Aggregation of Amyloid .BETA.-Protein and Its Neurotoxicity: Enhancement by Aluminum and Other Metals.

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  • KURODA YOICHIRO
    Department of Molecular & Cellular Neurobiology, Tokyo Metropolitan Institute for Neuroscience
  • KAWAHARA MASAHIRO
    Department of Molecular & Cellular Neurobiology, Tokyo Metropolitan Institute for Neuroscience

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Abstract

KURODA, Y. and KAWAHARA, M. Aggregation of Amyloid β-Protein and Its Neurotoxicity: Enhancement by Aluminum and Other Metals. Tohoku J. Exp. Med., 1994, 174 (3), 263-268 - The aggregation of amyloid β-protein has been suggested to enhance its neurotoxicity in cultured hippocampal neurons. We found that aluminum, an epidemiologic risk factor for Alzheimer's disease, promoted the aggregation of synthetic amyloid β-protein (β1-40) using immunoblotting and centrifugation. There were no significant changes by Ca or Mg. Other metals including Zn, Fe caused the small degree of aggregation compared to Al. Furthermore, β1-40 which was aggregated by aluminum was applied on cultured rat hippocampal neurons, and the characteristic deposition of amyloid fibrils was observed on cultured neurons. These results suggested that the degeneration of neurons and the deposition of amyloid β-protein were enhanced by aluminum

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