Specific binding of amyloid-β-protein to IMR-32 neuroblastoma cell membrane

Authors

  • S. Inaba,

    1. S. Inaba, T. Okada and M. Kodaka, Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
      S. Inaba and T. Konakahara, Faculty of Industrial Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan
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  • T. Okada,

    1. S. Inaba, T. Okada and M. Kodaka, Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
      S. Inaba and T. Konakahara, Faculty of Industrial Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan
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  • T. Konakahara,

    1. S. Inaba, T. Okada and M. Kodaka, Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
      S. Inaba and T. Konakahara, Faculty of Industrial Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan
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  • M. Kodaka

    1. S. Inaba, T. Okada and M. Kodaka, Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology (AIST), Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan
      S. Inaba and T. Konakahara, Faculty of Industrial Science and Technology, Tokyo University of Science, 2641 Yamazaki, Noda, Chiba 278-8510, Japan
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M. Kodaka
Institute for Biological Resources and Functions
National Institute of Advanced Industrial Science and Technology (AIST)
Central 6, 1-1-1 Higashi Tsukuba
Ibaraki 305-8566
Japan
Tel.: +81-29-861-6124
Fax: +81-29-861-6123
E-mail: m.kodaka@aist.go.jp

Abstract:

In flow cytometry using two detecting methods, we have found that amyloid-β-protein(1–40) [Aβ(1–40)] has high affinity to IMR-32 neuroblastoma cell membrane when it is aggregated to form β-sheet conformation, whereas random coil small Aβ-species has low affinity. The difference in the binding ability to the cell membranes well accounts for the cytotoxicity of Aβ(1–40); namely, aggregated β-sheet Aβ(1–40) gives cytotoxicity higher than random coil Aβ(1–40). Specific binding between Aβ(1–40) and ganglioside GM1 of the raft-like domain in lipid membrane is suggested from a surface plasmon resonance (SPR) experiment.

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