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


     

J Physiol Volume 529, Number 1, 119-130, November 15, 2000
This Article
Right arrow Full Text
Right arrow Full Text (PDF)
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 Kepplinger, K. J. F.
Right arrow Articles by Romanin, C.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Kepplinger, K. J. F.
Right arrow Articles by Romanin, C.
The Journal of Physiology (2000), 529.1, pp. 119-130
© Copyright 2000 The Physiological Society

Molecular determinant for run-down of L-type Ca2+ channels localized in the carboxyl terminus of the alpha1C subunit

Klaus J. F. Kepplinger, Günter Förstner, Heike Kahr, Katharina Leitner, Patrick Pammer, Klaus Groschner†, Nikolai M. Soldatov* and Christoph Romanin

Institute for Biophysics, University of Linz, A-4040 Linz, Austria, †Institute of Pharmacology and Toxicology, University of Graz, A-8010 Graz, Austria and *National Institute on Aging, NIH, Baltimore, MD 21224-6825, USA

  1. The role of the sequence 1572-1651 in the C-terminal tail of the alpha1C subunit in run-down of Ca2+ channels was studied by comparing functional properties of the conventional alpha1C,77 channel with those of three isoforms carrying alterations in this motif.

  2. The pore-forming alpha1C subunits were co-expressed with alpha2delta and beta2a subunits in HEK-tsA201 cells, a subclone of the human embryonic kidney cell line, and studied by whole-cell and single-channel patch-clamp techniques.

  3. Replacement of amino acids 1572-1651 in alpha1C,77 with 81 different amino acids leading to alpha1C,86 significantly altered run-down behaviour. Run-down of Ba2+ currents was rapid with alpha1C,77 channels, but was slow with alpha1C,86.

  4. Transfer of the alpha1C,86 segments L (amino acids 1572-1598) or K (amino acids 1595-1652) into the alpha1C,77 channel yielded alpha1C,77L and alpha1C,77K channels, respectively, the run-down of which resembled more that of alpha1C,77. These results demonstrate that a large stretch of sequence between residues 1572 and 1652 of alpha1C,86 renders Ca2+ channels markedly resistant to run-down.

  5. The protease inhibitor calpastatin added together with ATP was able to reverse the run-down of alpha1C,77 channels. Calpastatin expression was demonstrated in the HEK-tsA cells by Western blot analysis.

  6. These results indicate a significant role of the C-terminal sequence 1572-1651 of the alpha1C subunit in run-down of L-type Ca2+ channels and suggest this sequence as a target site for a modulatory effect by endogenous calpastatin.



This article has been cited by other articles:


Home page
 Cardiovasc ResHome page
B. J.J.M. Brundel, L. Ke, A.-J. Dijkhuis, X. Qi, A. Shiroshita-Takeshita, S. Nattel, R. H. Henning, and H. H. Kampinga
Heat shock proteins as molecular targets for intervention in atrial fibrillation
Cardiovasc Res, June 1, 2008; 78(3): 422 - 428.
[Abstract] [Full Text] [PDF]

Home page
 Proc. Natl. Acad. Sci. USAHome page
S. Tiwari, Y. Zhang, J. Heller, D. R. Abernethy, and N. M. Soldatov
Atherosclerosis-related molecular alteration of the human CaV1.2 calcium channel {alpha}1C subunit
PNAS, November 7, 2006; 103(45): 17024 - 17029.
[Abstract] [Full Text] [PDF]

Home page
 Am. J. Physiol. Cell Physiol.Home page
J.-J. Xu, L.-Y. Hao, A. Kameyama, and M. Kameyama
Calmodulin reverses rundown of L-type Ca2+ channels in guinea pig ventricular myocytes
Am J Physiol Cell Physiol, December 1, 2004; 287(6): C1717 - C1724.
[Abstract] [Full Text] [PDF]

Home page
 JGPHome page
D. Isaev, K. Solt, O. Gurtovaya, J. P. Reeves, and R. Shirokov
Modulation of the Voltage Sensor of L-type Ca2+ Channels by Intracellular Ca2+
J. Gen. Physiol., April 26, 2004; 123(5): 555 - 571.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. Kobrinsky, E. Schwartz, D. R. Abernethy, and N. M. Soldatov
Voltage-gated Mobility of the Ca2+ Channel Cytoplasmic Tails and Its Regulatory Role
J. Biol. Chem., February 7, 2003; 278(7): 5021 - 5028.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
M. Aoyama, M. Murakami, T. Iwashita, Y. Ito, K. Yamaki, and S. Nakayama
Slow Deactivation and U-Shaped Inactivation Properties in Cloned Cav1.2b Channels in Chinese Hamster Ovary Cells
Biophys. J., January 1, 2003; 84(1): 709 - 724.
[Abstract] [Full Text] [PDF]

Home page
 Biophys. JHome page
B. Calabrese, I. V. Tabarean, P. Juranka, and C. E. Morris
Mechanosensitivity of N-Type Calcium Channel Currents
Biophys. J., November 1, 2002; 83(5): 2560 - 2574.
[Abstract] [Full Text] [PDF]

Home page
 J. Pharmacol. Exp. Ther.Home page
D. R. Abernethy and N. M. Soldatov
Structure-Functional Diversity of Human L-Type Ca2+ Channel: Perspectives for New Pharmacological Targets
J. Pharmacol. Exp. Ther., March 1, 2002; 300(3): 724 - 728.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH TABLE OF CONTENTS
Copyright © 2000 The Physiological Society.