Acid phosphatase and protease activities in immobilized rat skeletal muscles

Frank Witzmann, J. P. Troup, R. H. Fitts

Research output: Contribution to journalArticle

11 Citations (Scopus)

Abstract

The effect of hind-limb immobilization on selected lysosomal enzyme activities was studied in rat hind-limb muscles composed primarily of type I, IIA, or IIB fibers. Following immobilization, acid protease and acid phosphatase both exhibited significant (P <0.05) increases in their activity per unit weight in all three fiber types. Acid phosphatase activity increased at day 14 of immobilization in the three muscles and returned to control levels by day 21. Acid protease activity also changed biphasically, displaying a higher and earlier rise than acid phosphatase. The pattern of change in acid protease, but not acid phosphatase, closely parallels observed muscle wasting. The present data therefore demonstrate enhanced proteolytic capacity of all three fiber types early during muscular atrophy. In addition, the data suggest a dependence of basal hydrolytic and proteolytic activities and their adaptive response to immobilization on muscle fiber composition.

Original languageEnglish (US)
Pages (from-to)1732-1736
Number of pages5
JournalCanadian Journal of Physiology and Pharmacology
Volume60
Issue number12
StatePublished - 1982
Externally publishedYes

Fingerprint

Acid Phosphatase
Immobilization
Skeletal Muscle
Peptide Hydrolases
Muscles
Acids
Extremities
Muscular Atrophy
Weights and Measures
Enzymes

ASJC Scopus subject areas

  • Physiology
  • Pharmacology

Cite this

Acid phosphatase and protease activities in immobilized rat skeletal muscles. / Witzmann, Frank; Troup, J. P.; Fitts, R. H.

In: Canadian Journal of Physiology and Pharmacology, Vol. 60, No. 12, 1982, p. 1732-1736.

Research output: Contribution to journalArticle

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