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.

引用

页码：38 / 42

页数：5

共 21 条

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