Age-related changes in the 20S and 26S proteasome activities in the liver of male F344 rats

Toshiaki Hayashi, S. Goto

Research output: Contribution to journalArticle

105 Citations (Scopus)

Abstract

Accumulation of altered proteins in old animals has been ascribed to slower turnover of proteins. Since proteasomes can be regarded as the major proteolytic enzymes responsible for the degradation of the majority of cellular proteins, we examined age-related changes of 20S and 26S proteasomes in the liver of young (8-10-month-old), middle-aged (15-18-month-old) and old (25-28-month-old) Fischer 344 male rats. The two forms of proteasomes were separated by glycerol gradient centrifugation. Fluorogenic peptides were used as substrates to evaluate three types of peptidase activities. The ratio of peptidase activities in the 20S proteasome vs. those in the 26S form did not appear to change with age. Unstimulated chymotrypsin-like activity found only in the 26S form decreased by 30% in the old rats as compared with that in the young ones, while no change in the activity was observed during aging when stimulated by sodium dodecyl sulfate. The trypsin-like activity declined significantly by 17% to an apparently similar extent in both 20S and 26S forms. The peptidylglutamyl peptide hydrolyzing activity exhibited gradual decrease with age, resulting in 60% lower value in the old rats as compared with the young animals. These changes are considered to account for the age-related extension of half-life of proteins. Since the amount of total proteasomes measured by immunoblot did not appear to change with age, posttranslational modifications or subunit replacement is possibly responsible for the decrease in the activities.

Original languageEnglish
Pages (from-to)55-66
Number of pages12
JournalMechanisms of Ageing and Development
Volume102
Issue number1
DOIs
Publication statusPublished - May 1 1998

Fingerprint

Inbred F344 Rats
Proteasome Endopeptidase Complex
Liver
Rats
Peptide Hydrolases
Animals
Proteins
Peptides
Centrifugation
Chymotrypsin
Post Translational Protein Processing
Sodium Dodecyl Sulfate
Glycerol
Trypsin
Half-Life
Aging of materials
ATP dependent 26S protease
Degradation
Substrates

Keywords

  • Aging
  • Liver
  • Peptidase
  • Protease
  • Proteasome
  • Rat

ASJC Scopus subject areas

  • Ageing
  • Biochemistry
  • Developmental Biology
  • Developmental Neuroscience

Cite this

Age-related changes in the 20S and 26S proteasome activities in the liver of male F344 rats. / Hayashi, Toshiaki; Goto, S.

In: Mechanisms of Ageing and Development, Vol. 102, No. 1, 01.05.1998, p. 55-66.

Research output: Contribution to journalArticle

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