Specific binding of amyloid-beta-protein to IMR-32 neuroblastoma cell membrane.
In flow cytometry using two detecting methods, we have found that amyloid-beta-protein(1-40) [Abeta(1-40)] has high affinity to IMR-32 neuroblastoma cell membrane when it is aggregated to form beta-sheet conformation, whereas random coil small Abeta-species has low affinity. The difference in the binding ability to the cell membranes well accounts for the cytotoxicity of Abeta(1-40); namely, aggregated beta-sheet Abeta(1-40) gives cytotoxicity higher than random coil Abeta(1-40). Specific binding between Abeta(1-40) and ganglioside GM1 of the raft-like domain in lipid membrane is suggested from a surface plasmon resonance (SPR) experiment.
Inaba
S
S
Institute for Biological Resources and Functions, National Institute of Advanced Industrial Science and Technology, Central 6, 1-1-1 Higashi, Tsukuba, Ibaraki 305-8566, Japan.
Okada
T
T
Konakahara
T
T
Kodaka
M
M
D016229:Amyloid beta-Peptides / Q000737:chemistry* / Q000378:metabolism* / Q000633:toxicity; D002462:Cell Membrane / Q000378:metabolism*; D002942:Circular Dichroism; D005434:Flow Cytometry / Q000379:methods; D005677:G(M1) Ganglioside / Q000378:metabolism; D006801:Humans; D008563:Membrane Lipids / Q000378:metabolism; D021962:Membrane Microdomains / Q000378:metabolism; D009447:Neuroblastoma / Q000378:metabolism*; D010446:Peptide Fragments / Q000737:chemistry / Q000378:metabolism / Q000633:toxicity; D011487:Protein Conformation; D020349:Surface Plasmon Resonance; D018675:Toxicity Tests; D014407:Tumor Cells, Cultured
D016229:Amyloid beta-Peptides; D008563:Membrane Lipids; D010446:Peptide Fragments; C078592:amyloid beta-protein (1-40); D005677:G(M1) Ganglioside