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Physiological Reviews, Vol. 82, No. 1, January 2002, pp. 205-244; 10.1152/physrev.00024.2001.
Copyright ©2002 by the American Physiological Society
The Water and Salt Research Center, Institute of Anatomy, and Institute of Experimental Clinical Research, University of Aarhus, Aarhus, Denmark; University of Leeds, Leeds, United Kingdom; Dongguk University, Kyungju, Korea; Department of Biological Chemistry, Johns Hopkins University School of Medicine, Baltimore; and National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland
Nielsen, Søren,
Jørgen Frøkiær,
David Marples,
Tae-Hwan Kwon,
Peter Agre, and
Mark A. Knepper.
Aquaporins in the Kidney: From Molecules to Medicine. Physiol. Rev. 82: 205-244, 2002.
The discovery of aquaporin-1 (AQP1)
answered the long-standing biophysical question of how water
specifically crosses biological membranes. In the kidney, at least
seven aquaporins are expressed at distinct sites. AQP1 is extremely
abundant in the proximal tubule and descending thin limb and is
essential for urinary concentration. AQP2 is exclusively expressed in
the principal cells of the connecting tubule and collecting duct and is
the predominant vasopressin-regulated water channel. AQP3 and AQP4
are both present in the basolateral plasma membrane of collecting duct
principal cells and represent exit pathways for water reabsorbed
apically via AQP2. Studies in patients and transgenic mice have
demonstrated that both AQP2 and AQP3 are essential for urinary
concentration. Three additional aquaporins are present in the kidney.
AQP6 is present in intracellular vesicles in collecting duct
intercalated cells, and AQP8 is present intracellularly at low
abundance in proximal tubules and collecting duct principal cells, but
the physiological function of these two channels remains undefined.
AQP7 is abundant in the brush border of proximal tubule cells and is
likely to be involved in proximal tubule water reabsorption. Body water
balance is tightly regulated by vasopressin, and multiple studies now
have underscored the essential roles of AQP2 in this. Vasopressin
regulates acutely the water permeability of the kidney collecting duct
by trafficking of AQP2 from intracellular vesicles to the apical plasma
membrane. The long-term adaptational changes in body water balance
are controlled in part by regulated changes in AQP2 and AQP3 expression
levels. Lack of functional AQP2 is seen in primary forms of diabetes
insipidus, and reduced expression and targeting are seen in several
diseases associated with urinary concentrating defects such as acquired nephrogenic diabetes insipidus, postobstructive polyuria, as well as
acute and chronic renal failure. In contrast, in conditions with water
retention such as severe congestive heart failure, pregnancy, and
syndrome of inappropriate antidiuretic hormone secretion, both
AQP2 expression levels and apical plasma membrane targetting are
increased, suggesting a role for AQP2 in the development of water
retention. Continued analysis of the aquaporins is providing detailed
molecular insight into the fundamental physiology and pathophysiology
of water balance and water balance disorders.
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