Induction of a fast-oxidative phenotype by chronic muscle stimulation: mechanical and biochemical studies.
We studied changes in the mechanical properties and myosin isoform composition of rabbit tibialis anterior muscles that were subjected to continuous stimulation at 2.5 Hz for up to 12 wk. The effects of stimulation at 2.5 Hz were less profound than those observed for the same duration of stimulation at 10 Hz (12). Stimulation at 10 Hz for 12 wk induced complete transformation to a slow-contracting muscle homogeneous in slow myosin isoforms; stimulation for the same period at 2.5 Hz resulted in moderate changes in contractile speed and a very small increase in the synthesis of slow myosin isoforms. On the other hand, the fatigue resistance of muscles stimulated at 2.5 Hz was as great, in both isometric and dynamic fatigue tests, as that of the muscles stimulated at 10 Hz. Thus entire fast skeletal muscles can be transformed to a state in which fast myosin isoforms continue to be synthesized, but the oxidative capacity is sufficient to support sustained working at a higher power output than that associated with slow muscle.
Jarvis
J C
JC
Department of Human Anatomy and Cell Biology, University of Liverpool, United Kingdom.
Sutherland
H
H
Mayne
C N
CN
Gilroy
S J
SJ
Salmons
S
S
D000818:Animals; D001696:Biomechanical Phenomena; D004558:Electric Stimulation; D004591:Electrophoresis, Polyacrylamide Gel; D005260:Female; D008297:Male; D018763:Muscle Fatigue; D009132:Muscles / Q000502:physiology*; D018995:Myosin Heavy Chains / Q000378:metabolism; D018994:Myosin Light Chains / Q000378:metabolism; D009218:Myosins / Q000378:metabolism*; D010084:Oxidation-Reduction; D010641:Phenotype; D011817:Rabbits; D013997:Time Factors
D018994:Myosin Light Chains; D018995:Myosin Heavy Chains; D009218:Myosins