Invited Review: plasticity and energetic demands of contraction in skeletal and cardiac muscle.
Numerous studies have explored the energetic properties of skeletal and cardiac muscle fibers. In this mini-review, we specifically explore the interactions between actin and myosin during cross-bridge cycling and provide a conceptual framework for the chemomechanical transduction that drives muscle fiber energetic demands. Because the myosin heavy chain (MHC) is the site of ATP hydrolysis and actin binding, we focus on the mechanical and energetic properties of different MHC isoforms. Based on the conceptual framework that is provided, we discuss possible sites where muscle remodeling may impact the energetic demands of contraction in skeletal and cardiac muscle.
Sieck
G C
GC
Department of Anesthesiology, Mayo Medical School and Foundation, Rochester, Minnesota 55905, USA. sieck.gary@mayo.edu
Regnier
M
M
D000199:Actins / Q000378:metabolism; D000205:Actomyosin / Q000378:metabolism; D000255:Adenosine Triphosphate / Q000378:metabolism; D000818:Animals; D006321:Heart / Q000502:physiology*; D006801:Humans; D009119:Muscle Contraction / Q000502:physiology*; D018485:Muscle Fibers, Skeletal / Q000502:physiology; D018482:Muscle, Skeletal / Q000502:physiology*; D009200:Myocardial Contraction / Q000502:physiology*; D018995:Myosin Heavy Chains / Q000378:metabolism
D000199:Actins; D000255:Adenosine Triphosphate; D000205:Actomyosin; D018995:Myosin Heavy Chains