubules through specialized channels. Although selective for water, the molecular structure of these channels is unknown. The CHIP28 protein is an abundant integral membrane protein in mammalian RBCs and renal proximal tubules and belongs to a family of membrane proteins with unknown functions. Oocytes from Xenopus laevis microinjected with in vitro-transcribed CHIP28 RNA exhibited increased osmotic water permeability; this was reversibly inhibited by mercuric chloride, a known inhibitor of water channels. Therefore it is likely that CHIP28 is a functional unit of membrane water channels.


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Interactions between Plasma Membrane Aquaporins Modulate Their Water Channel Activity.
K. Fetter, V. Van Wilder, M. Moshelion, and F. Chaumont (2004)
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Diurnal Regulation of Water Transport and Aquaporin Gene Expression in Maize Roots: Contribution of PIP2 Proteins.
F. Lopez, A. Bousser, I. Sissoeff, M. Gaspar, B. Lachaise, J. Hoarau, and A. Mahe (2003)
Plant Cell Physiol. 44, 1384-1395
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Water Permeability of C-Terminally Truncated Aquaporin 0 (AQP0 1-243) Observed in the Aging Human Lens.
L. E. Ball, M. Little, M. W. Nowak, D. L. Garland, R. K. Crouch, and K. L. Schey (2003)
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Distribution of aquaporin water channels AQP1 and AQP5 in the ductal system of the human pancreas.
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Countercurrent exchange in the renal medulla.
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Concentration of solutes in the renal inner medulla: interstitial hyaluronan as a mechano-osmotic transducer.
M. A. Knepper, G. M. Saidel, V. C. Hascall, and T. Dwyer (2003)
Am J Physiol Renal Physiol 284, F433-F446
   Abstract »    Full Text »    PDF »
Plasma Membrane Aquaporins Play a Significant Role during Recovery from Water Deficit.
P. Martre, R. Morillon, F. Barrieu, G. B. North, P. S. Nobel, and M. J. Chrispeels (2002)
Plant Physiology 130, 2101-2110
   Abstract »    Full Text »    PDF »
AQP3 Deficiency in Humans and the Molecular Basis of a Novel Blood Group System, GIL.
N. Roudier, P. Ripoche, P. Gane, P. Y. Le Pennec, G. Daniels, J.-P. Cartron, and P. Bailly (2002)
J. Biol. Chem. 277, 45854-45859
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A rat kidney tubule suspension for the study of vasopressin-induced shuttling of AQP2 water channels.
S. Shaw and D. Marples (2002)
Am J Physiol Renal Physiol 283, F1160-F1166
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Delayed onset of brain edema and mislocalization of aquaporin-4 in dystrophin-null transgenic mice.
Z. Vajda, M. Pedersen, E.-M. Fuchtbauer, K. Wertz, H. Stodkilde-Jorgensen, E. Sulyok, T. Doczi, J. D. Neely, P. Agre, J. Frokiar, et al. (2002)
PNAS 99, 13131-13136
   Abstract »    Full Text »    PDF »
TRANSPORT OF SMALL MOLECULES ACROSS CELL MEMBRANES: WATER CHANNELS AND UREA TRANSPORTERS.
B. E. Goodman (2002)
Advan Physiol Educ 26, 146-157
   Abstract »    Full Text »    PDF »
Altering Fish Embryos with Aquaporin-3: An Essential Step Toward Successful Cryopreservation.
M. Hagedorn, S.L. Lance, D.M. Fonseca, F.W. Kleinhans, D. Artimov, R. Fleischer, A.T.M.S. Hoque, M.B. Hamilton, and B.S. Pukazhenthi (2002)
Biol Reprod 67, 961-966
   Abstract »    Full Text »    PDF »
Functional Analysis of Water Channels in Barley Roots.
M. Katsuhara, Y. Akiyama, K. Koshio, M. Shibasaka, and K. Kasamo (2002)
Plant Cell Physiol. 43, 885-893
   Abstract »    Full Text »    PDF »
Ion Permeation of AQP6 Water Channel Protein. SINGLE-CHANNEL RECORDINGS AFTER Hg2+ ACTIVATION.
A. Hazama, D. Kozono, W. B. Guggino, P. Agre, and M. Yasui (2002)
J. Biol. Chem. 277, 29224-29230
   Abstract »    Full Text »    PDF »


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