Carbonyl modified proteins in cellular regulation, aging, and disease.
The oxidative modification of proteins by reactive species is implicated in the etiology or progression of a panoply of disorders and diseases. The level of these modified molecules can be quantitated by measurement of the protein carbonyl content, which has been shown to increase in a variety of diseases and processes, notably during aging. For the most part, oxidatively modified proteins are not repaired and must be removed by proteolytic degradation, a process which normally proceeds very efficiently, from microorganisms to mammals. In eukaryotes, removal is usually carried out by the proteosome, which selectively degrades oxidatively modified proteins, whether they be damaged by reactive oxygen species or specifically oxidized by cellular regulatory processes. The molecular deficiencies that cause accumulation of oxidatively modified proteins are not identified, but regardless of cause, the accumulation is likely to disrupt normal cellular function.
Levine
Rodney L
RL
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, MD 20892-0312, USA. rlevine@nih.gov
D000375:Aging / Q000378:metabolism*; D000818:Animals; D002255:Carbonic Acid / Q000737:chemistry*; D004194:Disease / Q000209:etiology*; D006801:Humans; D009097:Multienzyme Complexes / Q000502:physiology*; D010084:Oxidation-Reduction; D011506:Proteins / Q000737:chemistry* / Q000378:metabolism*; D017382:Reactive Oxygen Species / Q000378:metabolism*
D009097:Multienzyme Complexes; D011506:Proteins; D017382:Reactive Oxygen Species; D002255:Carbonic Acid