Am J Physiol Cell Physiol Watch the video to see how APS reaches out to developing nations.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
QUICK SEARCH:   [advanced]


     

Am J Physiol Cell Physiol 267: C1013-C1026, 1994;
0363-6143/94 $5.00
This Article
Right arrow Full Text (PDF)
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
Services
Right arrow Email this article to a friend
Right arrow Similar articles in this journal
Right arrow Similar articles in PubMed
Right arrow Alert me to new issues of the journal
Right arrow Download to citation manager
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Tzan, C. J.
Right arrow Articles by Lewis, S. A.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Tzan, C. J.
Right arrow Articles by Lewis, S. A.

AJP - Cell Physiology, Vol 267, Issue 4 C1013-C1026, Copyright © 1994 by American Physiological Society

ARTICLES

Mammalian urinary bladder permeability is altered by cationic proteins: modulation by divalent cations

C. J. Tzan, J. R. Berg and S. A. Lewis
Department of Physiology and Biophysics, University of Texas Medical Branch, Galveston 77555.

It was previously demonstrated that protamine sulfate (PS, a cationic polypeptide) as well as synthetic cationic polypeptides (CpP, e.g., polylysine and polyarginine) caused an increase in the apical membrane conductance of the mammalian urinary bladder epithelium that was voltage dependent. The membrane conductance induced by these CpP was mediated by a saturable binding site and was partially blocked by CpP (self-inhibition). The PS-induced membrane conductance can be modified by polyvalent cations at three sites. The first site was to competitively inhibit the interaction of PS with an apical membrane binding site. The second site was to reversibly block the conductance induced by PS. The relative binding affinity (block of PS-induced conductance) sequence was as follows: UO2(2+) > La3+ > Mn2+ > Ba2+ > or = Ca2+ > Sr2+. Although La3+, Mn2+, Ba2+, Ca2+, and Sr2+ inhibited > or = 81% of the PS-induced conductance, UO2(2+) inhibited only 51% and Mg2+ was without effect. The third site was to increase the rate of loss of the PS-induced conductance from the apical membrane. Although neither carbodiimides (carboxyl group reactive reagents) nor neuraminidase (cleaves sialic acid residues) altered the effect of PS on the urinary bladder conductance, PS increased the conductance of lipid bilayers composed of negatively charged phospholipids. A candidate for the binding site might be the negatively charged phosphate groups of membrane lipids.


This article has been cited by other articles:


Home page
 Am. J. Physiol. Regul. Integr. Comp. Physiol.Home page
R. Shioyama, Y. Aoki, H. Ito, Y. Matsuta, K. Nagase, N. Oyama, Y. Miwa, H. Akino, Y. Imamura, and O. Yokoyama
Long-lasting breaches in the bladder epithelium lead to storage dysfunction with increase in bladder PGE2 levels in the rat
Am J Physiol Regulatory Integrative Comp Physiol, August 1, 2008; 295(2): R714 - R718.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
T. J. Kleine, G. J. Gleich, and S. A. Lewis
Eosinophil peroxidase increases membrane permeability in mammalian urinary bladder epithelium
Am J Physiol Cell Physiol, March 1, 1999; 276(3): C638 - C647.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Renal Physiol.Home page
J. R. Berg, C. M. Spilker, and S. A. Lewis
Modulation of polymyxin B effects on mammalian urinary bladder
Am J Physiol Renal Physiol, August 1, 1998; 275(2): F204 - F215.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
T. J. Kleine, G. J. Gleich, and S. A. Lewis
Eosinophil major basic protein increases membrane permeability in mammalian urinary bladder epithelium
Am J Physiol Cell Physiol, July 1, 1998; 275(1): C93 - C103.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Visit Other APS Journals Online