Institute for Advanced Biosciences, Keio University, Tsuruoka, Yamagata, Japan.
Ann N Y Acad Sci. 2010 Jun;1197:33-9. doi: 10.1111/j.1749-6632.2009.05374.x.
By virtue of the progress in proteomics, the involvement of posttranslational modifications in aging has been more clearly demonstrated in recent years. We describe here that (1) carbonylation, a hallmark of protein oxidation in general, is paradoxically decreased in histone with aging and increased by calorie restriction (CR), (2) acetylation of lysine 9 and phosphorylation of serine 10 in histone H3 are decreased and increased, respectively, with aging, and (3) the acetylation level of multiple extranuclear proteins decreases significantly with aging, and the change was not only retarded but increased remarkably by CR in rat liver. Based on these findings, we discuss possible implications of the posttranslational protein modifications in biochemical processes underlying aging and CR-induced extension of life span.
近年来，得益于蛋白质组学的发展，翻译后修饰在衰老过程中的作用越来越明显。在这里，我们描述了以下内容：（1）羰基化，一般来说是蛋白质氧化的标志，在组蛋白中随着衰老而减少，但被热量限制（CR）所增加；（2）组蛋白 H3 上赖氨酸 9 的乙酰化和丝氨酸 10 的磷酸化分别随着衰老而减少和增加；（3）随着衰老，多个核外蛋白的乙酰化水平显著下降，而且这种变化不仅被延缓，而且在 CR 处理的大鼠肝脏中显著增加。基于这些发现，我们讨论了翻译后蛋白质修饰在衰老和 CR 诱导寿命延长的生化过程中的可能意义。
