Molecular and Functional Characterization of a Novel Cardiac-Specific Human Tropomyosin Isoform
Author(s) -
Sudarsan Rajan,
Ganapathy Jagatheesan,
Chehade N. Karam,
Marco Stephan LofranoAlves,
Ilona Bódi,
Arnold Schwartz,
Christian F. Bulcao,
Karen M. D’Souza,
Shahab A. Akhter,
Greg P. Boivin,
Dipak K. Dube,
Natalia Petrashevskaya,
Andrew B. Herr,
Roger Hullin,
Stephen B. Liggett,
Beata M. Wolska,
R. John Solaro,
David F. Wieczorek
Publication year - 2010
Publication title -
circulation
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 7.795
H-Index - 607
eISSN - 1524-4539
pISSN - 0009-7322
DOI - 10.1161/circulationaha.109.889725
Subject(s) - myofilament , gene isoform , tropomyosin , myofibril , dilated cardiomyopathy , heart failure , medicine , cardiomyopathy , cardiac muscle , actin , genetically modified mouse , endocrinology , microbiology and biotechnology , transgene , myocyte , biology , biochemistry , gene
Tropomyosin (TM), an essential actin-binding protein, is central to the control of calcium-regulated striated muscle contraction. Although TPM1alpha (also called alpha-TM) is the predominant TM isoform in human hearts, the precise TM isoform composition remains unclear.
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