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Fate of antidiuretic hormone water channel proteins after retrieval from apical membrane.

Publication ,  Journal Article
Zeidel, ML; Hammond, TG; Wade, JB; Tucker, J; Harris, HW
Published in: Am J Physiol
September 1993

In toad bladder granular cells, antidiuretic hormone (ADH) stimulates insertion of vesicles containing water channels (WCV), markedly increasing apical membrane osmotic water permeability (Pf). After withdrawal of ADH stimulation, WCV are removed from the apical membrane and fluid-phase markers endocytosed from the apical solution appear predominantly in endosomes at 10-15 min and multivesicular bodies at 30-60 min. Although the luminal contents of this endocytic pathway have been well characterized, the fate of membrane proteins, including functional ADH water channels in these vesicles remains unclear. Using electron microscopic, flow cytometric, and stopped-flow fluorescence measurements and characterization of labeled vesicle proteins, we examined the fate of membrane proteins contained within WCV. The protein complements of endosomes harvested after 10, 30, and 60 min of ADH withdrawal were similar. Selective covalent labeling of apical proteins during ADH stimulation followed by ADH reversal for 30 or 60 min showed that apical proteins colocalize with fluid-phase marker-labeled endosomes at all times, and most apically labeled protein bands present in the 10-min fraction were also present in the 30- and 60-min endosome fractions. Endosomes at 10 and 30 min but not at 60 min contained functional water channels revealed by high Pf and proton permeability, low activation energy of Pf, and sensitivity of Pf to mercurial reagents. We conclude that a portion of apically exposed membrane proteins, including candidate water channel proteins, travel together with fluid-phase markers from 10-min endosomes into later endosomal compartments. Functional water channels may be inactivated or some essential protein component selectively sorted away between 30 and 60 min after ADH withdrawal.

Duke Scholars

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

September 1993

Volume

265

Issue

3 Pt 1

Start / End Page

C822 / C833

Location

United States

Related Subject Headings

  • Water
  • Vasopressins
  • Urinary Bladder
  • Tissue Distribution
  • Permeability
  • Microscopy, Electron
  • Ion Channels
  • Epithelium
  • Epithelial Cells
  • Cell Membrane
 

Citation

APA
Chicago
ICMJE
MLA
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Zeidel, M. L., Hammond, T. G., Wade, J. B., Tucker, J., & Harris, H. W. (1993). Fate of antidiuretic hormone water channel proteins after retrieval from apical membrane. Am J Physiol, 265(3 Pt 1), C822–C833. https://doi.org/10.1152/ajpcell.1993.265.3.C822
Zeidel, M. L., T. G. Hammond, J. B. Wade, J. Tucker, and H. W. Harris. “Fate of antidiuretic hormone water channel proteins after retrieval from apical membrane.Am J Physiol 265, no. 3 Pt 1 (September 1993): C822–33. https://doi.org/10.1152/ajpcell.1993.265.3.C822.
Zeidel ML, Hammond TG, Wade JB, Tucker J, Harris HW. Fate of antidiuretic hormone water channel proteins after retrieval from apical membrane. Am J Physiol. 1993 Sep;265(3 Pt 1):C822–33.
Zeidel, M. L., et al. “Fate of antidiuretic hormone water channel proteins after retrieval from apical membrane.Am J Physiol, vol. 265, no. 3 Pt 1, Sept. 1993, pp. C822–33. Pubmed, doi:10.1152/ajpcell.1993.265.3.C822.
Zeidel ML, Hammond TG, Wade JB, Tucker J, Harris HW. Fate of antidiuretic hormone water channel proteins after retrieval from apical membrane. Am J Physiol. 1993 Sep;265(3 Pt 1):C822–C833.

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

September 1993

Volume

265

Issue

3 Pt 1

Start / End Page

C822 / C833

Location

United States

Related Subject Headings

  • Water
  • Vasopressins
  • Urinary Bladder
  • Tissue Distribution
  • Permeability
  • Microscopy, Electron
  • Ion Channels
  • Epithelium
  • Epithelial Cells
  • Cell Membrane