help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS

Biophysical Journal 70: 1316-1325 (1996)
© 1996 the Biophysical Society

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 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
Right arrow reprints & permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Sohma, Y
Right arrow Articles by Gray, M A
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Sohma, Y
Right arrow Articles by Gray, M A

Two barium binding sites on a maxi K+ channel from human vas deferens epithelial cells.

Y Sohma, A Harris, C J Wardle, B E Argent and M A Gray

Department of Physiological Sciences, University Medical School, Newcastle upon Tyne, United Kingdom.

ABSTRACT

Using the patch clamp technique, we have investigated the blockade of maxi-K+ channels present on vas deferens epithelial cells by extracellular Ba2+. With symmetrical 140 mM K+ solutions, Ba2+ produced discrete blocking events consisting of both long closings of seconds duration (slow block) and fast closings of milliseconds duration (flickering block). Kinetic analysis showed that flickering block occurred according to an "open channel blocking" scheme and was eliminated by reducing external K+ to 4.5 mM. Slow block showed a complex voltage-dependence. At potentials between -20 mV and 20 mV, blockade was voltage-dependent; at potentials greater than 20 mV, blockade was voltage-independent, but markedly sensitive to the extracellular K+ concentration. These data reveal that the vas deferens maxi-K+ channel has two Ba2+ binding sites accessible from the extracellular side. Site one is located at the cytoplasmic side of the gating region and binding to this site causes flickering block. Site two is located close to the extracellular mouth of the channel and binding to this site causes slow block.




This article has been cited by other articles:


Home page
J. Physiol.Home page
X. Wu, Y. Yang, P. Gui, Y. Sohma, G. A. Meininger, G. E. Davis, A. P. Braun, and M. J. Davis
Potentiation of large conductance, Ca2+-activated K+ (BK) channels by {alpha}5{beta}1 integrin activation in arteriolar smooth muscle
J. Physiol., March 15, 2008; 586(6): 1699 - 1713.
[Abstract] [Full Text] [PDF]


Home page
J. Gen. Physiol.Home page
J. B. Park, H. J. Kim, P. D. Ryu, and E. Moczydlowski
Effect of Phosphatidylserine on Unitary Conductance and Ba2+ Block of the BK Ca2+-activated K+ Channel: Re-examination of the Surface Charge Hypothesis
J. Gen. Physiol., April 28, 2003; 121(5): 375 - 398.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
M. Bertog, D. J. Smith, A. Bielfeld-Ackermann, J. Bassett, D. J. P. Ferguson, C. Korbmacher, and A. Harris
Ovine male genital duct epithelial cells differentiate in vitro and express functional CFTR and ENaC
Am J Physiol Cell Physiol, May 1, 2000; 278(5): C885 - C894.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
D. C. Devor and R. A. Frizzell
Modulation of K+ channels by arachidonic acid in T84 cells. II. Activation of a Ca2+-independent K+ channel
Am J Physiol Cell Physiol, January 1, 1998; 274(1): C149 - C160.
[Abstract] [Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 1996 by the Biophysical Society.