Sipe J D
Department of Biochemistry, Boston University School of Medicine, Massachusetts 02118.
Crit Rev Clin Lab Sci. 1994;31(4):325-54. doi: 10.3109/10408369409084679.
The biochemistry of amyloidosis as it relates to clinical medicine and experimental pathology is presented. Amyloidoses are complex disorders in which normally soluble precursors undergo pathological conformational changes and polymerize as insoluble fibrils with the beta-pleated sheet conformation. Over the past 20 years, 16 biochemically diverse proteins have been identified as fibrillar constituents of amyloid deposits; in all cases the protein-protein interactions that result in amyloid fibril formation appear to be stabilized both by the structure and the microenvironment of the precursor protein. Either genetic predisposition or dysfunctions of the immune system favor amyloid fibril formation. In particular, macrophage function is a factor in the pathogenesis of many of the amyloidoses. The diagnosis of amyloidosis involves acquisition of a tissue biopsy, staining of the specimen with Congo red, and observation of classic green birefringence on polarization microscopy. The subdiagnosis of the systemic amyloidoses involves characterization of variant or monoclonal plasma amyloid precursor proteins in the context of clinical symptoms. Treatment is generally supportive, with the use of antiinflammatory therapy, dialysis, or transplantation and genetic counseling where indicated.
本文介绍了与临床医学和实验病理学相关的淀粉样变性的生物化学。淀粉样变性是一种复杂的疾病，其中正常可溶的前体经历病理性构象变化，并聚合成具有β-折叠片层构象的不溶性纤维。在过去20年中，已鉴定出16种生化性质不同的蛋白质作为淀粉样沉积物的纤维成分；在所有情况下，导致淀粉样纤维形成的蛋白质-蛋白质相互作用似乎都通过前体蛋白质的结构和微环境而得以稳定。遗传易感性或免疫系统功能障碍均有利于淀粉样纤维的形成。特别是，巨噬细胞功能是许多淀粉样变性发病机制中的一个因素。淀粉样变性的诊断包括获取组织活检标本、用刚果红对标本进行染色以及在偏振显微镜下观察典型的绿色双折射。全身性淀粉样变性的亚诊断涉及在临床症状背景下对变异或单克隆血浆淀粉样前体蛋白的特征分析。治疗通常是支持性的，包括使用抗炎疗法、透析或移植，并在必要时进行遗传咨询。
