Kieliszek Marek, Sapazhenkava Katsiaryna
Department of Food Biotechnology and Microbiology, Institute of Food Sciences, Warsaw University of Life Sciences-SGGW, Nowoursynowska 159 C, Warsaw, 02-776, Poland.
Biol Trace Elem Res. 2025 Mar;203(3):1251-1268. doi: 10.1007/s12011-024-04245-x. Epub 2024 Jun 3.
In recent years, increasing attention has been paid to research on diseases related to the deposition of misfolded proteins (amyloids) in various organs. Moreover, modern scientists emphasise the importance of selenium as a bioelement necessary for the proper functioning of living organisms. The inorganic form of selenium-sodium selenite (redox-active)-can prevent the formation of an insoluble polymer in proteins. It is very important to undertake tasks aimed at understanding the mechanisms of action of this element in inhibiting the formation of various types of amyloid. Furthermore, yeast cells play an important role in this matter as a eukaryotic model organism, which is intensively used in molecular research on protein amyloidosis. Due to the lack of appropriate treatment in the general population, the problem of amyloidosis remains unsolved. This extracellular accumulation of amyloid is one of the main factors responsible for the occurrence of Alzheimer's disease. The review presented here contains scientific information discussing a brief description of the possibility of amyloid formation in cells and the use of selenium as a factor preventing the formation of these protein aggregates. Recent studies have shown that the yeast model can be successfully used as a eukaryotic organism in biotechnological research aimed at understanding the essence of the entire amyloidosis process. Understanding the mechanisms that regulate the reaction of yeast to selenium and the phenomenon of amyloidosis is important in the aetiology and pathogenesis of various disease states. Therefore, it is imperative to conduct further research and analysis aimed at explaining and confirming the role of selenium in the processes of protein misfolding disorders. The rest of the article discusses the characteristics of food protein amyloidosis and their use in the food industry. During such tests, their toxicity is checked because not all food proteins can produce amyloid that is toxic to cells. It should also be noted that a moderate diet is beneficial for the corresponding disease relief caused by amyloidosis.
近年来，人们越来越关注对各种器官中错误折叠蛋白（淀粉样蛋白）沉积相关疾病的研究。此外，现代科学家强调硒作为生物体正常功能所必需的生物元素的重要性。无机形式的硒——亚硒酸钠（具有氧化还原活性）——可以防止蛋白质中不溶性聚合物的形成。开展旨在了解该元素抑制各种类型淀粉样蛋白形成作用机制的任务非常重要。此外，酵母细胞作为真核模式生物在这一问题上发挥着重要作用，它被广泛应用于蛋白质淀粉样变性的分子研究中。由于普通人群中缺乏适当的治疗方法，淀粉样变性问题仍然没有得到解决。淀粉样蛋白的这种细胞外积累是导致阿尔茨海默病发生的主要因素之一。本文的综述包含了科学信息，讨论了细胞中淀粉样蛋白形成的可能性的简要描述以及硒作为防止这些蛋白质聚集体形成的因素的应用。最近的研究表明，酵母模型可以成功地用作真核生物，用于旨在理解整个淀粉样变性过程本质的生物技术研究。了解调节酵母对硒反应和淀粉样变性现象的机制在各种疾病状态的病因学和发病机制中很重要。因此，必须进行进一步的研究和分析，以解释和证实硒在蛋白质错误折叠疾病过程中的作用。文章的其余部分讨论了食物蛋白淀粉样变性的特征及其在食品工业中的应用。在这类测试中，会检查它们的毒性，因为并非所有食物蛋白都会产生对细胞有毒的淀粉样蛋白。还应注意的是，适度饮食有利于缓解由淀粉样变性引起的相应疾病。
