Human brain beta-secretase contains heparan sulfate glycoconjugates

被引:5
作者
Matsumoto, A
Matsumoto, R
Enomoto, T
Baba, H
机构
[1] OSAKA TEISHIN HOSP,DEPT INTERNAL MED 1,OSAKA 543,JAPAN
[2] KOBE UNIV,SCH MED,DEPT INTERNAL MED 3,KOBE 650,JAPAN
关键词
serine protease; beta-secretase; beta-amyloid; heparan sulfate; Alzheimer's disease; negative charge; extracellular matrix;
D O I
10.1016/0304-3940(96)12723-3
中图分类号
Q189 [神经科学];
学科分类号
071006 ;
摘要
A polyclonal antibody against the 68 kDa beta-secretase was established, which recognizes a single 68 kDa band in brain homogenate of Alzheimer's disease patients and normal aged. Western analysis revealed that the protease is an acidic glycoprotein with negative charge on its glycoconjugate(s). Sensitiveness to heparitinase and glycopeptidase A indicates that the protease contains asparagine-linked oligosaccharide with heparan sulfate moieties. Specific detection of the 68 kDa band in the analysis using anti-heparan sulfate antibody, and its Lime-course-dependent degradation, also confirm the above results. It seems that, like human blood coagulation factors IXa and XIa, the glycoconjugate(s) attached to the protease interfere with substrate specificity, stability and topological restriction of proteolysis in brain extracellular matrix, where diffuse plaque formation is taking place.
引用
收藏
页码:105 / 108
页数:4
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