ABNORMAL DISTRIBUTION OF CATHEPSIN PROTEINASES AND ENDOGENOUS INHIBITORS (CYSTATINS) IN THE HIPPOCAMPUS OF PATIENTS WITH ALZHEIMERS-DISEASE, PARKINSONISM-DEMENTIA COMPLEX ON GUAM, AND SENILE DEMENTIA AND IN THE AGED

被引:78
作者
II, K
ITO, H
KOMINAMI, E
HIRANO, A
机构
[1] KITANO HOSP, DEPT NEUROL, OSAKA, JAPAN
[2] JUNTENDO UNIV, SCH MED, DEPT BIOCHEM, TOKYO 113, JAPAN
[3] YESHIVA UNIV ALBERT EINSTEIN COLL MED, MONTEFIORE MED CTR, DIV NEUROPATHOL, BRONX, NY 10461 USA
关键词
CATHEPSINS; CYSTATINS; IMMUNOHISTOCHEMISTRY; ALZHEIMERS DISEASE; PARKINSONISM-DEMENTIA COMPLEX ON GUAM;
D O I
10.1007/BF01614769
中图分类号
R602 [外科病理学、解剖学]; R32 [人体形态学];
学科分类号
100101 ;
摘要
The immunolocalization of cathepsins B(CB), H and L and cystatins alpha(Calpha) and beta(Cbeta) were examined in the hippocampus of cases of sporadic Alzheimer's disease (12 cases), parkinsonism-dementia complex on Guam (eight cases), senile dementia of Alzheimer type (two cases), aged subjects with marked senile change (one case) and controls (12 cases, including six normal subjects). CB was lower in most nerve cells in patients than in controls, but markedly increased at the sites of intracellular neurofibrillary tangles (NFTs) and degenerative neurites and/or dendrites in and outside senile plaques (SPs), indicating its close involvement in the metabolisms of various proteins in NFT and SPs. Abundant Calpha and Cbeta were demonstrated in SP amyloid, suggesting that they are amyloid constituents or co-exist with amyloid. The present study indicated that CB, Calpha and Cbeta are closely involved in abnormal protein metabolism in NFTs and SP amyloid and suggested that degeneration or denaturation of intracellular proteins, including substrates for proteases and lysosomes, from some acquired cause, results in absolute and/or relative overload for these proteolytic systems, including their inhibitors. This results in incomplete and/or abnormal proteolysis related to NFT and/or amyloid formation.
引用
收藏
页码:185 / 194
页数:10
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