The Mammalian Urinary Bladder: It's More Than Accommodating

Physiology ◽  
1986 ◽  
Vol 1 (2) ◽  
pp. 61-65 ◽  
Author(s):  
Sk Lewis

Once tacitly assumed to be an inert sac, as evidenced by the lack of information in physiology textbooks, the mammalian urinary bladder epithelium is instead a dynamic system. We stress the structure-function relationship, which allows the bladder epithelium to accomodate large fluctuations in urine volume by orderly insertion and withdrawal of cytoplasmic vesicles. This process, coupled to a recently described hormonally regulated transport system, allows the bladder to maintain urine ionic composition nearly constant. In addition, studies on the bladder have revealed a novel regulatory system of ion transport involving channel degradation and turnover.

Nature ◽  
1982 ◽  
Vol 297 (5868) ◽  
pp. 685-688 ◽  
Author(s):  
Simon A. Lewis ◽  
José L. C. de Moura

Pathology ◽  
1974 ◽  
Vol 6 (4) ◽  
pp. 343-350 ◽  
Author(s):  
Mary E. Schultz ◽  
Michael W. Weldon

1989 ◽  
Vol 66 (1-2) ◽  
pp. 99-106
Author(s):  
Pierre Favard ◽  
Nina Favard ◽  
Qian Long Zhu ◽  
Jacques Bourguet ◽  
Jean-Pierre Lechaire

2013 ◽  
Vol 189 (4S) ◽  
Author(s):  
Sara Colopy ◽  
Dale Bjorling ◽  
William Mulligan ◽  
Wade Bushman

1996 ◽  
Vol 270 (1) ◽  
pp. C372-C381 ◽  
Author(s):  
J. Siner ◽  
A. Paredes ◽  
C. Hosselet ◽  
T. Hammond ◽  
K. Strange ◽  
...  

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.


1982 ◽  
Vol 203 (4) ◽  
pp. 429-440 ◽  
Author(s):  
Joseph Alroy ◽  
Frederick B. Merk ◽  
D. James Morré ◽  
Ronald S. Weinstein

1985 ◽  
Vol 211 (3) ◽  
pp. 239-245 ◽  
Author(s):  
Walter L. Davis ◽  
Ruth Gwendolyn Jones ◽  
Phillip C. Richemont ◽  
David B. P. Goodman

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