ABNORMAL AND DEFICIENT PROCESSING OF BETA-AMYLOID PRECURSOR PROTEIN IN FAMILIAL ALZHEIMERS-DISEASE LYMPHOBLASTOID-CELLS

被引：38

作者：

MATSUMOTO, A ^{[1
]}

FUJIWARA, Y ^{[1
]}

机构：

[1] KOBE UNIV,SCH MED,DEPT RADIAT BIOPHYS,KUSUNOKI CHO 7-5-1,CHUO KU,KOBE 650,JAPAN

来源：

BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS | 1991年 / 175卷 / 02期

关键词：

D O I：

10.1016/0006-291X(91)91572-T

中图分类号：

Q5 [生物化学]; Q7 [分子生物学];

学科分类号：

071010 ; 081704 ;

摘要：

Western blot analysis showed abnormal processing of β-amyloid precursor protein (APP) in lymphoblastoid cell lines (LCLs) of familial Alzheimer's disease (FAD). Antibody raised against central APP751 revealed that media of early and late-onset FAD LCLs had highly increased amounts of a 120 kD long-lived, SDS-stable, heat-labile complex of the Kunitz protease inhibitor domain of secreted APP and a ∼70 kD FAD-specific, yet unidentified serine protease. Antibody against the βA4-cytoplasmic domain showed a slower APP processing and increased amounts of 16 kD C-terminal preamyloid in lysates of early and late-onset FAD LCLs, first indicating a deficient intra-βA4 proteolysis in FAD as a possible cause of abundant amyloid deposits in AD brain. © 1991.

引用

页码：361 / 365

页数：5

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