Role of renal aquaporins in escape from vasopressin-induced antidiuresis in rat.

Ecelbarger, Carolyn A.; Nielsen, Søren; Olson, Beatriz R.; Murase, Takashi; Baker, Erin A.; Knepper, Mark A.; Verbalis, Joseph G.

doi:10.1172/jci119352

Cited by 215 publications

(173 citation statements)

References 33 publications

(46 reference statements)

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“…Water deprivation increased AQP2 expression in rats chronically given V 2 R antagonists (24), indicating that the effect of water deprivation on AQP2 expression is not solely due to AVP-elicited cAMP accumulation. Water loading decreased AQP2 expression, despite chronic administration of the V 2 Rspecific agonist desmopressin (8).…”

Section: Discussionmentioning

confidence: 92%

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Osmolality and solute composition are strong regulators of AQP2 expression in renal principal cells

Storm

Klussmann

Geelhaar

et al. 2003

American Journal of Physiology-Renal Physiology

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. Osmolality and solute composition are strong regulators of AQP2 expression in renal principal cells. Am J Physiol Renal Physiol 284: F189-F198, 2003. First published August 13, 2002; 10.1152/ajprenal.00245.2002The water permeability of the renal collecting duct is regulated by the insertion of aquaporin-2 (AQP2) into the apical plasma membrane of epithelial (principal) cells. Using primary cultured epithelial cells from the inner medulla of rat kidney (IMCD cells), we show that osmolality and solute composition are potent regulators of AQP2 mRNA and protein synthesis, as well as the classical cAMP-dependent pathway, but do not affect the arginine vasopressin-induced AQP2 shuttle. In the presence of the cAMP analog dibutyryl cAMP (DBcAMP, 500 M), NaCl and sorbitol, but not urea, evoked a robust increase of AQP2 expression in IMCD cells, with NaCl being far more potent than sorbitol. cAMP-responsive elementbinding protein phosphorylation increased with DBcAMP concentrations but was not altered by changes in osmolality. In the rat and human AQP2 promoter, we identified a putative tonicity-responsive element. We conclude that, in addition to the arginine vasopressin/cAMP-signaling cascade, a further pathway activated by elevated effective osmolality (tonicity) is crucial for the expression of AQP2 in IMCD cells, and we suggest that the effect is mediated via the tonicityresponsive element. osmolality; aquaporin-2; kidney; gene regulation; toxicity responsive enhancer THE WATER CHANNEL aquaporin-2 (AQP2), expressed in epithelial (principal) cells of renal collecting ducts, is required for the vasopressin-dependent concentration of urine (7). AQP2 abundance increases from the kidney cortex to the inner region of the kidney medulla (29), as does osmolality. The water permeability of the inner medullary collecting duct (IMCD) is rapidly regulated (within minutes) by the antidiuretic hormone arginine vasopressin (AVP), which binds to heptahelical vasopressin V 2 receptors (V 2 R), located mainly in the basolateral plasma membrane of principal cells. Activation of the V 2 R causes stimulation of adenylyl cyclase via the G protein G S , leading to elevation of cAMP. The subsequent activation of protein kinase A (PKA) initiates the translocation of AQP2-bearing vesicles from the cytosol to the plasma membrane, in which AQP2 is inserted by an exocytosis-like process (short-term regulation) (D. Lorenz, A. Krylov, V. Hagen, J. Zipper, W. Rosenthal, P. Pohl, and K. Maric, unpublished observations; 30). In addition, the signaling cascade described above governs the expression of AQP2 (long-term regulation) by PKA-mediated phosphorylation of the transcription factor cAMP-responsive element (CRE)-binding protein (CREB) (13,16). Given the fact that AQP2 biosynthesis is usually shut off shortly after IMCD cells are established in primary culture (10), most studies on AQP2 long-term regulation have been performed using animal models (29, 37). We recently established primary cultured IMCD cells as a model system (17,18,21,22). Thes...

