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Cloning of an aquaporin homologue present in water channel containing endosomes of toad urinary bladder.

Publication ,  Journal Article
Siner, J; Paredes, A; Hosselet, C; Hammond, T; Strange, K; Harris, HW
Published in: Am J Physiol
January 1996

Regulation of total body water balance in amphibians by antidiuretic hormone (ADH) contributed to their successful colonization of terrestrial habitats approximately 200-300 million years ago. In the mammalian kidney, ADH modulates epithelial cell apical membrane water permeability (Pf) by fusion and retrieval of cytoplasmic vesicles containing water channel proteins called aquaporins (AQPs). To determine the role of AQPs in ADH-elicited Pf in amphibians, we have identified and characterized a unique AQP from Bufo marinus called AQP toad bladder (AQP-TB). AQP-TB possesses many structural features common to other AQPs, AQP-TB is expressed abundantly in ADH-responsive tissues, including toad urinary bladder and skin as well as lung, skeletal muscle, kidney, and brain. In a manner identical to that reported for the mammalian ADH-elicited water channel AQP2, AQP-TB expression is increased significantly by intervals of dehydration or chronic ADH stimulation. However, expression of AQP-TB protein in Xenopus laevis oocytes does not significantly increase oocyte Pf. The lack of expression of functional AQP-TB water channels in oocytes may result from intracellular sequestration of AQP-TB due to the presence of a YXRF sequence motif present in its carboxyterminal domain.

Duke Scholars

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

January 1996

Volume

270

Issue

1 Pt 1

Start / End Page

C372 / C381

Location

United States

Related Subject Headings

  • Water
  • Vasopressins
  • Urinary Bladder
  • Tissue Distribution
  • Sequence Homology
  • Oocytes
  • Molecular Sequence Data
  • Ion Channels
  • Immunoblotting
  • Flow Cytometry
 

Citation

APA
Chicago
ICMJE
MLA
NLM
Siner, J., Paredes, A., Hosselet, C., Hammond, T., Strange, K., & Harris, H. W. (1996). Cloning of an aquaporin homologue present in water channel containing endosomes of toad urinary bladder. Am J Physiol, 270(1 Pt 1), C372–C381. https://doi.org/10.1152/ajpcell.1996.270.1.C372
Siner, J., A. Paredes, C. Hosselet, T. Hammond, K. Strange, and H. W. Harris. “Cloning of an aquaporin homologue present in water channel containing endosomes of toad urinary bladder.Am J Physiol 270, no. 1 Pt 1 (January 1996): C372–81. https://doi.org/10.1152/ajpcell.1996.270.1.C372.
Siner J, Paredes A, Hosselet C, Hammond T, Strange K, Harris HW. Cloning of an aquaporin homologue present in water channel containing endosomes of toad urinary bladder. Am J Physiol. 1996 Jan;270(1 Pt 1):C372–81.
Siner, J., et al. “Cloning of an aquaporin homologue present in water channel containing endosomes of toad urinary bladder.Am J Physiol, vol. 270, no. 1 Pt 1, Jan. 1996, pp. C372–81. Pubmed, doi:10.1152/ajpcell.1996.270.1.C372.
Siner J, Paredes A, Hosselet C, Hammond T, Strange K, Harris HW. Cloning of an aquaporin homologue present in water channel containing endosomes of toad urinary bladder. Am J Physiol. 1996 Jan;270(1 Pt 1):C372–C381.

Published In

Am J Physiol

DOI

ISSN

0002-9513

Publication Date

January 1996

Volume

270

Issue

1 Pt 1

Start / End Page

C372 / C381

Location

United States

Related Subject Headings

  • Water
  • Vasopressins
  • Urinary Bladder
  • Tissue Distribution
  • Sequence Homology
  • Oocytes
  • Molecular Sequence Data
  • Ion Channels
  • Immunoblotting
  • Flow Cytometry