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SYMPOSIUM |
*
Department of Cell Biology, Institute of Anatomy, University of Aarhus,
Aarhus, Denmark
Department of Cell Biology, Institute of Experimental Clinical Research,
Aarhus University Hospital, Aarhus, Denmark
School of Biomedical Sciences, University of Leeds, United
Kingdom.
Correspondence to Dr. Søren Nielsen, Department of Cell Biology, Institute of Anatomy, University of Aarhus, DK-8000 Aarhus, Denmark. Phone: +45 8942 3046; Fax: +45 8619 8664; E-mail: SN{at}ANA.AAU.DK
Abstract
Abstract. The discovery of aquaporin membrane water channels by Agre and coworkers answered a long-standing biophysical question of how water specifically crosses biologic membranes, and provided insight, at the molecular level, into the fundamental physiology of water balance and the pathophysiology of water balance disorders. Of nine aquaporin isoforms, at least six are known to be present in the kidney at distinct sites along the nephron and collecting duct. Aquaporin-1 (AQP1) is extremely abundant in the proximal tubule and descending thin limb, where it appears to provide the chief route for proximal nephron water reabsorption. AQP2 is abundant in the collecting duct principal cells and is the chief target for vasopressin to regulate collecting duct water reabsorption. Acute regulation involves vasopressin-regulated trafficking of AQP2 between an intracellular reservoir and the apical plasma membrane. In addition, AQP2 is involved in chronic/adaptational regulation of body water balance achieved through regulation of AQP2 expression. Importantly, multiple studies have now identified a critical role of AQP2 in several inherited and acquired water balance disorders. This concerns inherited forms of nephrogenic diabetes insipidus and several, much more common acquired types of nephrogenic diabetes insipidus where AQP2 expression and/or targeting are affected. Conversely, AQP2 expression and targeting appear to be increased in some conditions with water retention such as pregnancy and congestive heart failure. AQP3 and AQP4 are basolateral water channels located in the kidney collecting duct, and AQP6 and AQP7 appear to be expressed at lower abundance at several sites including the proximal tubule. This review focuses mainly on the role of AQP2 in water balance regulation and in the pathophysiology of water balance disorders.
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R. S. Pedersen, H. Bentzen, J. N. Bech, and E. B. Pedersen Effect of water deprivation and hypertonic saline infusion on urinary AQP2 excretion in healthy humans Am J Physiol Renal Physiol, May 1, 2001; 280(5): F860 - F867. [Abstract] [Full Text] [PDF]
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L. N. Nejsum, T.-H. Kwon, D. Marples, A. Flyvbjerg, M. A. Knepper, J. Frokiar, and S. Nielsen Compensatory increase in AQP2, p-AQP2, and AQP3 expression in rats with diabetes mellitus Am J Physiol Renal Physiol, April 1, 2001; 280(4): F715 - F726. [Abstract] [Full Text] [PDF]
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E. Feraille and A. Doucet Sodium-Potassium-Adenosinetriphosphatase-Dependent Sodium Transport in the Kidney: Hormonal Control Physiol Rev, January 1, 2001; 81(1): 345 - 418. [Abstract] [Full Text] [PDF]
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D. Promeneur, T.-H. Kwon, M. Yasui, G.-H. Kim, J. Frokiar, M. A. Knepper, P. Agre, and S. Nielsen Regulation of AQP6 mRNA and protein expression in rats in response to altered acid-base or water balance Am J Physiol Renal Physiol, December 1, 2000; 279(6): F1014 - F1026. [Abstract] [Full Text] [PDF]
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 E.J. Kamsteeg, I. Heijnen, C.H. van Os, and P.M.T. Deen The Subcellular Localization of an Aquaporin-2 Tetramer Depends on the Stoichiometry of Phosphorylated and Nonphosphorylated Monomers J. Cell Biol., November 13, 2000; 151(4): 919 - 930. [Abstract] [Full Text] [PDF]
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T.-H. Kwon, U. H. Laursen, D. Marples, A. B. Maunsbach, M. A. Knepper, J. Frokiar, and S. Nielsen Altered expression of renal AQPs and Na+ transporters in rats with Lithium-induced NDI Am J Physiol Renal Physiol, September 1, 2000; 279(3): F552 - F564. [Abstract] [Full Text] [PDF]
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D. Promeneur, T.-H. Kwon, J. Frokiar, M. A. Knepper, and S. Nielsen Vasopressin V2-receptor-dependent regulation of AQP2 expression in Brattleboro rats Am J Physiol Renal Physiol, August 1, 2000; 279(2): F370 - F382. [Abstract] [Full Text] [PDF]
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 S. Nielsen, T.-H. Kwon, J. Frokiar, and M. A. Knepper Key Roles of Renal Aquaporins in Water Balance and Water-Balance Disorders Physiology, June 1, 2000; 15(3): 136 - 143. [Abstract] [Full Text] [PDF]
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J. Loffing, D. Loffing-Cueni, A. Macher, S. C. Hebert, B. Olson, M. A. Knepper, B. C. Rossier, and B. Kaissling Localization of epithelial sodium channel and aquaporin-2 in rabbit kidney cortex Am J Physiol Renal Physiol, April 1, 2000; 278(4): F530 - F539. [Abstract] [Full Text] [PDF]
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A. N. van Hoek, T. Ma, B. Yang, A. S. Verkman, and D. Brown Aquaporin-4 is expressed in basolateral membranes of proximal tubule S3 segments in mouse kidney Am J Physiol Renal Physiol, February 1, 2000; 278(2): F310 - F316. [Abstract] [Full Text] [PDF]
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T.-H. Kwon, J. Frokiaer, P. Fernandez-Llama, M. A. Knepper, and S. Nielsen Reduced abundance of aquaporins in rats with bilateral ischemia-induced acute renal failure: prevention by alpha -MSH Am J Physiol Renal Physiol, September 1, 1999; 277(3): F413 - F427. [Abstract] [Full Text] [PDF]
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W. Foster, A. Helm, I. Turnbull, H. Gulati, B. Yang, A. S. Verkman, and W. R. Skach Identification of Sequence Determinants That Direct Different Intracellular Folding Pathways for Aquaporin-1 and Aquaporin-4 J. Biol. Chem., October 27, 2000; 275(44): 34157 - 34165. [Abstract] [Full Text] [PDF]
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B. Yang, A. Gillespie, E. J. Carlson, C. J. Epstein, and A. S. Verkman Neonatal Mortality in an Aquaporin-2 Knock-in Mouse Model of Recessive Nephrogenic Diabetes Insipidus J. Biol. Chem., January 19, 2001; 276(4): 2775 - 2779. [Abstract] [Full Text] [PDF]
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C. Zhang, J. M. Sands, and J. D. Klein Vasopressin rapidly increases phosphorylation of UT-A1 urea transporter in rat IMCDs through PKA Am J Physiol Renal Physiol, January 1, 2002; 282(1): F85 - F90. [Abstract] [Full Text] [PDF]
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