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Decrease in human quadriceps muscle protein turnover consequent upon leg immobilization.

J N Gibson, D Halliday, W L Morrison

    Clinical Science (London, England : 1979)
    |April 1, 1987
    PubMed
    Summary
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    Leg immobilization after tibial fracture significantly reduces quadriceps muscle protein synthesis and causes muscle fiber atrophy. This highlights the detrimental effects of prolonged inactivity on muscle health and function.

    Area of Science:

    • Muscle physiology
    • Biochemistry
    • Orthopedics

    Background:

    • Unilateral leg immobilization following tibial fracture can lead to muscle atrophy.
    • Understanding the impact on muscle protein turnover is crucial for rehabilitation.

    Purpose of the Study:

    • To assess quadriceps muscle protein turnover after unilateral leg immobilization.
    • To quantify changes in muscle protein synthetic rate and fiber characteristics.

    Main Methods:

    • Primed-constant intravenous infusion of L-[1-13C]leucine over 7 hours.
    • Analysis of quadriceps muscle biopsies for 13C enrichment.
    • Measurement of muscle RNA activity and fiber diameters.

    Main Results:

    • Muscle protein synthetic rate was significantly lower in the immobilized leg (0.034%/h) compared to the uninjured leg (0.046%/h).

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  • Muscle RNA activity decreased significantly in the immobilized leg.
  • Type I muscle fibers showed significant atrophy in the immobilized leg.

    • Conclusions:

    • Leg immobilization significantly impairs quadriceps muscle protein synthesis.
    • Immobilization leads to atrophy, particularly in type I muscle fibers.
    • These findings underscore the importance of early rehabilitation to mitigate muscle loss.