NEUTRAL ENDOPEPTIDASE CAN HYDROLYZE BETA-AMYLOID(1-40) BUT SHOWS NO EFFECT ON BETA-AMYLOID PRECURSOR PROTEIN-METABOLISM

被引:176
作者
HOWELL, S
NALBANTOGLU, J
CRINE, P
机构
[1] UNIV MONTREAL,FAC MED,DEPT BIOCHIM,MONTREAL,PQ H3C 3J7,CANADA
[2] MCGILL UNIV,MONTREAL NEUROL INST,DEPT NEUROL & NEUROSURG,MONTREAL,PQ H3A 2B4,CANADA
基金
英国医学研究理事会;
关键词
BETA-AMYLOID; AMYLOID PRECURSOR PROTEIN; NEUTRAL ENDOPEPTIDASE (EC 3.4.24.11); ALZHEIMERS DISEASE; NEURO2A CELLS;
D O I
10.1016/0196-9781(95)00021-B
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
High performance liquid chromatographic analyses of incubations of beta-amyloid(1-40) with neutral endopeptidase revealed at least nine product peaks, indicating that neutral endopeptidase can cleave P-amyloid at multiple sites. Mass spectroscopic analysis of hydrolyzed P-amyloid identified at least five cleavage sites, between residues Glu(3)-Phe(4), Gly(9)-Trp(10), Phe(19)-Phe(20), Ala(30)-Ile(31), and Gly(33)-Leu(34). In contrast, amyloid precursor protein metabolism in Neuro2A cells was unaffected by the expression of recombinant neutral endopeptidase in the same cells or by the addition of a secreted form of neutral endopeptidase to spent Neuro2A cell media.
引用
收藏
页码:647 / 652
页数:6
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