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

Biophysical Journal 71: 759-768 (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 Hilgemann, D W
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Hilgemann, D W

Unitary cardiac Na+, Ca2+ exchange current magnitudes determined from channel-like noise and charge movements of ion transport.

D W Hilgemann

Department of Physiology, University of Texas Southwestern Medical Center at Dallas 75235-9040, USA. hilgeman@utsw.swmed.edu

ABSTRACT

The cardiac Na+, Ca2+ exchanger (NCX1) is thought to achieve a high turnover rate, but all estimates to date are indirect. Two new strategies demonstrate that maximum unitary exchange currents are about 1 fA (6000 unitary charges per s) and that they fluctuate between on and off levels similar to ion channel currents. First, exchange current noise has been identified in small cardiac patches with properties expected for a gated transport process. Noise power density spectra correlate well with exchanger inactivation kinetics, and the noise has a predicted bell-shaped dependence on the activation states of the exchanger. From the magnitudes of exchange current noise, maximum unitary exchange currents are estimated to be 0.6-1.3 fA. Second, charge movements with rates of approximately 5000 s-1 have been isolated for the transport of both Na+ and Ca2+ in giant membrane patches using nonsaturating ion concentrations. The Na+ transport reactions are disabled or "immobilized" by exchanger inactivation reactions, thus confirming that inactivation generates fully inactive exchanger states.




This article has been cited by other articles:


Home page
J. Biol. Chem.Home page
A. A. Zdebik, G. Zifarelli, E.-Y. Bergsdorf, P. Soliani, O. Scheel, T. J. Jentsch, and M. Pusch
Determinants of Anion-Proton Coupling in Mammalian Endosomal CLC Proteins
J. Biol. Chem., February 15, 2008; 283(7): 4219 - 4227.
[Abstract] [Full Text] [PDF]


Home page
J. Physiol.Home page
A. Yaradanakul, S. Feng, C. Shen, V. Lariccia, M.-J. Lin, J. Yang, Kang T. M., P. Dong, H. L. Yin, J. P. Albanesi, et al.
Dual control of cardiac Na+ Ca2+ exchange by PIP2: electrophysiological analysis of direct and indirect mechanisms
J. Physiol., August 1, 2007; 582(3): 991 - 1010.
[Abstract] [Full Text] [PDF]


Home page
J Biomol ScreenHome page
S. Geibel, N. Flores-Herr, T. Licher, and H. Vollert
Establishment of Cell-Free Electrophysiology for Ion Transporters: Application for Pharmacological Profiling
J Biomol Screen, April 1, 2006; 11(3): 262 - 268.
[Abstract] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
T. L. Radzyukevich, A. E. Moseley, D. A. Shelly, G. A. Redden, M. M. Behbehani, J. B. Lingrel, R. J. Paul, and J. A. Heiny
The Na+-K+-ATPase {alpha}2-subunit isoform modulates contractility in the perinatal mouse diaphragm
Am J Physiol Cell Physiol, November 1, 2004; 287(5): C1300 - C1310.
[Abstract] [Full Text] [PDF]


Home page
Cardiovasc ResHome page
K. R Sipido, P. G.A Volders, M. A Vos, and F. Verdonck
Altered Na/Ca exchange activity in cardiac hypertrophy and heart failure: a new target for therapy?
Cardiovasc Res, March 1, 2002; 53(4): 782 - 805.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
M. Shigekawa and T. Iwamoto
Cardiac Na+-Ca2+ Exchange : Molecular and Pharmacological Aspects
Circ. Res., May 11, 2001; 88(9): 864 - 876.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
R. T. Szerencsei, J. E. Tucker, C. B. Cooper, R. J. Winkfein, P. J. Farrell, K. Iatrou, and P. P. M. Schnetkamp
Minimal Domain Requirement for Cation Transport by the Potassium-dependent Na/Ca-K Exchanger. COMPARISON WITH AN NCKX PARALOG FROM CAENORHABDITIS ELEGANS
J. Biol. Chem., January 7, 2000; 275(1): 669 - 676.
[Abstract] [Full Text] [PDF]


Home page
J. Biol. Chem.Home page
M. Condrescu, B. M. Hantash, Y. Fang, and J. P. Reeves
Mode-specific Inhibition of Sodium-Calcium Exchange during Protein Phosphatase Blockade
J. Biol. Chem., November 19, 1999; 274(47): 33279 - 33286.
[Abstract] [Full Text] [PDF]


Home page
Physiol. Rev.Home page
M. P. Blaustein and W. J. Lederer
Sodium/Calcium Exchange: Its Physiological Implications
Physiol Rev, July 1, 1999; 79(3): 763 - 854.
[Abstract] [Full Text] [PDF]


Home page
Physiol. Rev.Home page
A. Meir, S. Ginsburg, A. Butkevich, S. G. Kachalsky, I. Kaiserman, R. Ahdut, S. Demirgoren, and R. Rahamimoff
Ion Channels in Presynaptic Nerve Terminals and Control of Transmitter Release
Physiol Rev, July 1, 1999; 79(3): 1019 - 1088.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
Y. Fang, M. Condrescu, and J. P. Reeves
Regulation of Na+/Ca2+ exchange activity by cytosolic Ca2+ in transfected Chinese hamster ovary cells
Am J Physiol Cell Physiol, July 1, 1998; 275(1): C50 - C55.
[Abstract] [Full Text] [PDF]


Home page
Am. J. Physiol. Cell Physiol.Home page
B. Linck, Z. Qiu, Z. He, Q. Tong, D. W. Hilgemann, and K. D. Philipson
Functional comparison of the three isoforms of the Na+/Ca2+ exchanger (NCX1, NCX2, NCX3)
Am J Physiol Cell Physiol, February 1, 1998; 274(2): C415 - C423.
[Abstract] [Full Text] [PDF]


Home page
Circ. Res.Home page
K. R. Sipido, M. Maes, and F. Van de Werf
Low Efficiency of Ca2+ Entry Through the Na+-Ca2+ Exchanger as Trigger for Ca2+ Release From the Sarcoplasmic Reticulum : A Comparison Between L-Type Ca2+ Current and Reverse-Mode Na+-Ca2+ Exchange
Circ. Res., December 19, 1997; 81(6): 1034 - 1044.
[Abstract] [Full Text]




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