Proteome oxidative carbonylation during oxidative stress-induced premature senescence of WI-38 human fibroblasts. (March 2018)

• Record Type: Journal Article
• Authors: Le Boulch, Marine; Ahmed, Emad K.; Rogowska-Wrzesinska, Adelina; Baraibar, Martín A.; Friguet, Bertrand
• Is Part Of: Mechanisms of ageing and development. Volume 170(2018)
• Page Start: 59
• Page End: 71
• Publication Date: 2018-03
• Subjects: SIPS stress-induced premature senescence -- HDFs human diploid fibroblasts -- SIPS fibroblasts stress-induced premature senescent fibroblasts -- t-BHP tert-butyl hydroperoxide -- ROS reactive oxygen species -- IEF isoelectrofocusing -- DTT dithiothreitol -- RMI relative modification index -- MS mass spectrometry -- PBS phosphate buffered saline -- DNPH dinitrophenylhydrazine -- BSA bovine serum albumin; Protein oxidation -- Stress-induced premature senescence (SIPS) -- Fibroblasts -- Oxidative stress -- Proteomics -- Ageing; Aging -- Periodicals; Developmental biology -- Periodicals; Aging -- Periodicals; Developmental Biology -- Periodicals; Vieillissement -- Périodiques; Biologie du développement -- Périodiques; Aging; Developmental biology; Periodicals; 612.67
• DOI: 10.1016/j.mad.2017.07.005
• Languages: English
• ISSNs: 0047-6374

Abstract

Highlights: Oxidative carbonylation proteomics have been performed in fibroblasts after SIPS. A restricted set of increasingly carbonylated proteins have been identified. Several proteins belonging to the cytoskeleton have been found. Other proteins are involved in protein maintenance and intermediate metabolism. Data mining reveals potentially affected stress response-related signalling pathways. Abstract: 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.