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Methionine oxidation and aging.

Earl R Stadtman1, Holly Van Remmen, Arlan Richardson

  • 1Laboratory of Biochemistry, National Heart, Lung and Blood Institute, Bethesda, MD 20892, USA. Earl.Stadtman@nih.gov

Biochimica Et Biophysica Acta
|February 1, 2005
PubMed
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Oxidized proteins, particularly methionine sulfoxide (MetO), increase with age. Methionine sulfoxide reductases (Msr

Area of Science:

  • Biochemistry
  • Molecular Biology
  • Gerontology

Background:

  • Oxidative stress from reactive oxygen species (ROS) damages proteins, accumulating during aging and disease.
  • Sulfur-containing amino acids like methionine and cysteine are particularly susceptible to ROS-induced oxidation.
  • Oxidation of methionine to methionine sulfoxide (MetO) is reversible via methionine sulfoxide reductases (Msr's).

Purpose of the Study:

  • To review studies on methionine sulfoxide (MetO) accumulation during aging.
  • To explore the mechanisms influencing MetO levels and the role of Msr activity in aging.

Main Methods:

  • Literature review of studies investigating protein oxidation and aging.
  • Analysis of MetO levels in various aging models (replicative senescence, erythrocytes, mouse tissues).

Related Experiment Videos

  • Examination of factors affecting MetO levels, including ROS generation, antioxidant capacity, proteolysis, and Msr activity.

    • Main Results:

    • Protein MetO content increases with age in replicative senescence and erythrocyte aging models.
    • MetO levels did not increase with age in mouse tissues.
    • Aging is associated with decreased Msr activity in some animal tissues.

    Conclusions:

    • Changes in MetO levels reflect complex alterations in oxidative balance and repair mechanisms.
    • Decreased Msr activity contributes to MetO accumulation and is linked to reduced lifespan.
    • Enhanced Msr activity may extend maximum lifespan, highlighting its critical role in aging.