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Susceptibilities of various myofibrillar proteins to muscle serine protease

N Yasogawa, Y Sanada, N Katunuma

    Journal of Biochemistry
    |May 1, 1978
    PubMed

    Insights

    Skeletal muscle serine protease degrades myofibrillar proteins like myosin and actin. Myosin heavy chains were fragmented, while alpha-actinin and M-protein remained intact.

    Area of Science:

    • Muscle physiology
    • Protein biochemistry

    Background:

    • Skeletal muscle serine proteases play a role in protein turnover.
    • Understanding myofibrillar protein degradation is crucial for muscle health.

    Purpose of the Study:

    • To investigate the degradation activity of skeletal muscle serine protease on native myofibrillar proteins.
    • To determine the susceptibility order of various myofibrillar proteins to this protease.

    Main Methods:

    • Fluorometric determination of liberated amino acids/peptides using o-phthalaldehyde.
    • Sodium dodecyl sulfate-polyacrylamide gel electrophoresis (SDS-PAGE) to analyze protein fragments.

    Main Results:

    • Myosin was degraded, with heavy chains fragmenting into 100,000 and 88,000 molecular weight components.
    • Troponin-T and tropomyosin were rapidly degraded, troponin-I slowly, and troponin-C not at all.
    • Actin showed slow degradation, while alpha-actinin and M-protein were resistant.

    Conclusions:

    • Skeletal muscle serine protease exhibits differential degradation of myofibrillar proteins.
    • Myosin, troponin, tropomyosin, and actin are susceptible to varying degrees, unlike alpha-actinin and M-protein.

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