RELATIONSHIP BETWEEN OXIDATION OF MYOFIBRILLAR PROTEINS AND CONTRACTILE PROPERTIES IN SOLEUS MUSCLES FROM HYPERTHYROID RAT
- VernacularTitle:甲状腺機能亢進症モデルラットにおけるヒラメ筋の収縮機能と筋原線維の酸化的修飾との関係
- Author:
TAKASHI YAMADA
;
TAKAAKI MISHIMA
;
MAKOTO SAKAMOTO
;
MINAKO SUGIYAMA
;
SATOSHI MATSUNAGA
;
MASANOBU WADA
- Publication Type:Journal Article
- Keywords:
reactive oxygen species;
hyperthyroidism;
specific force reduction;
redox status
- From:Japanese Journal of Physical Fitness and Sports Medicine
2007;56(5):473-480
- CountryJapan
- Language:Japanese
-
Abstract:
We tested the hypothesis that a force reduction in soleus muscles from hyperthyroid rats would be associated with oxidative modification of myofibrillar proteins. Daily injection of thyroid hormone [3, 5, 3’-triiodo-L-thyronine (T3)] for 21 days depressed isometric forces in whole soleus muscle across a range of stimulus frequencies (1, 10, 20, 40, 75 and 100 Hz) (P<0.05). In fiber bundles, hyperthyroidism also led to pronounced reductions (P<0.05) in both K+- and 4-chloro-m-cresol-induced contracture forces. The degrees of the reductions were similar between these two contractures. These reductions in force production were accompanied by a remarkable increment (103% ; P<0.05) in carbonyl groups comprised in myofibrillar proteins. In additional experiments, we have also tested the efficacy of carvedilol, a non-selective β1-β2-blocker that possesses anti-oxidative properties. Treatment with carvedilol prevented T3-induced oxidation of myofibrillar proteins. However, carvedilol did not improve the hyperthyroid-induced reductions in force production. These data suggest that oxidative modification of myofibrillar proteins may not account for the reductions in force production of hyperthyroid rat soleus muscle.
