Differential effects of glycation on protein aggregation and amyloid formation.
Differential effects of glycation on protein aggregation and amyloid formation.
复制标题
糖化对蛋白质聚集和淀粉样蛋白形成的差异作用。
DOI：
10.3389/fmolb.2014.00009
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发表时间：
2014
影响因子：
5
通讯作者：
Sirangelo I
中科院分区：
文献类型：
--
作者：
Iannuzzi C;Irace G;Sirangelo I
淀粉样蛋白是一类不溶性蛋白质物质，通常由错误折叠的蛋白质形成的直链无分支原纤维组成。阿尔茨海默病、传染性海绵状脑病和家族性淀粉样变性等构象疾病与受影响组织中淀粉样蛋白聚集体的存在有关。大多数病例是散发的，这表明几个因素必须有助于这些疾病的发作和进展。其中，在过去的10年中，蛋白质的非酶糖化被报道刺激蛋白质聚集和淀粉样蛋白沉积。在这篇综述中，我们分析了这一领域的最新进展，表明糖基化诱导的影响可能不会被广泛的强烈依赖于蛋白质结构。事实上，作为一种翻译后修饰，糖基化可以在促进、加速和/或稳定途径上和途径外物质方面差异性地影响聚集过程。
Amyloids are a class of insoluble proteinaceous substances generally composed of linear un-branched fibrils that are formed from misfolded proteins. Conformational diseases such as Alzheimer's disease, transmissible spongiform encephalopathies, and familial amyloidosis are associated with the presence of amyloid aggregates in the affected tissues. The majority of the cases are sporadic, suggesting that several factors must contribute to the onset and progression of these disorders. Among them, in the past 10 years, non-enzymatic glycation of proteins has been reported to stimulate protein aggregation and amyloid deposition. In this review, we analyze the most recent advances in this field suggesting that the effects induced by glycation may not be generalized as strongly depending on the protein structure. Indeed, being a post-translational modification, glycation could differentially affects the aggregation process in promoting, accelerating and/or stabilizing on-pathway and off-pathway species.