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Am J Physiol Cell Physiol 270: C372-C381, 1996;
0363-6143/96 $5.00
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AJP - Cell Physiology, Vol 270, Issue 1 C372-C381, Copyright © 1996 by American Physiological Society

ARTICLES

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

J. Siner, A. Paredes, C. Hosselet, T. Hammond, K. Strange and H. W. Harris
Division of Nephrology, Children's Hospital, Boston, Massachusetts 02115, USA.

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.


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