Kisilevsky R
Department of Pathology, Queen's University, Kingston, Ontario, Canada.
Ann N Y Acad Sci. 1997 Sep 26;826:117-27. doi: 10.1111/j.1749-6632.1997.tb48465.x.
Amyloid is a generic term referring to extracellular fibrillar protein deposits defined by their unique tinctorial, ultrastructural, and protein conformational properties. At least 17 different forms have been identified. In each form the deposit consists of a disease-specific (or pathologic process-specific) protein and a set of common components. The disease-specific protein serves as the basis for the classification of the amyloids. In inflammation-associated (AA) amyloid it can be demonstrated that interactive processes between serum amyloid A (SAA), the AA precursor, and the common components, are likely responsible for AA amyloid deposition. Understanding the details of these interactions provide targets for therapeutic interference that are successful in vivo. Analogous interactions take place between the common components and the beta-protein and beta-protein precursor responsible for the congophilic angiopathy and neuritic plaque amyloid in Alzheimer's disease. Interference with beta-protein/common component interaction in vitro both prevents and reverses beta-protein fibril assembly, indicating that successful delivery of effective agents across the blood-brain barrier should prevent and possibly reverse amyloid deposition in Alzheimer's disease.
淀粉样蛋白是一个通用术语，指的是细胞外纤维状蛋白质沉积物，其定义基于其独特的染色、超微结构和蛋白质构象特性。已鉴定出至少17种不同形式。在每种形式中，沉积物由疾病特异性（或病理过程特异性）蛋白质和一组共同成分组成。疾病特异性蛋白质是淀粉样蛋白分类的基础。在炎症相关（AA）淀粉样蛋白中，可以证明血清淀粉样蛋白A（SAA，AA前体）与共同成分之间的相互作用过程可能是AA淀粉样蛋白沉积的原因。了解这些相互作用的细节为体内成功的治疗干预提供了靶点。在共同成分与负责阿尔茨海默病中嗜刚果红血管病和神经炎性斑块淀粉样蛋白的β蛋白及β蛋白前体之间也发生类似的相互作用。体外干扰β蛋白/共同成分相互作用既能防止又能逆转β蛋白原纤维组装，这表明有效药物成功通过血脑屏障递送应能防止并可能逆转阿尔茨海默病中的淀粉样蛋白沉积。
