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| Content Provider | World Health Organization (WHO)-Global Index Medicus |
|---|---|
| Author | Tinker-mill, Claire Tabner, Brian J. Mayes, Jennifer Zhang, Hao Kolosov, Oleg Allsop, David |
| Description | Author Affiliation: Mayes J ( From the Division of Biomedical and Life Sciences, Faculty of Health and Medicine.) |
| Abstract | According to the 'amyloid cascade' hypothesis of Alzheimer disease, the formation of Aß fibrils and senile plaques in the brain initiates a cascade of events leading to the formation of neurofibrillary tangles, neurodegeneration, and the symptom of dementia. Recently, however, emphasis has shifted away from amyloid fibrils as the predominant toxic form of Aß toward smaller aggregates, referred to as 'soluble oligomers.' These oligomers have become one of the prime suspects for involvement in the early oxidative damage that is evident in this disease. This raises the question whether or not Aß fibrils are actually 'inert tombstones' present at the end of the aggregation process. Here we show that, when Aß(1-42) aggregates, including fibrils, are bound to Cu(II) ions, they retain their redox activity and are able to degrade hydrogen peroxide (H2O2) with the formation of hydroxyl radicals and the consequent oxidation of the peptide (detected by formation of carbonyl groups). We find that this ability increases as the Cu(II):peptide ratio increases and is accompanied by changes in aggregate morphology, as determined by atomic force microscopy. When aggregates are prepared in the copresence of Cu(II) and Zn(II) ions, the ratio of Cu(II):Zn(II) becomes an important factor in the degeneration of H2O2, the formation of carbonyl groups in the peptide, and in aggregate morphology. We believe, therefore, that Aß fibrils can destroy H2O2 and generate damaging hydroxyl radicals and, so, are not necessarily inert end points. |
| ISSN | 00219258 |
| e-ISSN | 1083351X |
| Journal | Journal of Biological Chemistry |
| Issue Number | 17 |
| Volume Number | 289 |
| Language | English |
| Publisher | American Society for Biochemistry and Molecular Biology (United States) |
| Publisher Date | 2014-04-25 |
| Publisher Place | United States |
| Access Restriction | Open |
| Subject Keyword | Alzheimer Disease Metabolism Amyloid Beta-Peptides Copper Hydrogen Peroxide Peptide Fragments Reactive Oxygen Species Microscopy, Atomic Force Protein Binding Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
| Content Type | Text |
| Resource Type | Article |
| Subject | Cell Biology Biochemistry Molecular Biology |
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