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Section: Discussionmentioning

confidence: 92%

“…Altered TonEBP activity, due to altered medullary tonicity, might be responsible for AVP/cAMP-independent changes in AQP2 expression observed in water loading and thirsting (8,24). The increase in AQP2 expression from kidney cortex to inner medulla (29) is also well explained by an increasing activity of TonEBP from kidney cortex to medulla.…”

Section: Discussionmentioning

confidence: 99%

Osmolality and solute composition are strong regulators of AQP2 expression in renal principal cells

Storm

Klussmann

Geelhaar

et al. 2003

American Journal of Physiology-Renal Physiology

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“…Plasma sodium concentration may rise, but tends to stabilize in the hyponatraemic range. Further animal studies have shown the`escape from antidiuresis' to be due to a decrease in the expression of aquaporin-2 water channels (AQP 2 ) without a concomitant fall in the expression of the basolateral aquaporin water channels (Ecelbarger et al, 1997).…”

Section: Euvolaemic Hyponatraemiamentioning

confidence: 99%

Hyponatraemia

Smith

McKenna

Thompson

2000

Clinical Endocrinology

121

103

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“…Accordingly, normal and AVP-deficient Brattleboro rats infused with AVP over a period of several days display increased levels of AQP2 expression (10,13,11). Conversely, animals administered with V 2 -receptor antagonists display decreased levels of AQP2 expression (12).…”

mentioning

confidence: 99%

Dual Influence of Aldosterone on AQP2 Expression in Cultured Renal Collecting Duct Principal Cells

Hasler

Mordasini

Bianchi

et al. 2003

Journal of Biological Chemistry

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In the renal collecting duct (CD) the major physiological role of aldosterone is to promote Na ؉ reabsorption. In addition, aldosterone may also influence CD water permeability elicited by vasopressin (AVP). We have previously shown that endogenous expression of the aquaporin-2 (AQP2) water channel in immortalized mouse cortical CD principal cells (mpkCCD C14 ) grown on filters is dramatically increased by administration of physiological concentrations of AVP. In the present study, we investigated the influence of aldosterone on AQP2 expression in mpkCCD C14 cells by RNase protection assay and Western blot analysis. Aldosterone reduced AQP2 mRNA and protein expression when administered together with AVP for short periods of time (<24 h). For longer periods of time, however, aldosterone increased AQP2 protein expression despite sustained low expression levels of AQP2 mRNA. Both events were dependent on mineralocorticoid receptor occupancy because they were both induced by a low concentration of aldosterone (10 ؊9 M) and were abolished by the mineralocorticoid receptor antagonist canrenoate. Inhibition of lysosomal AQP2 protein degradation increased AQP2 protein expression in AVP-treated cells, an effect that was potentiated by aldosterone. Finally, both aldosterone and actinomycin D delayed AQP2 protein decay following AVP washout, but in a non-cumulative manner. Taken together, our data suggest that aldosterone tightly modulates AQP2 protein expression in cultured mpkCCD C14 cells by increasing AQP2 protein turnover while maintaining low levels of AQP2 mRNA expression.Water permeability of the renal collecting duct (CD) 1 depends almost exclusively on the antidiuretic hormone [8-arginine]vasopressin (AVP), which exerts its action principally through tight regulation of aquaporin-2 (AQP2) expression. AQP2 belongs to the family of water channel proteins that facilitate osmotically driven water movement across cell membranes. At least six members of the AQP family (AQP1, AQP2, AQP3, AQP4, AQP6, and AQP7) are expressed in the kidney (1-4) and three of them, AQP2, AQP3, and AQP4, are expressed in CD principal cells (5-7). AVP increases CD water permeability by binding to the vasopressin V 2 -receptor located in the basolateral membrane of CD principal cells, an event that promotes AQP2 translocation from intracellular storage vesicles to the apical membrane (8). Water exits the cells through AQP3 and AQP4 water channels expressed in the basolateral membrane of CD cells. This process, induced by acute increases in AVP plasma concentration, occurs within minutes and is reversible. Declining levels of circulating AVP quickly lead to endocytotic retrieval of apical AQP2 and to reduced CD water permeability (8).Besides this rapid action, AVP also controls AQP2 expression over longer periods of time (from several hours to several days) (9). Accordingly, normal and AVP-deficient Brattleboro rats infused with AVP over a period of several days display increased levels of AQP2 expression (10, 13, 11). Conversely, animals admin...

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Role of renal aquaporins in escape from vasopressin-induced antidiuresis in rat.

Cited by 215 publications

References 33 publications

Osmolality and solute composition are strong regulators of AQP2 expression in renal principal cells

Osmolality and solute composition are strong regulators of AQP2 expression in renal principal cells

Hyponatraemia

Dual Influence of Aldosterone on AQP2 Expression in Cultured Renal Collecting Duct Principal Cells

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