Muscle plasticity related to changes in tubulin and αB-crystallin levels induced by eccentric contraction in rat skeletal muscles.
We used the model of eccentric contraction of the hindlimb muscle by Ochi et al. to examine the role of eccentric contraction in muscle plasticity. This model aims to focus on stimulated skeletal muscle responses by measuring tissue weights and tracing the quantities of αB-crystallin and tubulin. The medial gastrocnemius muscle (GCM) responded to electrically induced eccentric contraction (EIEC) with significant increases in tissue weight (p < 0.01) and the ratio of tissue weight to body weight (p < 0.05); however, there was a decrease in soleus muscle weight after EIEC. EIEC in the GCM caused contractile-induced sustenance of the traced proteins, but the soleus muscle exhibited a remarkable decrease in α-tubulin and a 19% decrease in αB-crystallin. EIEC caused fast-to-slow myosin heavy chain (MHC) isoform type-oriented shift within both the GCM and soleus muscle. These results have shown that different MHC isoform type-expressing slow and fast muscles commonly undergo fast-to-slow type MHC isoform transformation. This suggests that different levels of EIEC affected each of the slow and fast muscles to induce different quantitative changes in the expression of αB-crystallin and α-tubulin.
['Jee|H|H|', 'Ochi|E|E|', 'Sakurai|T|T|', 'Lim|J-Y|JY|', 'Nakazato|K|K|', 'Hatta|H|H|']
D000818:Animals D004558:Electric Stimulation D008297:Male D009119:Muscle Contraction D018482:Muscle, Skeletal D018995:Myosin Heavy Chains D020033:Protein Isoforms D016059:Range of Motion, Articular D051381:Rats D017208:Rats, Wistar D014404:Tubulin D038203:alpha-Crystallin B Chain
skeletal muscle electrically induced eccentric contraction myosin heavy chain cytoskeleton heat shock protein isoform type transition