help button home button Biophys. J.
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
This Article
Right arrow Full Text
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 Hill, A. P.
Right arrow Articles by Sitsapesan, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hill, A. P.
Right arrow Articles by Sitsapesan, R.

Biophys J, June 2002, p. 3037-3047, Vol. 82, No. 6

DIDS Modifies the Conductance, Gating, and Inactivation Mechanisms of the Cardiac Ryanodine Receptor

Adam Parker Hill* and Rebecca Sitsapesandagger

 *Imperial College of Science, Technology and Medicine, London SW3 6LY; and  dagger University of Bristol, Bristol BS8 1TD, United Kingdom

The effects of the covalent modifier of amino groups, 4,4'-diisothiocyanostilbene-2,2'-disulfonic acid (DIDS) on the single-channel properties of purified sheep cardiac ryanodine receptors (RyR) incorporated into planar phospholipid bilayers were investigated. DIDS increased single-channel conductance and open probability (Po) and induced unique modifications to the voltage-dependence of gating. The effects of DIDS on conduction and gating were irreversible within the time scale of the experiments, and both effects were dependent on the permeant ion. DIDS induced a greater increase in conductance with Ca2+ (20%) compared with K+ (8%) as the permeant ion. After modification by DIDS, all channels could be rapidly inactivated in a voltage-dependent manner. The open probability of the DIDS-modified channel decreased with increasing positive or negative transmembrane potentials; however, inactivation was only observed at negative potentials. Our results demonstrate that inactivation of RyR channels is dependent on the ligand activating the channel, and this will have consequences for the control and termination of sarcoplasmic reticulum Ca2+ release in cardiac cells.

Biophys J, June 2002, p. 3037-3047, Vol. 82, No. 6
© 2002 by the Biophysical Society   0006-3495/02/06/3037/11  $2.00


This article has been cited by other articles:


Home page
 Am. J. Physiol. Heart Circ. Physiol.Home page
D. Guo, L. Young, C. Patel, Z. Jiao, Y. Wu, T. Liu, P. R. Kowey, and G.-X. Yan
Calcium-activated chloride current contributes to action potential alternations in left ventricular hypertrophy rabbit
Am J Physiol Heart Circ Physiol, July 1, 2008; 295(1): H97 - H104.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Pharmacol.Home page
A. P. Hill, O. Kingston, and R. Sitsapesan
Functional Regulation of the Cardiac Ryanodine Receptor by Suramin and Calmodulin Involves Multiple Binding Sites
Mol. Pharmacol., May 1, 2004; 65(5): 1258 - 1268.
[Abstract] [Full Text]

Home page
 J. Biol. Chem.Home page
A. F. Dulhunty, S. M. Curtis, S. Watson, L. Cengia, and M. G. Casarotto
Multiple Actions of Imperatoxin A on Ryanodine Receptors: INTERACTIONS WITH THE II-III LOOP "A" FRAGMENT
J. Biol. Chem., March 19, 2004; 279(12): 11853 - 11862.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
E. R. O'Neill, M. M. Sakowska, and D. R. Laver
Regulation of the Calcium Release Channel from Skeletal Muscle by Suramin and the Disulfonated Stilbene Derivatives DIDS, DBDS, and DNDS
Biophys. J., March 1, 2003; 84(3): 1674 - 1689.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2002 by the Biophysical Society.