Key result
The relative turnover rate of thin filament proteins in rabbit skeletal muscle is asynchronous, with the order of turnover rate being troponin > tropomyosin > actin.
This preclinical study demonstrates asynchronous turnover of thin filament proteins in rabbit skeletal muscle, with troponin turning over fastest, followed by tropomyosin and actin.
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Preclinical rabbit skeletal muscle data warrant caution before clinical extrapolation; leaves open sarcomere protein dynamics in human cardiac disease models.
The relative turnover rate of protein components of the thin filament was measured by a continuous double isotope method. Both 3H-lysine and 14C-lysine were administered continuously in the diet to male adult rabbits for 7 days. On the 7th day, the 14C-lysine was discontinued while the 3H-lysine was continued for 14 additional days. The relative turnover rate of the protein components was estimated from the 3H/14C ratios of the isolated protein of the same animal. From the different ratios of 3H/14C of each protein fraction, asynchronous turnover of the thin fila-ment proteins (actin, tropomyosin and troponin) was concluded. The order of degree in relative turnover rate is as follows: troponin>tropomyosin>actin.
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Funabiki et al. (1973) studied Healthy (animal model) (n=4). Continuous double isotope administration (3H-lysine and 14C-lysine) was evaluated on Relative turnover rate of thin filament proteins (actin, tropomyosin, troponin). The relative turnover rate of thin filament proteins in rabbit skeletal muscle is asynchronous, with the order of turnover rate being troponin > tropomyosin > actin.
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