title: Proteins bearing oxidation-induced carbonyl groups are not preferentially ubiquitinated.
abstract: A substantial part of soluble, oxidized proteins are degraded by the proteasome. However, it is still under debate whether these oxidized proteins are degraded by the 26S proteasome in an ubiquitin-dependent way or in an ubiquitin-independent way by the 20S proteasome. Therefore, we treated cells with H(2)O(2) and UV-A irradiation and detected protein carbonyls and ubiquitination by immunoblotting. Separation of ubiquitinated proteins from non-ubiquitinated reveals that most oxidized proteins are not ubiquitinated.
authors.affiliation: Institute of Nutrition, Department of Nutritional Toxicology, Friedrich Schiller University Jena, Dornburger Straße 24, 07743 Jena, Germany.
authors.forename: Marc
authors.initials: M
authors.lastname: Kästle
authors.forename: Tilman
authors.initials: T
authors.lastname: Grune
mesh_terms: D045744:Cell Line, Tumor; D006801:Humans; D006861:Hydrogen Peroxide / Q000494:pharmacology*; D010084:Oxidation-Reduction; D018384:Oxidative Stress; D050050:Protein Carbonylation; D011499:Protein Processing, Post-Translational; D011506:Proteins / Q000378:metabolism*; D054875:Ubiquitination; D014466:Ultraviolet Rays
chemical_list: D011506:Proteins; D006861:Hydrogen Peroxide