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Oxidation of myosin heavy chain and reduction in force production in hyperthyroid rat soleus

¹Graduate School of Biosphere Science, Hiroshima University, Hiroshima; ²Institute of Health Sciences and Physical Education, Osaka City University, Osaka; and ³Faculty of Integrated Arts and Sciences, Hiroshima University, Hiroshima, Japan

Submitted 17 November 2005 ; accepted in final form 27 December 2005

We tested the hypothesis that a force reduction in hyperthyroid rat soleus muscle would be associated with oxidative modification in myosin heavy chain (MHC). Daily injection of thyroid hormone [3,5,3'-triiodo-L-thyronine (T₃)] for 21 days depressed isometric forces of whole soleus muscle across a range of stimulus frequencies (P < 0.01). In fiber bundles, hyperthyroidism also led to pronounced reductions (P < 0.01) in both K⁺- and 4-chloro-m-cresol-induced contracture forces. The degrees of the reductions were similar between these two contractures that were induced by distinct reagents. Treatment with T₃ elicited a significant decrease (14%; P < 0.05) in the relative content of MHC contained in myofibrillar proteins. The content of carbonyl groups in myofibrillar protein extracts was elevated (P < 0.05) by 50% in T₃-treated muscles. Immunoblot analyses on T₃-treated muscles showed a greater increase (106%; P < 0.05) of the carbonyl content in MHC than in myofibrillar protein extracts. These data suggest that in hyperthyroidism the decrease in force production of skeletal muscles may stem primarily from failure in myofibrillar protein function resulting from oxidative modification of MHC.

reactive oxygen species; hyperthyroidism; force reduction; excitation-contraction coupling; fatigue

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