Novel transitions in MHC isoforms: separate and combined effects of thyroid hormone and mechanical unloading
- 1 December 1998
- journal article
- research article
- Published by American Physiological Society in Journal of Applied Physiology
- Vol. 85 (6) , 2237-2248
- https://doi.org/10.1152/jappl.1998.85.6.2237
Abstract
Single-fiber (n = 3,818 fibers) electrophoretic analyses were used to delineate the separate and combined effects of hyperthyroidism (T3) and hindlimb suspension (HS) on the myosin heavy chain (MHC) isoform composition (1-, 2-, and 4-wk time points) of the rat soleus muscle. The key findings of this study are as follows. First, T3 and HS both altered the distribution of MHC isoforms at the single-fiber level; however, the populations of fibers produced by these two interventions were clearly different from one another. Second, T3 + HS rapidly converted the soleus into a fast muscle, producing large increases in the relative contents of the fast type IIx and IIb MHC isoforms which were primarily expressed in several populations of hybrid fibers (e.g., types I/IIa/IIx, I/IIx/IIb, I/IIa/IIx/IIb). Finally, T3 + HS produced unique populations of hybrid fibers that did not adhere to the I↔IIa↔IIx↔IIb sequential scheme of MHC plasticity. Collectively, the findings of this study demonstrate that the intervention of T3 + HS is a powerful model for manipulating and studying MHC isoform plasticity in slow skeletal muscle.Keywords
This publication has 29 references indexed in Scilit:
- Interaction of hyperthyroidism and hindlimb suspension on skeletal myosin heavy chain expressionJournal of Applied Physiology, 1998
- Single-fiber and whole muscle analyses of MHC isoform plasticity: interaction between T3 and unloadingAmerican Journal of Physiology-Cell Physiology, 1997
- Quantitative Analyses of Myosin Heavy‐Chain mRNA and Protein Isoforms in Single Fibers Reveal a Pronounced Fiber Heterogeneity in Normal Rabbit MusclesEuropean Journal of Biochemistry, 1997
- Thyroid hormone effects on contractility and myosin composition of soleus muscle and single fibres from young and old rats.The Journal of Physiology, 1996
- Thyroid HormoneExercise and Sport Sciences Reviews, 1996
- Thyroid hormone regulation of myosin heavy chain isoform composition in young and old rats, with special reference to IIX myosinActa Physiologica Scandinavica, 1995
- The continuum of pure and hybrid myosin heavy chain-based fibre types in rat skeletal muscleHistochemistry and Cell Biology, 1993
- 8 The Plasticity of Skeletal MuscleExercise and Sport Sciences Reviews, 1991
- Three myosin heavy chain isoforms in type 2 skeletal muscle fibresJournal of Muscle Research and Cell Motility, 1989
- All Members of the MHC Multigene Family Respond to Thyroid Hormone in a Highly Tissue-Specific MannerScience, 1986