Role of oxidative carbonylation in protein quality control and senescence.
Proteins can become modified by a large number of reactions involving reactive oxygen species. Among these reactions, carbonylation has attracted a great deal of attention due to its irreversible and unrepairable nature. Carbonylated proteins are marked for proteolysis by the proteasome and the Lon protease but can escape degradation and form high-molecular-weight aggregates that accumulate with age. Such carbonylated aggregates can become cytotoxic and have been associated with a large number of age-related disorders, including Parkinson's disease, Alzheimer's disease, and cancer. This review focuses on the generation of and defence against protein carbonyls and speculates on the potential role of carbonylation in protein quality control, cellular deterioration, and senescence.
Nyström
Thomas
T
Department of Cell and Molecular Biology-Microbiology, Göteborg University, Göteborg, Sweden. thomas.nystrom@gmm.gu.se
D000367:Age Factors; D000375:Aging / Q000378:metabolism*; D000596:Amino Acids / Q000378:metabolism; D046912:Multiprotein Complexes / Q000737:chemistry / Q000378:metabolism*; D009942:Organometallic Compounds / Q000737:chemistry / Q000378:metabolism*; D010084:Oxidation-Reduction; D021381:Protein Transport; D011506:Proteins / Q000737:chemistry / Q000378:metabolism*; D017382:Reactive Oxygen Species / Q000378:metabolism
D000596:Amino Acids; D046912:Multiprotein Complexes; D009942:Organometallic Compounds; D011506:Proteins; D017382:Reactive Oxygen Species