Schultz R T
Am J Pathol. 1977 Feb;86(2):321-41.
Heavily radiolabeled plasma proteins were injected intravenously into mice with experimentally induced amyloid lesions, and the distribution of the labeled protein with respect to vascular spaces and the amyloid lesions determined by autoradiography. Radiolabeled albumin and IgG entered early amyloid lesions so quickly and in such high concentration as to indicate that much of the volume of these early lesions must be occupied by circulating plasma. Entry of these same proteins into advanced lesions was definitely reduced. High-molecular-weight proteins remained largely in vascular spaces. In situ saline perfusion resulted in considerable removal of protein from early lesions but very little alteration in their greenish-yellow birefringence when stained with Congo red. An initial alteration in vascular permeability with circulation of plasma proteins in tissue spaces quickly followed by a progressively increasing deposition of fibrous proteins on an underlying cellular framework may be the sequence of events in amyloid formation.
将放射性标记程度很高的血浆蛋白静脉注射到患有实验性诱导淀粉样病变的小鼠体内，通过放射自显影确定标记蛋白相对于血管间隙和淀粉样病变的分布。放射性标记的白蛋白和免疫球蛋白快速且以高浓度进入早期淀粉样病变，这表明这些早期病变的大部分体积必定被循环血浆占据。相同蛋白进入晚期病变的情况明显减少。高分子量蛋白主要留在血管间隙。原位盐水灌注导致早期病变中的蛋白大量清除，但用刚果红染色时其黄绿双折射变化很小。血管通透性最初改变，血浆蛋白在组织间隙循环，随后纤维蛋白在潜在细胞框架上逐渐沉积增加，这可能是淀粉样蛋白形成过程中的一系列事件。
