Department of Biochemistry, School of Life Sciences, University of KwaZulu Natal, Westville Campus, Block F3, University Road, Private Bag X54001, Durban 4000, South Africa.
Biomed Res Int. 2013;2013:826706. doi: 10.1155/2013/826706. Epub 2013 Mar 31.
Amylin is primarily responsible for classifying type II diabetes as an amyloid (protein misfolding) disease as it has great potential to aggregate into toxic nanoparticles, thereby resulting in loss of pancreatic β-cells. Although type II diabetes is on the increase each year, possibly due to bad eating habits of modern society, research on the culprit for this disease is still in its early days. In addition, unlike the culprit for Alzheimer's disease, amyloid β-peptide, amylin has failed to receive attention worthy of being featured in an abundance of review articles. Thus, the aim of this paper is to shine the spotlight on amylin in an attempt to put it onto the top of researchers' to-do list since the secondary complications of type II diabetes have far-reaching and severe consequences on public health both in developing and fully developed countries alike. This paper will cover characteristics of the amylin aggregates, mechanisms of toxicity, and a particular focus on inhibitors of toxicity and techniques used to assess these inhibitors.
胰岛淀粉样多肽主要负责将 II 型糖尿病归类为淀粉样(蛋白错误折叠)疾病,因为它很容易聚集形成毒性纳米颗粒,从而导致胰腺β细胞丧失。尽管 II 型糖尿病每年都在增加,可能是由于现代社会不良的饮食习惯,但对这种疾病的罪魁祸首的研究仍处于早期阶段。此外,与阿尔茨海默病的罪魁祸首淀粉样β肽不同,胰岛淀粉样多肽尚未受到足够的关注,值得在大量评论文章中重点介绍。因此,本文旨在聚焦于胰岛淀粉样多肽,试图将其置于研究人员的待办事项清单之首,因为 II 型糖尿病的继发性并发症对发展中国家和发达国家的公共健康都有着深远而严重的影响。本文将涵盖胰岛淀粉样多肽聚集物的特征、毒性机制,以及特别关注毒性抑制剂和用于评估这些抑制剂的技术。