Dember Laura M
Renal Section, Boston University School of Medicine, EBRC 504, 650 Albany Street, Boston, MA 02118, USA.
J Am Soc Nephrol. 2006 Dec;17(12):3458-71. doi: 10.1681/ASN.2006050460. Epub 2006 Nov 8.
The amyloidoses are a group of disorders in which soluble proteins aggregate and deposit extracellularly in tissues as insoluble fibrils, causing progressive organ dysfunction. The kidney is one of the most frequent sites of amyloid deposition in AL, AA, and several of the hereditary amyloidoses. Amyloid fibril formation begins with the misfolding of an amyloidogenic precursor protein. The misfolded variants self-aggregate in a highly ordered manner, generating protofilaments that interact to form fibrils. The fibrils have a characteristic appearance by electron microscopy and generate birefringence under polarized light when stained with Congo red dye. Advances in elucidating the mechanisms of amyloid fibril formation, tissue deposition, and tissue injury have led to new and more aggressive treatment approaches for these disorders. This article reviews the pathogenesis, diagnosis, clinical manifestations, and treatment of the amyloidoses, focusing heavily on the renal aspects of each of these areas.
淀粉样变性是一组疾病，其中可溶性蛋白质聚集并以不溶性纤维的形式在组织细胞外沉积，导致进行性器官功能障碍。肾脏是AL、AA及几种遗传性淀粉样变性中淀粉样蛋白沉积最常见的部位之一。淀粉样纤维的形成始于淀粉样前体蛋白的错误折叠。错误折叠的变体以高度有序的方式自我聚集，产生原丝，原丝相互作用形成纤维。这些纤维在电子显微镜下具有特征性外观，用刚果红染料染色后在偏振光下产生双折射。在阐明淀粉样纤维形成、组织沉积和组织损伤机制方面的进展，已导致针对这些疾病的新的、更积极的治疗方法。本文综述了淀粉样变性的发病机制、诊断、临床表现及治疗，重点关注这些领域中每个方面的肾脏问题。
