Metal-catalyzed oxidative damage and oligomerization of the amyloid-peptide of Alzheimer's disease

被引:25
作者
Ali, FEA
Barnham, KJ
Barrow, CJ
Separovic, F [1 ]
机构
[1] Univ Melbourne, Sch Chem, Melbourne, Vic 3010, Australia
[2] Univ Melbourne, Dept Pathol, Melbourne, Vic 3010, Australia
关键词
D O I
10.1071/CH04026
中图分类号
O6 [化学];
学科分类号
0703 ;
摘要
The most common form of dementia in old age is Alzheimer's disease ( AD). The presence in the brain of senile plaque is the major pathological marker of AD. The plaques are primarily composed of aggregated amyloid-beta peptide (Abeta). Abeta is a 40 - 42 amino acid peptide that is a proteolytic product derived from the beta-amyloid precursor protein. The function of Abeta and the exact mechanism of Abeta aggregation and neurotoxicity are unclear. However, metal coordination by Abeta plays an important role in inducing aggregation and the generation of reactive oxygen species, which appears to be at least partially responsible for Abeta neurotoxicity. In this review we examine the role of copper and zinc ions in Abeta neurotoxicity, especially with regards to the generation of free radicals. We discuss the role of copper or zinc ions in oxidative damage and Abeta conformational changes and the relationship of these metals to AD.
引用
收藏
页码:511 / 518
页数:8
相关论文
共 118 条
[31]   Zinc takes the center stage:: its paradoxical role in Alzheimer's disease [J].
Cuajungco, MP ;
Fagét, KY .
BRAIN RESEARCH REVIEWS, 2003, 41 (01) :44-56
[32]   Zinc and Alzheimer's disease: Is there a direct link? [J].
Cuajungco, MP ;
Lees, GJ .
BRAIN RESEARCH REVIEWS, 1997, 23 (03) :219-236
[33]   Alzheimer's disease amyloid-β binds copper and zinc to generate an allosterically ordered membrane-penetrating structure containing superoxide dismutase-like subunits [J].
Curtain, CC ;
Ali, F ;
Volitakis, I ;
Cherny, RA ;
Norton, RS ;
Beyreuther, K ;
Barrow, CJ ;
Masters, CL ;
Bush, AI ;
Barnham, KJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2001, 276 (23) :20466-20473
[34]   Metal ions, pH, and cholesterol regulate the interactions of Alzheimer's disease amyloid-β peptide with membrane lipid [J].
Curtain, CC ;
Ali, FE ;
Smith, DG ;
Bush, AI ;
Masters, CL ;
Barnham, KJ .
JOURNAL OF BIOLOGICAL CHEMISTRY, 2003, 278 (05) :2977-2982
[35]  
Curtain Cyril C., 2003, Current Medicinal Chemistry - Immunology Endocrine & Metabolic Agents, V3, P309, DOI 10.2174/1568013033483276
[36]   Oxidative stress, antioxidant defenses, and damage removal, repair, and replacement systems [J].
Davies, KJA .
IUBMB LIFE, 2000, 50 (4-5) :279-289
[37]   Amyloid β peptides do not form peptide-derived free radicals spontaneously, but can enhance metal-catalyzed oxidation of hydroxylamines to nitroxides [J].
Dikalov, SI ;
Vitek, MP ;
Maples, KR ;
Mason, RP .
JOURNAL OF BIOLOGICAL CHEMISTRY, 1999, 274 (14) :9392-9399
[38]   Metal binding and oxidation of amyloid-β within isolated senile plaque cores:: Raman microscopic evidence [J].
Dong, J ;
Atwood, CS ;
Anderson, VE ;
Siedlak, SL ;
Smith, MA ;
Perry, G ;
Carey, PR .
BIOCHEMISTRY, 2003, 42 (10) :2768-2773
[39]  
Esler WP, 1996, J NEUROCHEM, V66, P723
[40]   A critical role for tyrosine residues in His6Ni-mediated protein cross-linking [J].
Fancy, DA ;
Kodadek, T .
BIOCHEMICAL AND BIOPHYSICAL RESEARCH COMMUNICATIONS, 1998, 247 (02) :420-426