Nyström Thomas
Department of Cell and Molecular Biology-Microbiology, Göteborg University, Göteborg, Sweden.
EMBO J. 2005 Apr 6;24(7):1311-7. doi: 10.1038/sj.emboj.7600599. Epub 2005 Mar 3.
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.
蛋白质可通过大量涉及活性氧的反应发生修饰。在这些反应中，羰基化因其不可逆和不可修复的特性而备受关注。羰基化蛋白质会被蛋白酶体和Lon蛋白酶标记以待蛋白水解，但它们可能逃脱降解并形成随年龄增长而积累的高分子量聚集体。这种羰基化聚集体可能具有细胞毒性，并与大量与年龄相关的疾病有关，包括帕金森病、阿尔茨海默病和癌症。本综述聚焦于蛋白质羰基的产生及防御，并推测羰基化在蛋白质质量控制、细胞退化和衰老中的潜在作用。
