Advertisement
JBC

HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
QUICK SEARCH:   [advanced]


     

A more recent version of this article appeared on November 25, 2005
This Article
Right arrow Full Text (Accepted Manuscript)
Right arrow All Versions of this Article:
280/47/39302    most recent
M506566200v1
Right arrow Alert me when this article is cited
Right arrow Alert me if a correction is posted
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
Right arrowRequest Permissions
Citing Articles
Right arrow Citing Articles via HighWire
Right arrow Citing Articles via Google Scholar
Google Scholar
Right arrow Articles by Smida Rezgui, S.
Right arrow Articles by Marty, I.
Right arrow Search for Related Content
PubMed
Right arrow PubMed Citation
Right arrow Articles by Smida Rezgui, S.
Right arrow Articles by Marty, I.
Social Bookmarking
Add to CiteULike   Add to Complore   Add to Connotea   Add to Del.icio.us   Add to Digg   Add to Reddit   Add to Technorati  
What's this?

Papers In Press, published online ahead of print September 21, 2005
J. Biol. Chem, 10.1074/jbc.M506566200
Submitted on June 16, 2005
Revised on September 20, 2005
Accepted on September 21, 2005

Triadin (TRISK 95) over-expression blocks excitation-contraction coupling in rat skeletal myotubes

Sophia Smida Rezgui, Stéphane Vassilopoulos, Julie Brocard, Jean Claude Platel, Alexandre Bouron, Christophe Aarnoult, Sarah Oddoux, Luis Garcia, Michel De Waard, and Isabelle Marty

INSERM U607- CCFP, Grenoble 38054

Corresponding Author: imarty{at}cea.fr

In order to identify the function of triadin in skeletal muscle, adenovirus mediated over-expression of Trisk 95 or Trisk 51, the two major skeletal muscle isoforms, was induced in rat skeletal muscle primary cultures, and the physiological behaviour of the modified cells was analyzed. Over-expression did not modify the expression level of their protein partners: ryanodine receptor, dihydropyridine receptor, and the other triadin. Caffeine induced-calcium release was also unaffected by triadin overexpression. Nevertheless, in the absence of extracellular calcium, depolarization induced calcium release was almost abolished in Trisk 95 over-expressing myotubes (T95 myotubes), and not modified in Trisk 51 over-expressing myotubes (T51 myotubes). This was not due to a modification of dihydropyridine receptors as depolarization in presence of external calcium still induced a calcium release, and the activation curve of dihydropyridine receptor was unchanged, in both T95 and T51 myotubes. The calcium release complex was also maintained in T95 myotubes as Trisk 95, ryanodine receptor, dihydropyridine receptor and Trisk 51 were still co-localized. The effect of Trisk 95 over-expression on depolarization-induced calcium release was reversed by a simultaneous infection with an antisense Trisk 95 adenovirus, indicating the specificity of this effect. Thus, the level of Trisk 95 and not Trisk 51 is important on regulating the calcium release complex, and an excess of this protein can lead to an inhibition of the physiological function of the complex.


Add to CiteULike CiteULike   Add to Complore Complore   Add to Connotea Connotea   Add to Del.icio.us Del.icio.us   Add to Digg Digg   Add to Reddit Reddit   Add to Technorati Technorati    What's this?


This article has been cited by other articles:


Home page
 J. Physiol.Home page
J. Fodor, M. Gonczi, M. Sztretye, B. Dienes, T. Olah, L. Szabo, E. Csoma, P. Szentesi, G. P. Szigeti, I. Marty, et al.
Altered expression of triadin 95 causes parallel changes in localized Ca2+ release events and global Ca2+ signals in skeletal muscle cells in culture
J. Physiol., December 1, 2008; 586(23): 5803 - 5818.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
X. Shen, C. Franzini-Armstrong, J. R. Lopez, L. R. Jones, Y. M. Kobayashi, Y. Wang, W. G. L. Kerrick, A. H. Caswell, J. D. Potter, T. Miller, et al.
Triadins Modulate Intracellular Ca2+ Homeostasis but Are Not Essential for Excitation-Contraction Coupling in Skeletal Muscle
J. Biol. Chem., December 28, 2007; 282(52): 37864 - 37874.
[Abstract] [Full Text] [PDF]

Home page
 JGPHome page
S. A. Goonasekera, N. A. Beard, L. Groom, T. Kimura, A. D. Lyfenko, A. Rosenfeld, I. Marty, A. F. Dulhunty, and R. T. Dirksen
Triadin Binding to the C-Terminal Luminal Loop of the Ryanodine Receptor is Important for Skeletal Muscle Excitation Contraction Coupling
J. Gen. Physiol., September 24, 2007; 130(4): 365 - 378.
[Abstract] [Full Text] [PDF]

Home page
 J. Physiol.Home page
A. J. Rose, T. J. Alsted, J. B. Kobbero, and E. A. Richter
Regulation and function of Ca2+-calmodulin-dependent protein kinase II of fast-twitch rat skeletal muscle
J. Physiol., May 1, 2007; 580(3): 993 - 1005.
[Abstract] [Full Text] [PDF]

Home page
 Mol. Cell. Biol.Home page
E. J. Jaehnig, A. B. Heidt, S. B. Greene, I. Cornelissen, and B. L. Black
Increased Susceptibility to Isoproterenol-Induced Cardiac Hypertrophy and Impaired Weight Gain in Mice Lacking the Histidine-Rich Calcium-Binding Protein
Mol. Cell. Biol., December 15, 2006; 26(24): 9315 - 9326.
[Abstract] [Full Text] [PDF]

Home page
 J. Biol. Chem.Home page
E. H. Lee, G. Cherednichenko, I. N. Pessah, and P. D. Allen
Functional Coupling between TRPC3 and RyR1 Regulates the Expressions of Key Triadic Proteins
J. Biol. Chem., April 14, 2006; 281(15): 10042 - 10048.
[Abstract] [Full Text] [PDF]


HOME HELP FEEDBACK SUBSCRIPTIONS ARCHIVE SEARCH
 All ASBMB Journals   Molecular and Cellular Proteomics 
 Journal of Lipid Research   ASBMB Today 
Copyright © 2005 by the American Society for Biochemistry and Molecular Biology.
Advertisement
spacer
Advertisement
Advertisement