Maruyama K, Kametani F, Ikeda S, Ishihara T, Yanagisawa N
Department of Medicine (Neurology), Shinshu University School of Medicine, Matsumoto, Japan.
Neurosci Lett. 1992 Sep 14;144(1-2):38-42. doi: 10.1016/0304-3940(92)90710-o.
We isolated and carried out a chemical analysis of the amyloid fibril protein from the leptomeningeal vessels of a case with non-hereditary cerebral amyloid angiopathy (CAA) showing dual immunohistochemical reactivity with antibodies to both beta-protein and cystatin C. A crude amyloid fibril fraction reacted only with anti-beta-protein antibody, and cystatin C immunoreactivity was observed in the first PBS supernatant. Complete amino acid sequence of this cystatin C-immunoreactive protein showed a homologous structure to that of normal cystatin C. It is concluded that cystatin C is not an intrinsic component of the amyloid fibril in this type of CAA.
我们从一例非遗传性脑淀粉样血管病（CAA）患者的软脑膜血管中分离出淀粉样原纤维蛋白并进行了化学分析，该患者的淀粉样原纤维蛋白与β蛋白和胱抑素C抗体均呈现双重免疫组化反应性。粗制的淀粉样原纤维部分仅与抗β蛋白抗体反应，而在首次磷酸盐缓冲盐水（PBS）上清液中观察到胱抑素C免疫反应性。这种胱抑素C免疫反应性蛋白的完整氨基酸序列显示出与正常胱抑素C同源的结构。得出的结论是，在这类CAA中，胱抑素C不是淀粉样原纤维的固有成分。
