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Age-related changes in oxidized proteins.

C N Oliver, B W Ahn, E J Moerman

    The Journal of Biological Chemistry
    |April 25, 1987
    PubMed
    Summary
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    Oxidative modification of proteins increases with age, leading to reduced enzyme activity. This process is accelerated in aging cells and genetic aging disorders, suggesting a key role in the aging process.

    Area of Science:

    • Biochemistry
    • Cellular Aging
    • Oxidative Stress

    Background:

    • Oxidative inactivation of metabolic enzymes is a known phenomenon.
    • Accumulation of less active enzymes is observed during cellular aging.

    Purpose of the Study:

    • To investigate the levels of oxidatively modified proteins in aging model systems.
    • To correlate these changes with enzyme activity and heat lability.

    Main Methods:

    • Analysis of oxidatively modified proteins in circulating erythrocytes and cultured fibroblasts.
    • Comparison of protein modification levels in normal aging versus genetic progeroid syndromes.
    • Enzymatic assays and heat stability tests on modified enzymes.

    Main Results:

    Related Experiment Videos

    • Oxidatively modified protein levels increase with age in erythrocytes, correlating with decreased enzyme activity.
    • In fibroblasts, increased protein modification is observed after age 60 and significantly elevated in progeria and Werner's syndrome.
    • Oxidative modification of glucose-6-phosphate dehydrogenase increases its heat lability.

    Conclusions:

    • Oxidative modification of proteins contributes to the loss of enzyme function and increased heat lability during aging.
    • Mixed function oxidation systems play a role in age-related enzyme dysfunction.
    • Accelerated oxidative modification in progeroid syndromes highlights its significance in premature aging.