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Urinary content of aquaporin 1 and 2 in nephrogenic diabetes insipidus.

P M Deen, R A van Aubel, A F van Lieburg and C H van Os
JASN June 1996, 7 (6) 836-841;
P M Deen
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R A van Aubel
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A F van Lieburg
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C H van Os
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Abstract

Hereditary nephrogenic diabetes insipidus (NDI) is caused by mutations in either the X-chromosomal gene encoding the vasopressin V2-receptor or in the autosomal gene encoding aquaporin-2. Expressed in Xenopus oocytes, the AQP2 gene mutations found in NDl have been shown to reduce the stability of the encoded protein. This study investigated the in vivo stability of mutant and wild-type aquaporin-2 proteins by measuring their excretion in urine of NDl patients and healthy individuals. On immunoblots, the urine samples from healthy volunteers revealed clear aquaporin-1 and aquaporin-2 signals in antidiuretic but not diuretic states. In the urine of a female patient, whose NDl is explained by low expression of the wild-type V2-receptor gene, aquaporin-2 excretion was high and comparable with that in a healthy individual during antidiuresis. In the urine of a male patient with a non-sense mutation in the V2-receptor gene, a weak aquaporin-2 signal was detected. In NDl patients with mutations in the aquaporin-2 gene, aquaporin-2 could not be detected in urine, suggesting a low stability of mutant aquaporin-2 proteins. In four out of seven NDl patients, aquaporin-1 excretion was relatively high, which suggests a compensatory increase in proximal reabsorption in NDl.

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Journal of the American Society of Nephrology
Vol. 7, Issue 6
1 Jun 1996
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Urinary content of aquaporin 1 and 2 in nephrogenic diabetes insipidus.
P M Deen, R A van Aubel, A F van Lieburg, C H van Os
JASN Jun 1996, 7 (6) 836-841;

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Urinary content of aquaporin 1 and 2 in nephrogenic diabetes insipidus.
P M Deen, R A van Aubel, A F van Lieburg, C H van Os
JASN Jun 1996, 7 (6) 836-841;
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Cited By...

  • Nucleotides Downregulate Aquaporin 2 via Activation of Apical P2 Receptors
  • LIP5 Interacts with Aquaporin 2 and Facilitates Its Lysosomal Degradation
  • Glycosylation Is Important for Cell Surface Expression of the Water Channel Aquaporin-2 but Is Not Essential for Tetramerization in the Endoplasmic Reticulum
  • The Role of Putative Phosphorylation Sites in the Targeting and Shuttling of the Aquaporin-2 Water Channel
  • Cell-Biologic and Functional Analyses of Five New Aquaporin-2 Missense Mutations that Cause Recessive Nephrogenic Diabetes Insipidus
  • Detection of Na+ Transporter Proteins in Urine
  • Urinary Excretion of Aquaporin-2 in Rat Is Mediated by a Vasopressin-Dependent Apical Pathway
  • An impaired routing of wild-type aquaporin-2 after tetramerization with an aquaporin-2 mutant explains dominant nephrogenic diabetes insipidus
  • Adenosine Triphosphate-Dependent Transport of Anionic Conjugates by the Rabbit Multidrug Resistance-Associated Protein Mrp2 Expressed in Insect Cells
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