Carnosine and anserine act as effective transglycating agents in decomposition of aldose-derived Schiff bases.
Carnosine and anserine act as effective transglycating agents in decomposition of aldose-derived Schiff bases.
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DOI：
10.1016/j.bbrc.2005.08.033
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发表时间：
2005-10
影响因子：
3.1
通讯作者：
B. Szwergold
中科院分区：
文献类型：
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作者：
B. Szwergold
有许多出版物描述了肌肽（β-丙烯酰组氨酸）和雁氨酸（β-丙烯酰-1- n -甲基组氨酸）对细胞和器官功能的积极作用。我们特别感兴趣的是，这些二肽的作用是延缓和（在一个实例中）逆转非酶糖基化。迄今为止，对这些抗糖基化作用的主要解释是肌肽和鹅胺可以作为替代和竞争性糖基化靶标，从而保护蛋白质免受这一有害过程的影响。在本文中，我们记录了这两种肽可以延缓或逆转糖基化的另一种机制。这个过程涉及到非酶糖基化级联的最初中间体（醛胺，又称希夫碱）的分解，通过肌肽和/或羊丝氨酸对预形成的醛胺（如葡萄糖赖氨酸）的亲核攻击。如果未来的研究表明这种反应在生理上是重要的，那么这种机制可以解释肌肽和雁胺作为抗糖化剂的一些有益作用。
There are numerous publications describing the positive effects of carnosine (β-alanyl-histidine) and anserine (β-alanyl-1-N-methyl-histidine) on cell and organ function. Of special interest to us is the fact that these dipeptides act to retard and (in one instance) reverse non-enzymatic glycation. To date, the primary explanation for these anti-glycating effects has been the fact that carnosine and anserine can serve as alternative and competitive glycation targets, thereby protecting proteins from this deleterious process. In this paper, we document another mechanism by which these two peptides can retard or reverse glycation. The process involves decomposition of the very first intermediates of the non-enzymatic glycation cascade (aldosamines a.k.a. Schiff bases) by nucleophilic attack of carnosine and/or anserine on the preformed aldosamine such as glucosyl-lysine. If future research shows this reaction is to be physiologically important, this mechanism could explain some of the beneficial effects of carnosine and anserine as anti-glycating agents.