Cookies on this website
We use cookies to ensure that we give you the best experience on our website. If you click 'Continue' we'll assume that you are happy to receive all cookies and you won't see this message again. Click 'Find out more' for information on how to change your cookie settings.
Skip to main content

This chapter focuses on research aimed at detecting age-related increases in oxidative damage to protein or lipid components of the mitochondrion. Aging has been associated with both an increase in oxidative damage to proteins and a decrease in protein turnover and repair. The age-related increase in protein modifications includes cross-linkages, fragmentation, carbonylation, glycation, and advanced glycation end-product formation. Several research support mitochondria as the primary source of reactive oxygen species (ROS). Hence, mitochondrial proteins-including the complexes of the electron transport chain and members of other metabolic pathways-are likely to be particularly susceptible to modifications as a result of oxidative damage. Certain cellular components are known to be sensitive to oxidative stress. Specifically, proteins containing iron-sulfur clusters (Fe-S proteins) are highly sensitive to superoxide. Polyunsaturated fatty acids of membrane lipids are susceptible to peroxidation by ROS. The lipid peroxides (lipid-OOH) formed can decompose in the presence of transition metals such as iron to give alkoxy (lipid-O) radicals. These lipid radicals may alter membrane fluidity and subsequently affect the activity of membrane-bound proteins and membrane permeability, ultimately leading to cell degeneration. © 2005 Elsevier Inc. All rights reserved.

Original publication





Book title

Handbook of the Biology of Aging

Publication Date



124 - 148