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Triadins Modulate Intracellular Ca2+ Homeostasis but Are Not Essential for Excitation-Contraction Coupling in Skeletal Muscle.

Authors :
Xiaohua Shen
Franzini-Armstrong, Clara
Lopez, Jose R.
Jones, Larry R.
Kobayashi, Yvonne M.
Ying Wang
Kerrick, W. Glenn L.
Caswell, Anthony H.
Potter, James D.
Miller, Todd
Allen, Paul D.
Perez, Claudio F.
Source :
Journal of Biological Chemistry. 12/28/2007, Vol. 282 Issue 52, p37864-37874. 11p. 2 Charts, 8 Graphs.
Publication Year :
2007

Abstract

To unmask the role of triadin in skeletal muscle we engineered pan-triadin-null mice by removing the first exon of the triadin gene. This resulted in a total lack of triadin expression in both skeletal and cardiac muscle. Triadin knockout was not embryonic or birth-lethal, and null mice presented no obvious functional phenotype. Western blot analysis of sarcoplasmic reticulum (SR) proteins in skeletal muscle showed that the absence of triadin expression was associated with down-regulation of Junctophilin-1, junctin, and calsequestrin but resulted in no obvious contractile dysfunction. Ca2+ imaging studies in null lumbricalis muscles and myotubes showed that the lack of triadin did not prevent skeletal excitation-contraction coupling but reduced the amplitude of their Ca2+ transients. Additionally, null myotubes and adult fibers had significantly increased myoplasmic resting free Ca2+ [³H]Ryanodine binding studies of skeletal muscle SR vesicles detected no differences in Ca2+ activation or Ca2+ and Mg2+ inhibition between wild-type and triadin-null animals. Subtle ultrastructural changes, evidenced by the appearance of longitudinally oriented triads and the presence of calsequestrin in the sacs of the longitudinal SR, were present in fast but not slow twitch-null muscles. Overall, our data support an indirect role for triadin in regulating myoplasmic Ca2+ homeostasis and organizing the molecular complex of the triad but not in regulating skeletal-type excitation-contraction coupling. [ABSTRACT FROM AUTHOR]

Details

Language :
English
ISSN :
00219258
Volume :
282
Issue :
52
Database :
Academic Search Index
Journal :
Journal of Biological Chemistry
Publication Type :
Academic Journal
Accession number :
28337901
Full Text :
https://doi.org/10.1074/jbc.M705702200