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

Biophysical Journal 71: 769-777 (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 Uehara, A
Right arrow Articles by Imanaga, I
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Uehara, A
Right arrow Articles by Imanaga, I

Rectification of rabbit cardiac ryanodine receptor current by endogenous polyamines.

A Uehara, M Fill, P Vélez, M Yasukochi and I Imanaga

Department of Physiology, Loyola University Chicago, Maywood, Illinois 60153, USA.

ABSTRACT

The actions of three endogenous polyamines (spermine, spermidine, and putrescine) were defined on Ca2+ release channels (ryanodine receptors, RyRs) isolated from rabbit cardiac sarcoplasmic reticulum. The current-voltage relationship of the RyR channel was N-shaped in the presence of polyamine (1-5 mM). Polyamine blocked conduction near 0 mV, but the blockade was relieved at large potentials. Polyamines acted (blocked) from both sides of the channel. Polyamine efficacy was dependent on current direction and was inversely related to the ion selectivity of the RyR pore. This suggests that polyamine interacts with current-carrying ions in the permeation pathway. The apparent half-block concentration of spermine at 0 mV was < 0.1 mM. The features of polyamine blockade suggest that the polyamines are permeable cationic blockers of the RyR channel. Further, the levels of polyamines found in muscle cells are sufficient to block single RyR channels and thus may alter the sarcoplasmic reticulum Ca2+ release process in situ.




This article has been cited by other articles:


Home page
Biophys. JHome page
X. Lin and R. D. Veenstra
Effect of Transjunctional KCl Gradients on the Spermine Inhibition of Connexin40 Gap Junctions
Biophys. J., July 15, 2007; 93(2): 483 - 495.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
H. Musa, E. Fenn, M. Crye, J. Gemel, E. C. Beyer, and R. D. Veenstra
Amino terminal glutamate residues confer spermine sensitivity and affect voltage gating and channel conductance of rat connexin40 gap junctions
J. Physiol., June 15, 2004; 557(3): 863 - 878.
[Abstract] [Full Text] [PDF]


Home page
Ann. N. Y. Acad. Sci.Home page
L. X. A. TRIPATHY, D. A. PASEK, and G. MEISSNER
Potential for Pharmacology of Ryanadine Receptor/Calcium Release Channels
Ann. N.Y. Acad. Sci., September 16, 1998; 853(1): 130 - 148.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. Iyer and A. H. Delcour
Complex Inhibition of OmpF and OmpC Bacterial Porins by Polyamines
J. Biol. Chem., July 25, 1997; 272(30): 18595 - 18601.
[Abstract] [Full Text] [PDF]


Home page
Pharmacol. Rev.Home page
R. Zucchi and S. Ronca-Testoni
The Sarcoplasmic Reticulum Ca2+ Channel/Ryanodine Receptor: Modulation by Endogenous Effectors, Drugs and Disease States
Pharmacol. Rev., March 1, 1997; 49(1): 1 - 52.
[Abstract] [Full Text] [PDF]


Home page
Pharmacol. Rev.Home page
J. L. Sutko, J. A. Airey, W. Welch, and L. Ruest
The Pharmacology of Ryanodine and Related Compounds
Pharmacol. Rev., March 1, 1997; 49(1): 53 - 98.
[Abstract] [Full Text] [PDF]




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