Amyloids are primarily known for their roles in neurodegenerative disorders, as well as in systemic diseases like diabetes. Evolutionary forces tend to maintain a healthy set of heritable characteristics, while eliminating toxic or unfavourable elements; but amyloids seem to represent an exception to this fundamental concept. In addition to their presence in mammals, amyloids also persist in the proteome of many lower organisms that may be linked with possible roles in survival, which are still unexplored. Herein, we address some unanswered questions regarding amyloids: are these well‐structured proteinaceous aggregates a by‐product of inefficient folding events, or have they been retained in our protein repertoire for as yet unknown functional roles; and how do protein misfolding and associated disorders originate, despite the presence of protein quality‐control systems inside the cells? This review aims to extend our current understanding about the multifaceted useful properties of amyloids and their functional interactions with other molecular pathways in various species; this may provide new insights to identify novel therapeutic strategies for ageing and neurodegenerative diseases.

中文翻译：

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多个物种的淀粉样蛋白：它们对生存有帮助吗？

淀粉样蛋白主要因其在神经退行性疾病以及糖尿病等全身性疾病中的作用而闻名。进化力量倾向于保持一组健康的遗传特征，同时消除有毒或不利因素；但淀粉样蛋白似乎代表了这一基本概念的一个例外。除了它们在哺乳动物中的存在之外，淀粉样蛋白还存在于许多低等生物的蛋白质组中，这些生物可能与生存中的可能作用有关，这些作用仍未得到探索。在这里，我们解决了一些关于淀粉样蛋白的悬而未决的问题：这些结构良好的蛋白质聚集体是低效折叠事件的副产品，还是它们被保留在我们的蛋白质库中以发挥未知的功能作用？以及蛋白质错误折叠和相关疾病是如何起源的，尽管细胞内存在蛋白质质量控​​制系统？本综述旨在扩展我们目前对淀粉样蛋白的多方面有用特性及其与不同物种中其他分子途径的功能相互作用的理解；这可能为确定衰老和神经退行性疾病的新治疗策略提供新的见解。