Myosin heavy chain isoforms and dynamic contractile properties: skeletal versus smooth muscle. Comp Biochem Physiol B Biochem Mol Biol 1998 Mar;119(3):425-34
Date
09/12/1998Pubmed ID
9734327DOI
10.1016/s0305-0491(98)00003-0Scopus ID
2-s2.0-0031903635 (requires institutional sign-in at Scopus site) 13 CitationsAbstract
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.
Author List
Eddinger TJAuthor
Thomas Eddinger PhD Bioological Sciences in the Biology department at Marquette UniversityMESH terms used to index this publication - Major topics in bold
AnimalsHumans
Models, Molecular
Muscle Contraction
Muscle, Skeletal
Muscle, Smooth
Muscle, Smooth, Vascular
Myosin Heavy Chains
