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Articles in PresS, published online ahead of print July 30, 2002
Am J Physiol Renal Physiol, 10.1152/ajprenal.00043.2002
Submitted on January 31, 2002
Accepted on July 11, 2002
1 Ronald O. Perelman Department of Dermatology and Departments of Pharmacology and Urology, Kaplan Comprehensive Cancer Center, New York University School of Medicine, New York, New York, USA
2 Departments of Medicine and Cell Biology and Physiology, University of Pittsburgh School of Medicine, Pittsburgh, Pennsylvania, USA
3 Lab Of Cellular Biology, NIDCD, National Institutes of Health, Bethesda, Maryland, USA
* To whom correspondence should be addressed. E-mail: zeidel{at}msx.dept-med.pitt.edu.
Although water, small nonelectrolytes and gases are freely permeable through most biological membranes, apical membranes of certain barrier epithelia exhibit extremely low permeabilities to these substances. The role of integral membrane proteins in this barrier function has been unclear. To study this problem, we have ablated the mouse gene encoding uroplakin III, one of the major protein subunits in urothelial apical membranes and measured the permeabilities of these membranes. Ablation of uroplakin III gene greatly diminishes the amounts of uroplakins on the apical urothelial membrane (J. Cell Biol., 151:961-71, 2000). Our results indicate that normal mouse urothelium exhibits high transepithelial resistance, and low urea and water permeabilities. The UPIII-deficient urothelium exhibits a normal transepithelial resistance (normal 2024± 122 Ohms cm2; knockout 2322 ±114; p > 0.5). However, the UPIII-deficient apical membrane has a significantly elevated water permeability (normal 0.91 ± 0.06 cm/sec x 105; knockout 1.83 ± 0.14; p < 0.05). The urea permeability of the UPIII-deficient membrane also increased although to a lesser extent (normal 2.22 ± 0.24 cm/sec x 106; knockout 2.93 ± 0.31; p = 0.12). These results indicate that reduced targeting of uroplakins to the apical membrane does not significantly alter the tight junction barrier, but does double the water permeability We provide the first demonstration that integral membrane proteins contribute to the apical membrane permeability barrier function of urothelium.
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