Husby G
Scand J Rheumatol. 1980;9(1):60-4. doi: 10.1080/03009748009098131.
Results of recent research have made it possible to classify amyloidosis by means of the chemical and antigenic characteristics of the amyloid fibrils. The chemical classification of amyloid correlates quite well with the various clinical types of amyloidosis. Monoclonal immunoglobulins constitute a major part of primary amyloid fibrils, while amyloid protein AA plays a similar role in secondary amyloidosis. In addition, structural properties of amyloid fibril proteins derived from medullary carcinoma of the thyroid and from senile cardiac amyloidosis respectively, have been shown to be unique for these clinical types of localized amyloidosis. A protein identical or similar to prealbumin appears to constitute an amyloid fibril subunit in familial amyloidotic polyneuropathy. However, the mechanisms by which the various amyloid precursor proteins are converted to fibrils and deposited in the tissues are still not clear.
近期的研究结果使得通过淀粉样纤维的化学和抗原特性对淀粉样变性进行分类成为可能。淀粉样变性的化学分类与各种临床类型的淀粉样变性相当吻合。单克隆免疫球蛋白构成原发性淀粉样纤维的主要部分,而淀粉样蛋白AA在继发性淀粉样变性中起类似作用。此外,分别源自甲状腺髓样癌和老年心脏淀粉样变性的淀粉样纤维蛋白的结构特性,已被证明对于这些临床类型的局限性淀粉样变性是独特的。一种与前白蛋白相同或相似的蛋白质似乎构成家族性淀粉样多神经病中的淀粉样纤维亚基。然而,各种淀粉样前体蛋白转化为纤维并沉积在组织中的机制仍不清楚。