Relationship of the reduction-oxidation state to protein degradation in skeletal and atrial muscle

Marc E Tischler, Julie M. Fagan

Research output: Contribution to journalArticle

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Abstract

Changes in proteolysis were correlated with the cell reduction-oxidation state in rat diaphragm and atrium. Protein degradation was measured in the presence of cycloheximide as the linear release of tyrosine into the medium. Intracellular ratios of lactate/pyruvate, total NADH NAD, and malate/pyruvate were used as indicators of the muscle reduction-oxidation state. Incubation of diaphragms with leucine (0.5-2.0 mm) or its transamination product, sodium α-ketoisocaproate (0.5 mm), resulted in a lower rate of proteolysis and a higher ratio of lactate/pyruvate and NADH NAD. These effects of leucine could be abolished by inhibiting its transamination with l-cycloserine. Unlike leucine, neither isoleucine nor valine alone produced any change in these parameters. Incubation of diaphragms with glucose (20 mm) or atria with sodium lactate (2 mm) produced a diminution of tyrosine release from the muscles and a rise in the ratio of total NADH NAD. Similarly, in incubated diaphragms of fasted rats, the anabolic effects of insulin, epinephrine and isoproterenol on protein degradation were associated with a higher malate/pyruvate ratio. In catabolic states, such as fasting, cortisol treatment of fasted, adrenalectomized rats or traumatization, enhanced muscle proteolysis was observed. Fresh-frozen diaphragms from these rats had both lower lactate/pyruvate and malate/pyruvate ratios than did muscles from control animals. These data show that diminution of proteolysis in diaphragm is accompanied by an increase of the NAD(P)H NAD(P) ratios. In contrast to these findings, chymostatin and leupeptin, which inhibit directly muscle proteinases, caused a decrease of the lactate/pyruvate and malate/pyruvate ratios. These results suggest that protein degradation in diaphragm and atrium is linked to the cellular redox state.

Original languageEnglish (US)
Pages (from-to)191-201
Number of pages11
JournalArchives of Biochemistry and Biophysics
Volume217
Issue number1
DOIs
StatePublished - 1982

Fingerprint

Pyruvic Acid
NAD
Proteolysis
Diaphragms
Diaphragm
Muscle
Skeletal Muscle
Degradation
Oxidation
Rats
Lactic Acid
Proteins
Muscles
Leucine
Tyrosine
Sodium Lactate
Cycloserine
Anabolic Agents
Isoleucine
Valine

ASJC Scopus subject areas

  • Biochemistry
  • Biophysics
  • Molecular Biology

Cite this

Relationship of the reduction-oxidation state to protein degradation in skeletal and atrial muscle. / Tischler, Marc E; Fagan, Julie M.

In: Archives of Biochemistry and Biophysics, Vol. 217, No. 1, 1982, p. 191-201.

Research output: Contribution to journalArticle

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