Rattan S I, Derventzi A, Clark B F
Department of Chemistry, Aarhus University, Denmark.
Ann N Y Acad Sci. 1992 Nov 21;663:48-62. doi: 10.1111/j.1749-6632.1992.tb38648.x.
Posttranslational modifications of proteins are involved in determining their activities, stability, and specificity of interaction. More than 140 major and minor modifications of proteins have been reported. Of these, only a few have been studied in relation to the aging of cells, tissues, and organisms. These include phosphorylation, methylation, ADP-ribosylation, oxidation, glycation, and deamidation. Several of these modifications occur on proteins involved in crucial cellular processes, such as DNA synthesis, protein synthesis, protein degradation, signal transduction, cytoskeletal organization, and the components of extracellular matrix. Some of the modifications are the markers of abnormal and altered proteins for rapid degradation. Others make them less susceptible to degradation by normal proteolytic enzymes, and hence these accumulate during aging.
蛋白质的翻译后修饰参与决定其活性、稳定性及相互作用的特异性。据报道，蛋白质有超过140种主要和次要修饰。其中，仅有少数修饰与细胞、组织和生物体的衰老相关。这些修饰包括磷酸化、甲基化、ADP核糖基化、氧化、糖基化和脱酰胺作用。其中一些修饰发生在参与关键细胞过程的蛋白质上，如DNA合成、蛋白质合成、蛋白质降解、信号转导、细胞骨架组织以及细胞外基质的成分。一些修饰是异常和改变的蛋白质快速降解的标记。其他修饰则使它们不易被正常的蛋白水解酶降解，因此这些修饰在衰老过程中会积累。
