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.
journal_name
Sci Repjournal_title
Scientific reportsauthors
Tanase M,Urbanska AM,Zolla V,Clement CC,Huang L,Morozova K,Follo C,Goldberg M,Roda B,Reschiglian P,Santambrogio Ldoi
10.1038/srep19311subject
Has Abstractpub_date
2016-01-18 00:00:00pages
19311issn
2045-2322pii
srep19311journal_volume
6pub_type
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