J Physiol Boston Smyposia
HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
 QUICK SEARCH:   [advanced]


     


J Physiol Volume 565, Number 3, 709-715, June 15, 2005 DOI: 10.1113/jphysiol.2005.086561
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
Right arrow Supplemental Data
Right arrow All Versions of this Article:
565/3/709    most recent
jphysiol.2005.086561v1
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 Babich, O.
Right arrow Articles by Shirokov, R.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Babich, O.
Right arrow Articles by Shirokov, R.

Rapid Report

Role of extracellular Ca2+ in gating of CaV1.2 channels

Olga Babich1, Dmytro Isaev1 and Roman Shirokov1

1 Department of Pharmacology and Physiology, University of Medicine and Dentistry of New Jersey, New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA

We examined changes in ionic and gating currents in CaV1.2 channels when extracellular Ca2+ was reduced from 10 mM to 0.1 µM. Saturating gating currents decreased by two-thirds (KD {approx} 40 µM) and ionic currents increased 5-fold (KD {approx} 0.5 µM) due to increasing Na+ conductance. A biphasic time dependence for the activation of ionic currents was observed at low [Ca2+], which appeared to reflect the rapid activation of channels that were not blocked by Ca2+ and a slower reversal of Ca2+ blockade of the remaining channels. Removal of Ca2+ following inactivation of Ca2+ currents showed that Na+ currents were not affected by Ca2+-dependent inactivation. Ca2+-dependent inactivation also induced a negative shift of the reversal potential for ionic currents suggesting that inactivation alters channel selectivity. Our findings suggest that activation of Ca2+ conductance and Ca2+-dependent inactivation depend on extracellular Ca2+ and are linked to changes in selectivity.

(Received 11 March 2005; accepted after revision 15 April 2005; first published online 21 April 2005)
Corresponding author R. Shirokov: Department of Pharmacology and Physiology, UMDNJ, New Jersey Medical School, 185 South Orange Avenue, Newark, NJ 07103, USA. Email: roman.shirokov{at}umdnj.edu




This article has been cited by other articles:


Home page
J. Physiol.Home page
C. Peinelt, A. Lis, A. Beck, A. Fleig, and R. Penner
2-Aminoethoxydiphenyl borate directly facilitates and indirectly inhibits STIM1-dependent gating of CRAC channels
J. Physiol., July 1, 2008; 586(13): 3061 - 3073.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
O. Babich, J. Reeves, and R. Shirokov
Block of CaV1.2 Channels by Gd3+ Reveals Preopening Transitions in the Selectivity Filter
J. Gen. Physiol., June 1, 2007; 129(6): 461 - 475.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
O. Babich, V. Matveev, A. L. Harris, and R. Shirokov
Ca2+-dependent Inactivation of CaV1.2 Channels Prevents Gd3+ Block: Does Ca2+ Block the Pore of Inactivated Channels?
J. Gen. Physiol., June 1, 2007; 129(6): 477 - 483.
[Abstract] [Full Text] [PDF]


Home page
JGPHome page
R. Olcese
And Yet It Moves: Conformational States of the Ca2+ Channel Pore
J. Gen. Physiol., June 1, 2007; 129(6): 457 - 459.
[Full Text] [PDF]




HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2005 The Physiological Society.