Quantitative proteomics of rat livers shows that unrestricted feeding is stressful for proteostasis with implications on life span

Galia Gat-Yablonski, Andrija Finka, Galit Pinto, Manfredo Quadroni, Biana Shtaif, Pierre Goloubinoff*

*Corresponding author for this work

Research output: Contribution to journalArticlepeer-review

Abstract

Studies in young mammals on the molecular effects of food restriction leading to prolong adult life are scares. Here, we used high-throughput quantitative proteomic analysis of whole rat livers to address the molecular basis for growth arrest and the apparent life-prolonging phenotype of the food restriction regimen. Over 1800 common proteins were significantly quantified in livers of ad libitum, restriction- and re-fed rats, which summed up into 92% of the total protein mass of the cells. Compared to restriction, ad libitum cells contained significantly less mitochondrial catabolic enzymes and more cytosolic and ER HSP90 and HSP70 chaperones, which are hallmarks of heat- and chemically-stressed tissues. Following re-feeding, levels of HSPs nearly reached ad libitum levels. The quantitative and qualitative protein values indicated that the restriction regimen was a least stressful condition that used minimal amounts of HSP-chaperones to maintain optimal protein homeostasis and sustain optimal life span. In contrast, the elevated levels of HSP-chaperones in ad libitum tissues were characteristic of a chronic stress, which in the long term could lead to early aging and shorter life span.

Original languageEnglish
Pages (from-to)1735-1758
Number of pages24
JournalAging
Volume8
Issue number8
DOIs
StatePublished - 2016

Funding

FundersFunder number
Schweizerischer Nationalfonds zur Förderung der Wissenschaftlichen Forschung140512/1

    Keywords

    • Aging
    • Catch up growth
    • Food restriction
    • Heat shock proteins
    • Mitochondria

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