The role of tropomyosin in the regulation of myocardial contraction and relaxation

Studies over the last 30 years have demonstrated the essential nature of the evolutionarily highly conserved tropomyosin (TM) protein. TM-deficient cells neither function properly nor survive, and mutations within this protein impair severely its function within the sarcomere. The ability to manipul...

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Bibliographic Details
Published in:	Pflügers Archiv Vol. 446; no. 1; pp. 1 - 8
Main Authors:	Wolska, Beata M, Wieczorek, David M F
Format:	Journal Article
Language:	English
Published:	Germany Springer Nature B.V 01-04-2003
Subjects:	Animals Cardiomyopathy, Hypertrophic, Familial - genetics Cardiomyopathy, Hypertrophic, Familial - physiopathology Diastole - physiology Humans Mutation Myocardial Contraction - physiology Protein Conformation Protein Isoforms - chemistry Protein Isoforms - genetics Protein Isoforms - physiology Tropomyosin - chemistry Tropomyosin - genetics Tropomyosin - physiology
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Summary:	Studies over the last 30 years have demonstrated the essential nature of the evolutionarily highly conserved tropomyosin (TM) protein. TM-deficient cells neither function properly nor survive, and mutations within this protein impair severely its function within the sarcomere. The ability to manipulate TM isoform expression genetically within functioning cardiomyocytes and the whole heart has proven essential in deciphering the physiological significance of the different TM isoforms. It is now apparent that alpha-TM and actin serve as the requisite backbone of the thin filament, with varying levels of beta- and gamma-TM, together with the troponin complex serving to modulate sarcomere function. Defining the mechanisms whereby specific TM isoform amino acid differences alter thin filament dynamics will enhance greatly the understanding of muscle contraction during both normal and pathological states.
Bibliography:	ObjectType-Article-2 SourceType-Scholarly Journals-1 ObjectType-Feature-3 content type line 23 ObjectType-Review-1
ISSN:	0031-6768 1432-2013
DOI:	10.1007/s00424-002-0900-3