Hirschfield Gideon M
NHS National Amyloidosis Centre, Royal Free Hospital, London, UK.
Semin Cell Dev Biol. 2004 Feb;15(1):39-44. doi: 10.1016/j.semcdb.2003.12.013.
Amyloidosis encompasses a spectrum of diseases in which there is disordered folding of certain proteins that leads to them being deposited as insoluble fibrils in the extracellular space. The result of this process is impaired tissue structure and function. Amyloidosis may be acquired or hereditary and local or systemic, and is defined according to the identity of the fibril precursor protein. Over 20 unrelated proteins can form amyloid fibrils in vivo, which all share a lamellar cross-beta-sheet structure composed of non-covalently associated protein or peptide subunits. Glycosaminoglycans and the pentraxin protein, serum amyloid P component, are universal non-fibrillar constituents of amyloid deposits that are believed to play a role in fibrillogenesis and fibril persistence. Greater understanding of the processes underlying amyloidogenesis, at all levels from cellular to clinical, has led to improvements in diagnosis, monitoring and treatment of this group of diseases, as well as pointing to possible future therapies.
淀粉样变性包括一系列疾病，在这些疾病中，某些蛋白质发生错误折叠，导致它们以不溶性纤维的形式沉积在细胞外空间。这一过程的结果是组织结构和功能受损。淀粉样变性可以是获得性的或遗传性的，局部的或全身性的，并根据纤维前体蛋白的特性来定义。超过20种不相关的蛋白质可在体内形成淀粉样纤维，它们都具有由非共价结合的蛋白质或肽亚基组成的层状交叉β-片层结构。糖胺聚糖和五聚体蛋白血清淀粉样P成分是淀粉样沉积物普遍存在的非纤维成分，据信它们在纤维形成和纤维持续存在中起作用。从细胞水平到临床水平，对淀粉样变性发生过程的更深入了解，已使这组疾病的诊断、监测和治疗得到改善，并指出了未来可能的治疗方法。
