TRANSGENIC MICE EXPRESSING THE AMYLOID-BETA PROTEIN-CONTAINING CARBOXYL-TERMINAL FRAGMENT OF THE ALZHEIMER AMYLOID PRECURSOR PROTEIN

被引：4

作者：

ARAKI, E

YAMADA, T

TAKEMURA, K

YAMAGUCHI, H

SAKIMURA, K

GOTO, I

SAKAKI, Y

机构：

[1] SHIONOGI INST MED SCI, OSAKA, JAPAN

[2] GUNMA UNIV, COLL MED CARE & TECHNOL, GUNMA, JAPAN

[3] NIIGATA UNIV, BRAIN RES INST, DEPT NEUROPHARMACOL, NIIGATA 951, JAPAN

[4] UNIV TOKYO, INST MED SCI, CTR HUMAN GENOME, TOKYO, JAPAN

来源：

AMYLOID-JOURNAL OF PROTEIN FOLDING DISORDERS | 1995年 / 2卷 / 02期

关键词：

ALZHEIMERS DISEASE (AD); AMYLOID PRECURSOR PROTEIN (A-BETA-PP); AMYLOID BETA; TRANSGENIC MICE; IMMUNOHISTOCHEMISTRY; NEURON SPECIFIC ENOLASE (NSE) PROMOTER;

D O I：

10.3109/13506129509031894

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：

The deposition of amyloid beta protein (A beta) in the brain is one of the main pathological features of Alzheimer's disease (AD). A beta is derived from the amyloid precursor protein (A beta PP). It was shown that the carboxyl-terminal 100 residues of A beta PP containing the A beta sequence could form amyloid-like fibrils, and could be neurotoxic in vitro. To investigate the relationship between this fragment and amyloidogenesis in vivo, we developed transgenic mice expressing the A beta-containing carboxyl-terminal fragment under the control of the neuron specific enolase promoter. In these mice, the mRNA from the transgene was expressed at a substantial level in the brain. However, immunohistochemical studies of the brains did not show any pathologic changes. These results suggest that the expression of the A beta containing carboxyl-terminal fragment itself may not directly lead to AD-like neuropathologic changes in vivo.

引用

页码：100 / 106

页数：7

共 29 条

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