Calcium-sensitive cross-bridge transitions in mammalian fast and slow skeletal muscle fibers.
The fundamental mechanism underlying the differing rates of tension development in fast and slow mammalian skeletal muscle is still unknown. Now, in skinned (membrane-permeabilized) single fibers it has been shown that the rate of formation of the strongly bound, force-producing cross-bridge between actin and myosin is calcium-sensitive in both fast and slow fibers and that the rate is markedly greater in fast fibers. The transition rates obtained at high calcium concentrations correlated with myosin isoform content, whereas at low calcium concentrations the thin filament regulatory proteins appeared to modulate the rate of tension development, especially in fast fibers. Fiber type-dependent differences in rates of cross-bridge transitions may account for the characteristic rates of tension development in mammalian fast and slow skeletal muscles.
Metzger
J M
JM
Department of Physiology, School of Medicine, University of Wisconsin, Madison 53706.
Moss
R L
RL
D000199:Actins / Q000378:metabolism; D000818:Animals; D002118:Calcium / Q000494:pharmacology*; D009119:Muscle Contraction / Q000187:drug effects*; D009132:Muscles / Q000187:drug effects / Q000502:physiology*; D009218:Myosins / Q000378:metabolism; D051381:Rats; D014336:Troponin / Q000378:metabolism
D000199:Actins; D014336:Troponin; D009218:Myosins; D002118:Calcium