Galeazzi Luciano, Corder Elizabeth H, Galeazz Roberta, Casoli Tiziana, Valli M Beatrice, Giunta Sergio
Laboratorio Analisi Chimico-Cliniche, Microbiologiche e di Diagnostica Molecolare, INRCA (IRCSS), Ancona, Italy.
Amyloid. 2002 Jun;9(2):103-7.
Mattson et al. (9) demonstrated lysis of human red blood cells (RBC) exposed to amyloid peptide Abeta(25-35), a new experimental model for amyloid-beta toxicity. Lysis resulted from poreformation in the RBC membranes and was completely prevented by concurrent exposure to Congo red We demonstrate that human serum, purified ApoE from human plasma, and recombinant isoforms of ApoE neutralize the Abeta(25-35) cytotoxicity: the E2 and E4 isoforms were marginally more effective than E3. Second, we demonstrate that Abeta(25-35) forms fibrils in the reaction mixtures using electron-microscopy. Together these results suggest that the RBC model might be useful in preliminary identification of natural and synthetic substances able to protect against amyloid-beta cytotoxic effects due to fibrillar Abeta(25-35). Such compounds would be candidate molecules for testing in neuronal systems.
马特森等人（9）证明，暴露于淀粉样肽β（25 - 35）的人红细胞（RBC）会发生裂解，这是一种新的β淀粉样蛋白毒性实验模型。裂解是由红细胞膜上形成孔道导致的，同时暴露于刚果红可完全阻止这种裂解。我们证明，人血清、从人血浆中纯化的载脂蛋白E（ApoE）以及ApoE的重组同工型可中和β（25 - 35）的细胞毒性：E2和E4同工型比E3稍有效。其次，我们使用电子显微镜证明β（25 - 35）在反应混合物中形成纤维。这些结果共同表明，红细胞模型可能有助于初步鉴定能够防止因纤维状β（25 - 35）引起的β淀粉样蛋白细胞毒性作用的天然和合成物质。这类化合物将是在神经元系统中进行测试的候选分子。
