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Content Provider | World Health Organization (WHO)-Global Index Medicus |
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Author | Komatsu, Hiroaki Uryu, Kunihiro Liu, Liu Xiao, Gang Lawson, John A. Axelsen, Paul H. Murray, Ian V. J. |
Description | Author Affiliation: Murray IV ( Department of Pharmacology, Center for Neurodegenerative Disease Research, Penn Genomics Institute, University of Pennsylvania, Philadelphia, PA 19104, USA.) |
Abstract | Evidence of oxidative stress and the accumulation of fibrillar amyloid beta proteins (Abeta) in senile plaques throughout the cerebral cortex are consistent features in the pathology of Alzheimer disease. To define a mechanistic link between these two processes, various aspects of the relationship between oxidative lipid membrane damage and amyloidogenesis were characterized by chemical and physical techniques. Earlier studies of this relationship demonstrated that oxidatively damaged synthetic lipid membranes promoted amyloidogenesis. The studies reported herein specify that 4-hydroxy-2-nonenal (HNE) is produced in both synthetic lipids and human brain lipid extracts by oxidative lipid damage and that it can account for accelerated amyloidogenesis. Abeta promotes the copper-mediated generation of HNE from polyunsaturated lipids, and in turn, HNE covalently modifies the histidine side chains of Abeta. HNE-modified Abeta have an increased affinity for lipid membranes and an increased tendency to aggregate into amyloid fibrils. Thus, the prooxidant activity of Abeta leads to its own covalent modification and to accelerated amyloidogenesis. These results illustrate how lipid membranes may be involved in templating the pathological misfolding of Abeta, and they suggest a possible chemical mechanism linking oxidative stress with amyloid formation. |
ISSN | 00219258 |
e-ISSN | 1083351X |
Journal | Journal of Biological Chemistry |
Issue Number | 13 |
Volume Number | 282 |
Language | English |
Publisher | American Society for Biochemistry and Molecular Biology (United States) |
Publisher Date | 2007-03-30 |
Publisher Place | United States |
Access Restriction | Open |
Subject Keyword | Amyloid Beta-Peptides Biosynthesis Toxicity Membrane Lipids Physiology Oxidative Stress Brain Cytology Drug Effects Metabolism Cell Membrane Child, Preschool Oxidation-Reduction Research Support, N.I.H., Extramural Research Support, Non-U.S. Gov't Biochemistry Molecular Biology |
Content Type | Text |
Resource Type | Article |
Subject | Molecular Biology Cell Biology Biochemistry |
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