Role of carbonyl modifications on aging-associated protein aggregation

Maya Tanase, Aleksandra M. Urbanska, Valerio Zolla, Cristina C. Clement, Liling Huang, Kateryna Morozova, Carlo Follo, Michael Goldberg, Barbara Roda, Pierluigi Reschiglian, Laura Santambrogio

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42 Scopus citations

Abstract

Protein aggregation is a common biological phenomenon, observed in different physiological and pathological conditions. Decreased protein solubility and a tendency to aggregate is also observed during physiological aging but the causes are currently unknown. Herein we performed a biophysical separation of aging-related high molecular weight aggregates, isolated from the bone marrow and splenic cells of aging mice and followed by biochemical and mass spectrometric analysis. The analysis indicated that compared to younger mice an increase in protein post-translational carbonylation was observed. The causative role of these modifications in inducing protein misfolding and aggregation was determined by inducing carbonyl stress in young mice, which recapitulated the increased protein aggregation observed in old mice. Altogether our analysis indicates that oxidative stress-related post-translational modifications accumulate in the aging proteome and are responsible for increased protein aggregation and altered cell proteostasis.

Original languageEnglish (US)
Article number19311
JournalScientific reports
Volume6
DOIs
StatePublished - Jan 18 2016

ASJC Scopus subject areas

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    Tanase, M., Urbanska, A. M., Zolla, V., Clement, C. C., Huang, L., Morozova, K., Follo, C., Goldberg, M., Roda, B., Reschiglian, P., & Santambrogio, L. (2016). Role of carbonyl modifications on aging-associated protein aggregation. Scientific reports, 6, [19311]. https://doi.org/10.1038/srep19311