 | REACTIVE OXYGEN SPECIES: FROM RADIATION TO MOLECULAR BIOLOGY: A Festschrift in Honor of Daniel L. Gilbert
Copyright © 2000 by the New York Academy of Sciences
description
Annals of the New York Academy of Sciences 899:191-208 (2000)
© 2000 New York Academy of Sciences
Protein Oxidation
EARL R. STADTMAN AND
RODNEY L. LEVINE
Laboratory of Biochemistry, National Heart, Lung, and Blood Institute, National Institutes of Health, Bethesda, Maryland 20892-0320 USA
Address for correspondence: Dr. Earl R. Stadtman, NIH, Building 3, Room 222, MSC 0342, Bethesda, MD 20892-0342. Voice: 301-496-4645; fax: 301-496-0599.
e-mail: erstadtman{at}nih.gov
The oxidative modification of proteins by reactive species, especially reactive oxygen species, is implicated in the etiology or progression of a panoply of disorders and diseases. These reactive species form through a large number of physiological and non-physiological reactions. An increase in the rate of their production or a decrease in their rate of scavenging will increase the oxidative modification of cellular molecules, including proteins. For the most part, oxidatively modified proteins are not repaired and must be removed by proteolytic degradation, and a decrease in the efficiency of proteolysis will cause an increase in the cellular content of oxidatively modified proteins. 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, most notably during aging. Accumulation of modified proteins disrupts cellular function either by loss of catalytic and structural integrity or by interruption of regulatory pathways.
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