Department of Biochemistry and Molecular Biology, Mayo Clinic, Rochester, Minnesota 55905, USA.
Annu Rev Biochem. 2013;82:745-74. doi: 10.1146/annurev-biochem-072611-130030. Epub 2013 Feb 28.
The amyloidoses are a group of protein misfolding diseases in which the precursor protein undergoes a conformational change that triggers the formation of amyloid fibrils in different tissues and organs, causing cell death and organ failure. Amyloidoses can be either localized or systemic. In localized amyloidosis, amyloid deposits form at the site of precursor protein synthesis, whereas in systemic amyloidosis, amyloid deposition occurs distant from the site of precursor protein secretion. We review the type of proteins and cells involved and what is known about the complex pathophysiology of these diseases. We focus on light chain amyloidosis to illustrate how biochemical and biophysical studies have led to a deeper understanding of the pathogenesis of this devastating disease. We also review current cellular, tissue, and animal models and discuss the challenges and opportunities for future studies of the systemic amyloidoses.
淀粉样变性是一组蛋白质错误折叠疾病,其中前体蛋白发生构象变化,触发不同组织和器官中淀粉样纤维的形成,导致细胞死亡和器官衰竭。淀粉样变性可以是局部的也可以是系统性的。在局部淀粉样变性中,淀粉样沉积物在前体蛋白合成部位形成,而在系统性淀粉样变性中,淀粉样沉积物发生在远离前体蛋白分泌部位的地方。我们回顾了涉及的蛋白质和细胞类型,以及对这些疾病复杂病理生理学的了解。我们重点介绍轻链淀粉样变性,以说明生化和生物物理研究如何导致对这种破坏性疾病发病机制的更深入理解。我们还回顾了当前的细胞、组织和动物模型,并讨论了系统性淀粉样变性未来研究的挑战和机遇。