Tropomyosin structure and function new insights

M Muthuchamy; P Rethinasamy; D F Wieczorek

doi:10.1016/S1050-1738(97)00004-2

Tropomyosin structure and function new insights

Trends Cardiovasc Med. 1997 May;7(4):124-8. doi: 10.1016/S1050-1738(97)00004-2.

Authors

M Muthuchamy¹, P Rethinasamy, D F Wieczorek

Affiliation

¹ Department of Molecular Genetics, Biochemistry, and Microbiology, University of Cincinnati Medical Center, Cincinnati, OH 45267-0524, USA.

PMID: 21235875
DOI: 10.1016/S1050-1738(97)00004-2

Abstract

Cardiac muscle contraction is dependent upon a cooperative interaction between thick and thin filament sarcomeric proteins. Tropomyosin (TM), an essential thin filament protein, interacts with actin and the troponin complex to regulate contractile activity. During muscle contraction, an increase of calcium (Ca(2+)) in the myofilament space promotes binding of Ca(2+) to troponin C, which alters the conformational state of TM and facilitates acto-myosin interactions. By coupling classic genetic approaches with recent developments in transgenic animal model systems, new insights have been provided on the functional role of TM isoforms in both normal and disease states. The focus of this article is to review the current state of knowledge on TM structure and function, with a particular emphasis on myocardial expression in transgenic mouse model systems. (Trends Cardiovasc Med 1997;7:124-128). © 1997, Elsevier Science Inc.