Giunta Sergio, Galeazzi Roberta, Valli M Beatrice, Corder Elizabeth H, Galeazzi Luciano
Laboratorio Analisi Chimico-Cliniche, Microbiologiche e Diagnostica Molecolare, Ospedale Geriatrico INRCA (IRCCS), via della Montagnola 81, 60100 Ancona, Italy.
Clin Chim Acta. 2004 Dec;350(1-2):129-36. doi: 10.1016/j.cccn.2004.07.025.
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.
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.
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.
These in vitro results suggest that transferrin may limit fibrillar beta amyloid formation in vivo and cytotoxicity.
淀粉样β蛋白25 - 35（Aβ(25 - 35)）的纤维状聚集体在体外能迅速形成，可溶解人红细胞（RBCs）。人血清、白蛋白和载脂蛋白E（ApoE）均可限制纤维化和细胞毒性。这些物质可能保护神经元免受Aβ(1 - 40/42)聚集体的影响。本研究对转铁蛋白（TF）进行了探究。
采用马特森红细胞模型来确定转铁蛋白与Aβ(25 - 35)共同孵育是否能防止红细胞溶解。使用刚果红染色和分光光度研究来探究在转铁蛋白存在的情况下纤维状Aβ(25 - 35)的形成。
我们发现，20μM的Aβ(25 - 35)与生理水平的转铁蛋白共同孵育可防止红细胞溶解以及大聚集体的形成。
这些体外实验结果表明，转铁蛋白可能在体内限制纤维状β淀粉样蛋白的形成及细胞毒性。
