Oxidative stress-induced proteome alterations target different cellular pathways in human myoblasts.

作者: Martin A. Baraibar , Janek Hyzewicz , Adelina Rogowska-Wrzesinska , Romain Ladouce , Peter Roepstorff

DOI: 10.1016/J.FREERADBIOMED.2011.06.032

关键词:

摘要: Although increased oxidative stress has been associated with the impairment of proliferation and function adult human muscle stem cells, proteins either involved in response or damaged by oxidation have not identified. A parallel proteomics approach was performed for analyzing protein expression profile as well preferentially oxidized upon hydrogen peroxide-induced stress. Fifteen were Among them, spots identified peroxiredoxins 1 6, glyceraldehyde-3-phosphate dehydrogenase, α-enolase shifted to a more acidic isoelectric point stress, indicating posttranslational modifications. Oxidized evidenced immunodetection derivatized carbonyl groups followed identification mass spectrometry. The carbonylated are mainly cytosolic carbohydrate metabolism, cellular assembly, homeostasis, synthesis degradation. Pathway analysis revealed skeletal muscular disorders, cell death, cancer-related main molecular networks altered. Interestingly, these pathways focused on two distinct proteins: p53 altered huntingtin carbonylation. This study emphasizes importance performing addressing different aspects proteome accurate view their changes

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