Myosin Heavy Chain Isoforms and Dynamic Contractile Properties: Skeletal Versus Smooth Muscle

Authors

Thomas J. Eddinger, Marquette UniversityFollow

Document Type

Article

Language

eng

Format of Original

10 p.

Publication Date

3-1998

Publisher

Elsevier

Source Publication

Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology

Source ISSN

1096-4959

Abstract

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.

Comments

Accepted version. Comparative Biochemistry and Physiology Part B: Biochemistry and Molecular Biology, Vol. 119, No. 3 (March 1998): 425-434. DOI. © 1998 Elsevier. Used with permission.

Recommended Citation

Eddinger, Thomas J., "Myosin Heavy Chain Isoforms and Dynamic Contractile Properties: Skeletal Versus Smooth Muscle" (1998). Biological Sciences Faculty Research and Publications. 192.
https://epublications.marquette.edu/bio_fac/192