Endogenous cathepsin B inhibitor activity in normal and myopathic red and white skeletal muscle

Muscle & Nerve
|April 1, 1982
PubMed

Insights

Vitamin E deficiency in guinea pigs increases cathepsin B activity in white muscles. However, this increase is offset by higher levels of cathepsin B inhibitors, suggesting no primary enzyme defect in muscular myopathy.

Area of Science:

  • Biochemistry
  • Muscle Physiology
  • Nutritional Science

Background:

  • Degenerative muscle diseases have obscure primary chemical lesions.
  • Vitamin E deficiency causes nutritional muscular myopathy in animals.
  • Lysosomal endoproteinases like cathepsin B play roles in muscle tissue.

Purpose of the Study:

  • To investigate cathepsin B activity and its endogenous inhibitor levels in vitamin E-deficient muscular myopathy.
  • To determine if altered cathepsin B activity is a primary defect in this condition.

Main Methods:

  • Assessed cathepsin B activity in red and white skeletal muscles of guinea pigs.
  • Measured endogenous cathepsin B inhibitor activity in the same muscle tissues.
  • Corrected cathepsin B activity for inhibitor levels.

Main Results:

  • A twofold increase in cathepsin B activity was observed in white muscles of vitamin E-deficient animals.
  • Normal and control groups showed significantly higher cathepsin B inhibitor activity compared to deficient animals.
  • Corrected cathepsin B specific activity in deficient muscle was not significantly different from normal or control tissues.

Conclusions:

  • The increased cathepsin B activity in vitamin E-deficient muscle is likely due to reduced inhibitor levels, not a primary enzyme abnormality.
  • This suggests that altered regulation of cathepsin B, rather than its intrinsic activity, is involved in nutritional muscular myopathy.

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