Proteome oxidative carbonylation during oxidative stress-induced premature senescence of WI-38 human fibroblasts

Le Boulch, M., Ahmed, Emad, Rogowska-Wrzesinska, A., Baraibar, M.A., Friguet, B.,

Abstract


© 2017 Elsevier B.V. Accumulation of oxidatively damaged proteins is a hallmark of cellular and organismal ageing, and is also a phenotypic feature shared by both replicative senescence and stress-induced premature senescence of human fibroblasts. Moreover, proteins that are building up as oxidized (i.e. the “Oxi-proteome”) during ageing and age-related diseases represent a restricted set of cellular proteins, indicating that certain proteins are more prone to oxidative carbonylation and subsequent intracellular accumulation. The occurrence of specific carbonylated proteins upon oxidative stress induced premature senescence of WI-38 human fibroblasts and their follow-up identification have been addressed in this study. Indeed, it was expected that the identification of these proteins would give insights into the mechanisms by which oxidatively damaged proteins could affect cellular function. Among these proteins, some are belonging to the cytoskeleton while others are mainly involved in protein quality control and/or biosynthesis as well as in redox and energy metabolism, the impairment of which has been previously associated with cellular ageing. Interestingly, the majority of these carbonylated proteins were found to belong to functional interaction networks pointing to signalling pathways that have been implicated in the oxidative stress response and subsequent premature senescence.


Other data

Title Proteome oxidative carbonylation during oxidative stress-induced premature senescence of WI-38 human fibroblasts
Authors Le Boulch, M. ; Ahmed, Emad ; Rogowska-Wrzesinska, A. ; Baraibar, M.A. ; Friguet, B. 
Issue Date 2017
Journal Mechanisms of Ageing and Development 
DOI 59
http://www.scopus.com/inward/record.url?eid=2-s2.0-85026661930&partnerID=MN8TOARS
170
1872-6216
10.1016/j.mad.2017.07.005
PubMed ID 28757326
Scopus ID 2-s2.0-85026661930

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