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- W101024661 abstract "Tropomyosin (Tm) is an essential component in the regulation of striated muscle contraction. Questions about Tm functional role have been difficult to study because sarcomere Tm content is not as easily manipulated as Troponin (Tn). Here we describe the method we recently developed to replace Tm-Tn of skeletal and cardiac myofibrils from animals and humans to generate an experimental model of homogeneous Tm composition and giving the possibility to measure a wide range of mechanical parameters of contraction (e.g. maximal force and kinetics of force generation). The success of the exchange was determined by SDS–PAGE and by mechanical measurements of calcium dependent force activation on the reconstituted myofibrils. In skeletal and cardiac myofibrils, the percentage of Tm replacement was higher than 90%. Maximal isometric tension was 30–35% lower in the reconstituted myofibrils than in control myofibrils but the rate of force activation (kACT) and that of force redevelopment (kTR) were not significantly changed. Preliminary results show the effectiveness of Tm replacement in human cardiac myofibrils. This approach can be used to test the functional impact of Tm mutations responsible for human cardiomyopathies." @default.
- W101024661 created "2016-06-24" @default.
- W101024661 creator A5001937050 @default.
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- W101024661 date "2010-01-01" @default.
- W101024661 modified "2023-09-27" @default.
- W101024661 title "Extraction and Replacement of the Tropomyosin–Troponin Complex in Isolated Myofibrils" @default.
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- W101024661 doi "https://doi.org/10.1007/978-1-4419-6366-6_9" @default.
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