Thyroid hormone regulation of myosin heavy chain isoform composition in young and old rats, with special reference to IIX myosin
- 1 February 1995
- journal article
- Published by Wiley in Acta Physiologica Scandinavica
- Vol. 153 (2), 109-116
- https://doi.org/10.1111/j.1748-1716.1995.tb09841.x
Abstract
The effects of 4 weeks of thyroid hormone (3,5,3′‐triiodothyronine, T3) treatment on the myosin heavy chain (MHC) composition were compared in the slow‐twitch soleus and the fast‐twitch extensor digitorum longus (EDL) muscles from young (3–6 months) and old (20–24 months) male albino rats. Four MHC isoforms were separated on silverstained 6% sodium dodecyl sulphate polyacrylamide gel electrophoresis. According to immunoblotting experiments with specific MHC monoclonal antibodies, the four MHCs corresponded to types I, IIB, IIX and IIA. In the soleus, the type I MHC content was higher in the old than in the young animals, and the type IIA content lower. Type IIX myosin was observed in some young control soleus, but not in old ones. After T3 treatment, the content of type I MHC decreased substantially in both young and old animals and that of type IIA increased. After T3 treatment, type IIX myosin was observed in both young and old animals, with a slighty higher IIX myosin content in old age, but the age‐related different in the contents of types I and IIA was diminished. In EDL, the type IIX MHC content was significantly higher in the old animals, at the significantly by T3 treatment in EDL, either in young or old animals. In conclusion, an age‐related motor unit transformation is observed in both the slow‐twich soleus and the fast‐twitch EDL and the capacity for MHC isoform switching in response to T3 treatment is not impaired in old age.Keywords
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