CHARACTERIZATION OF AMYLOID FIBRIL PROTEIN FROM A CASE OF CEREBRAL AMYLOID ANGIOPATHY SHOWING IMMUNOHISTOCHEMICAL REACTIVITY FOR BOTH BETA PROTEIN AND CYSTATIN-C

被引：37
作者：
MARUYAMA, K
KAMETANI, F
IKEDA, S
ISHIHARA, T
YANAGISAWA, N
机构：
[1] SHINSHU UNIV,SCH MED,DEPT MED NEUROL,MATSUMOTO,NAGANO 390,JAPAN
[2] TOKYO INST PSYCHIAT,DEPT MOLEC BIOL,TOKYO,JAPAN
[3] YAMAGUCHI UNIV,SCH MED,DEPT PATHOL 1,UBE,YAMAGUCHI 755,JAPAN
来源：
NEUROSCIENCE LETTERS | 1992年 / 144卷 / 1-2期
关键词：
CEREBRAL AMYLOID ANGIOPATHY; AMYLOID; BETA-PROTEIN; CYSTATIN-C; AMINO ACID SEQUENCE;
D O I：
10.1016/0304-3940(92)90710-O
中图分类号：
Q189 [神经科学];
学科分类号：
071006 ;
摘要：
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.
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页码：38 / 42
页数：5
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