Relationship of the redox state to muscle protein degradation.

Marc E Tischler, J. M. Fagan, D. Allen

Research output: Contribution to journalArticle

7 Citations (Scopus)

Abstract

With increasing muscle size, incubated or fresh-frozen leg muscles showed a more reduced redox state and slower proteolysis. The ln of these data gave a linear correlation showing faster proteolysis under more oxidized conditions. In incubated diaphragms, the inhibitory effects of insulin and catecholamines on proteolysis were associated with a more reduced state. Fasting, trauma or cortisol treatment led to accelerated proteolysis and a more oxidized state. Long term fasting and refeeding supported this relationship, as did streptozotocin diabetes. Like the NAD+ and NADP+ redox couples, the glutathione couple seemed to fit this relationship. Use of proteinase inhibitors showed that the redox state probably mediated the effects of the various factors on proteolysis rather than vice versa. Muscle contains thioltransferase which catalyzes the formation of glutathione-protein mixed disulfides. We propose that increased formation of oxidized glutathione and its interaction with muscle proteins may act as a signal for the initiation of proteolysis.

Original languageEnglish (US)
Pages (from-to)363-372
Number of pages10
JournalProgress in Clinical and Biological Research
Volume180
StatePublished - 1985
Externally publishedYes

Fingerprint

Muscle Proteins
Proteolysis
Oxidation-Reduction
Muscles
Glutathione
Fasting
Glutaredoxins
Experimental Diabetes Mellitus
Glutathione Disulfide
Diaphragm
NADP
Disulfides
NAD
Catecholamines
Hydrocortisone
Leg
Peptide Hydrolases
Insulin
Wounds and Injuries
Proteins

ASJC Scopus subject areas

  • Medicine(all)

Cite this

Relationship of the redox state to muscle protein degradation. / Tischler, Marc E; Fagan, J. M.; Allen, D.

In: Progress in Clinical and Biological Research, Vol. 180, 1985, p. 363-372.

Research output: Contribution to journalArticle

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