title: Redox proteomic investigation of tetracycline-induced steatosis.
abstract: Pathological levels of oxidative stress (OS) have been implicated in a broad spectrum of diseases. Carbonylation is an irreversible PTM that is considered as a universal indicator of OS. The development of new enrichment techniques coupled with the introduction of highly sensitive mass spectrometers has allowed the identification of carbonylated proteins in biological systems. In this study, Deng et al. (Proteomics 2015, 15, 148-159) utilized one of these methods to isolate and identify carbonylated proteins that are involved in tetracycline-induced steatosis. They identified 26 proteins that are targets of OS and most of them were located in the mitochondria. A key carbonylated protein that was identified is long chain specific acyl-CoA dehydrogenase, which has a major role in the β-oxidation of fatty acids. The researchers concluded that tetracycline-induced steatosis is a two-step process that involves lipid overload followed by OS.
authors.affiliation: Global Research and Development, Hospira Inc, Lake Forest, IL, USA.
authors.forename: Ashraf G
authors.initials: AG
authors.lastname: Madian
mesh_terms: D000818:Animals; D000900:Anti-Bacterial Agents; D005234:Fatty Liver / Q000139:chemically induced* / Q000378:metabolism*; D006801:Humans; D008099:Liver / Q000473:pathology*; D008297:Male; D050050:Protein Carbonylation; D011506:Proteins / Q000378:metabolism*; D013752:Tetracycline
chemical_list: D000900:Anti-Bacterial Agents; D011506:Proteins; D013752:Tetracycline
keywords: Carbonylation; Liver steatosis; Oxidative stress; Reactive oxygen species (ROS); Tetracycline