Myosin heavy chain isoforms and dynamic contractile properties: skeletal versus smooth muscle.
Myosin, one of the primary contractile muscle proteins, displays molecular, enzymatic, structural, functional and regulatory variability. This variability has been shown to account for a significant amount of the functional uniqueness of skeletal and smooth muscle. However, the universal generation of force and/or shortening by these two muscle types belies the ever-increasing number of known distinct differences that bring this about. Thus, the notion that the functional roles of skeletal and smooth muscle, their development and regulation, all appear to be uniquely applicable for their physiological purpose no longer appears heretical. This manuscript presents a cursory overview of the numerous ways in which these two types of muscle use a host of myosin molecules to bring about a common result, force generation and/or shortening.
Eddinger
T J
TJ
Department of Biology, Marquette University, Milwaukee, WI 53201-1881, USA. eddingert@vms.csd.mu.edu
D000818:Animals; D006801:Humans; D008958:Models, Molecular; D009119:Muscle Contraction / Q000502:physiology*; D018482:Muscle, Skeletal / Q000502:physiology*; D009130:Muscle, Smooth / Q000502:physiology*; D009131:Muscle, Smooth, Vascular / Q000502:physiology; D018995:Myosin Heavy Chains / Q000737:chemistry / Q000235:genetics / Q000502:physiology*
D018995:Myosin Heavy Chains