Transferrin neutralization of amyloid β 25-35 cytotoxicity

被引:25
作者
Giunta, S
Galeazzi, R
Valli, MB
Corder, EH
Galeazzi, L
机构
[1] IRCCS, Lab Anal Chim Clin Microbiol & Diagnost Mol, Ospedale Geriatr INRCA, I-60100 Ancona, Italy
[2] Duke Univ, Ctr Demog Studies, Durham, NC 27708 USA
关键词
transferrin; amyloid beta; Alzheimer pathogenesis; red blood cells;
D O I
10.1016/j.cccn.2004.07.025
中图分类号
R446 [实验室诊断]; R-33 [实验医学、医学实验];
学科分类号
1001 [基础医学];
摘要
Background: Fibrillar aggregates of amyloid beta 25-35 (Abeta(25-35)) form rapidly in vitro able to lyse human red blood cells (RBCs). Human sera, albumin, and apolipoprotein E (ApoE) each limit fibrillation and cytotoxicity. Potentially, these substances protect neurons from Abeta(1-40/42) aggregates. Transferrin (TF) is investigated in this study. Methods: The Mattson red blood cells model was employed to determine whether co-incubation of transferrin and Abeta(25-35) prevented lysis. The formation of fibrillar Abeta(25-35) in the presence of transferrin was investigated using Congo red staining and spectrophotometric studies. Results: We found that incubation of 20 muM Abeta(25-35) with physiologic levels of transferrin prevented red blood cells lysis and the formation of macro-aggregates. Conclusions: These in vitro results suggest that transferrin may limit fibrillar amyloid formation in vivo and cytotoxicity. (C) 2004 Published by Elsevier B.V.
引用
收藏
页码:129 / 136
页数:8
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