Key result
The relative content of MyHC I isoform in human skeletal muscle was 2.6 times higher than in horse muscle and 6.3 times higher than in rat muscle.
Cross-Sectional (n=32)
Answers are grounded in this paper and cite their sources.
Species differences in MyHC I content warrant caution extrapolating animal data to humans; leaves open optimal models for human muscle research.
The distribution of myosin heavy (MyHC) and myosin light chain (MyLC) isoform pattern in horse, rat and human skeletal muscle was investigated to establish relations between them and the role of myosin isoform patterns in mammalian muscle with different twitch characteristics was studied. These two isoforms were separated in a SDS-PAGE gel system, stained using the coomassie and silver staining procedures, and the results were analyzed using a G:BOX system. The relative content of MyHC I isoform in muscle was 2.6 times higher than in human compared to horse muscle (p < 0.001), and 6.3 times higher than in rat muscle (p < 0.001). The relative content of MyHC IIx/d isoform in horse muscle is 2.7 times, and in rat muscle 2.2 times higher in comparison with human muscle (p < 0.001). The role of the MyLC isoform distribution in mammalian skeletal muscle seems to depend on the oxidative capacity of muscles.
No takes yet. Share an insight, caveat, or question.
Kaasik et al. (2012) conducted a cross-sectional in Healthy (n=32). Human species vs. Horse and rat species was evaluated on Relative content of MyHC I isoform in skeletal muscle (2.6 times higher than horse, 6.3 times higher than rat, p=<0.001). The relative content of MyHC I isoform in human skeletal muscle was 2.6 times higher than in horse muscle and 6.3 times higher than in rat muscle.
Synapse has enriched 10 related papers. Consider them for comparative context: