Format

Send to:

Choose Destination
See comment in PubMed Commons below
EMBO J. 2005 Apr 6;24(7):1311-7. Epub 2005 Mar 3.

Role of oxidative carbonylation in protein quality control and senescence.

Author information

  • 1Department of Cell and Molecular Biology-Microbiology, Göteborg University, Göteborg, Sweden. thomas.nystrom@gmm.gu.se

Abstract

Proteins can become modified by a large number of reactions involving reactive oxygen species. Among these reactions, carbonylation has attracted a great deal of attention due to its irreversible and unrepairable nature. Carbonylated proteins are marked for proteolysis by the proteasome and the Lon protease but can escape degradation and form high-molecular-weight aggregates that accumulate with age. Such carbonylated aggregates can become cytotoxic and have been associated with a large number of age-related disorders, including Parkinson's disease, Alzheimer's disease, and cancer. This review focuses on the generation of and defence against protein carbonyls and speculates on the potential role of carbonylation in protein quality control, cellular deterioration, and senescence.

PMID:
15775985
[PubMed - indexed for MEDLINE]
PMCID:
PMC1142534
Free PMC Article
PubMed Commons home

PubMed Commons

0 comments
How to join PubMed Commons

    Supplemental Content

    Full text links

    Icon for HighWire Icon for PubMed Central
    Loading ...
    Write to the Help Desk