The mechanisms of aquaporin control in the renal collecting duct

Klussmann, Enno; Maric, Kenan; Rosenthal, Walter

doi:10.1007/bfb0119577

Cited by 92 publications

(53 citation statements)

References 292 publications

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“…This hormone controls transcellular water transport by regulating the redistribution of AQP2-bearing vesicles to the apical membrane of collecting duct principal cells (Knepper and Inoue, 1997;Klussmann et al, 2000). We utilized the collecting duct cell line CD8 stably transfected with the vasopressin-sensitive water channel AQP2 to investigate the functional involvement of SNARE proteins in the process of regulated insertion of the AQP2 water channel.…”

Section: Discussionmentioning

confidence: 99%

Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells

Gouraud

Laera

Calamita

et al. 2002

Journal of Cell Science

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The involvement of soluble N-ethylmaleimide sensitive factor-attachment protein receptor (SNARE) proteins in the cAMP-induced exocytosis of aquaporin 2 (AQP2)containing vesicles was investigated in AQP2-transfected renal CD8 cells. RT-PCR and western blot analysis confirmed the presence of the SNARE homologs VAMP/synaptobrevin-2, syntaxin-1, syntaxin-4 and SNAP-23 in CD8 cells. Tetanus neurotoxin (TeNT) was efficient in cleaving synaptobrevin-like protein both in vitro and in intact CD8 cells incubated with the toxin. TeNT treatment in intact CD8 cells completely abolished cAMP-stimulated AQP2 targeting to the plasma membrane, as assessed by quantification of cell-surface immunoreactivity to an anti-AQP2 antibody raised against a peptide reproducing the extracellular AQP2 C-loop

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Section: Discussionmentioning

confidence: 99%

Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells

Gouraud

Laera

Calamita

et al. 2002

Journal of Cell Science

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“…When AVP is not present, AQP-2 channels are retrieved via endocytosis. In the basolateral membrane of the cell, AQP-3 and AQP-4 channels allow for waters' passage though the cell and into circulation [15][16][17]. Aquaporins are a family of water channels.…”

Section: Introductionmentioning

confidence: 99%

Diabetes Insipidus: A Review

Shapiro¹

2013

J Diabetes Metab

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“…AQP2, a highly glycosylated protein, is processed through the endoplasmic reticulum (ER) and Golgi network where it is folded correctly and then targeted to vesicles that are directed to the subapical region of the plasma membrane. Thereafter, water permeability of the inner medullary collecting duct (IMCD) cells can be rapidly regulated by the antidiuretic hormone arginine vasopressin that binds to heptahelical vasopressin V 2 receptors (V 2 R), located mainly in the basolateral membrane of principal cells (Klussmann et al, 2000;Storm et al, 2003;Ward et al, 1999). Activation of the V 2 R causes stimulation of adenylyl cyclase via the G protein G S , leading to elevation of cAMP and subsequent activation of protein kinase A (PKA) (Wade et al, 1981).…”

Section: Introductionmentioning

confidence: 99%

Loss of calcineurin Aα results in altered trafficking of AQP2 and in nephrogenic diabetes insipidus

Gooch

Guler

Barnes

et al. 2006

Journal of Cell Science

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The serine/threonine phosphatase calcineurin is an important signaling molecule involved in kidney development and function. One potential target of calcineurin action is the water channel aquaporin 2 (AQP2). In this study, we examined the effect of loss of calcineurin Aα (CnAα) on AQP2 function in vivo. CnAα null mice were found to have defective post-natal urine-concentrating ability and an impaired urine-concentrating response to vasopressin. Expression of AQP2 is normal but, paradoxically, vasopressin-mediated phosphorylation of the channel is decreased compared with wild-type littermates and there is no accumulation of AQP2 in the apical membrane. Calcineurin protein and activity was found in innermedullary collecting duct vesicles, and loss of calcineurin expression and activity was associated with a loss of AQP2 in the vesicle fraction. As such, the lack of vasopressin-mediated phosphorylation of AQP2 might be the result of a defect in normal trafficking of AQP2 to apical-targeted vesicles. Likewise, treatment of wild-type mice with cyclosporin A to inhibit calcineurin produces a similarly impaired urine-concentrating response to vasopressin and alterations in AQP2 phosphorylation and trafficking. These experiments demonstrate that, CnAα is required for normal intracellular trafficking of AQP2 and loss of calcineurin protein or activity disrupts AQP2 function.

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The mechanisms of aquaporin control in the renal collecting duct

Cited by 92 publications

References 292 publications

Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells

Functional involvement of VAMP/synaptobrevin-2 in cAMP-stimulated aquaporin 2 translocation in renal collecting duct cells

Diabetes Insipidus: A Review

Loss of calcineurin Aα results in altered trafficking of AQP2 and in nephrogenic diabetes insipidus

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