Amyloid β‐protein (Aβ) associated with lipid molecules: immunoreactivity distinct from that of soluble Aβ

FEBS Letters

Ihara, Yasuo²  Chakrabartty, Avijit¹  McLaurin, JoAnne¹  Yanagisawa, Katsuhiko³  Michikawa, Makoto³ 

[1] Division of Molecular and Structural Biology, Ontario Cancer Institute and Department of Medical Biophysics, University of Toronto, 610 University Avenue, Toronto, Ontario M5G 2M9, Canada;Department of Neuropathology, Faculty of Medicine, University of Tokyo, 7-3-1, Hongo, Bunkyo-ku, Tokyo 113, Japan;Department of Dementia Research, National Institute for Longevity Sciences, 36-3 Gengo, Morioka, Obu 474, Japan

关键词: Alzheimer's disease;    Amyloid β-protein;    Monoclonal antibody;    GM1 ganglioside;    AD;    Alzheimer's disease;    Aβ;    amyloid β-protein;    βAPP;    β-amyloid precursor protein;    MG;    mixed ganglioside;    PC;    phosphatidylcholine;    PI;    phosphatidylinositol;   

DOI  :  10.1016/S0014-5793(97)01484-1

学科分类：生物化学/生物物理

来源: John Wiley & Sons Ltd.

【 摘 要 】

We previously identified a novel amyloid β-protein (Aβ), that binds to GM1 ganglioside, in brains exhibiting the early pathological changes of AD. In this study, we raised monoclonal antibodies, using membrane fractions containing abundant GM1 ganglioside-bound Aβ as antigens. Monoclonal antibody 4396, produced in this study, immunoprecipitates Aβ42 in the membrane fractions of brains with diffuse plaques, but does not react with soluble Aβ42 or GM1 ganglioside. Furthermore, this antibody recognizes the Aβ bound to lipid vesicles containing GM1 ganglioside, and unexpectedly, phosphatidylinositol. In contrast, a control anti-Aβ monoclonal antibody does not recognize the Aβ bound to these lipid vesicles. These results indicate that Aβ associated with lipids has an immunoreactivity distinct from that of soluble A.

【 授权许可】

Unknown