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J.Health Sci., 49(5), 341-347, 2003
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Aluminum-Induced Conformational Changes of beta-Amyloid Protein and the Pathogenesis of Alzheimer's Disease
Masahiro Kawahara*
Department of Analytical Chemistry, School of Pharmaceutical Sciences, Kyushu University of Health and Welfare, 1714-1 Yoshino-cho, Nobeoka-city, Miyazaki 882-8508, Japan
Aggregation and subsequent conformational change of Alzheimer's beta-amyloid protein (A beta P) enhance its neurotoxicity. Therefore, factors that inhibit or promote conformational changes of A beta P play crucial roles in the pathogenesis of Alzheimer's disease (AD). Moreover, recent studies have suggested that a common mechanism is based on the diverse diseases termed "conformational diseases" including neurodegenerative diseases such as AD, prion diseases, Parkinson's disease, and Huntington's disease. These diseases share similarity in the formation of beta-sheet containing amyloid fibrils by disease-related proteins and the introduction of apoptotic degeneration. Aluminum, an environmental risk factor for AD, is a widely used cross-linker that causes conformational changes of A beta P and other proteins. This report reviews and discusses characteristics of aluminum-induced conformational changes of A beta P and their implication in pathogenesis of AD. Taking together our results and those of numerous other studies, we hypothesize that aluminum-induced conformational changes enhance the neurotoxicity of A beta P and lead to development of AD.
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