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Degradation Products of Amyloid Protein: Are They The Culprits?
Current Alzheimer Research ( IF 2.1 ) Pub Date : 2020-08-31 , DOI: 10.2174/1567205017666201203142103
Dmitry V Zaretsky 1 , Maria Zaretskaia 1
Affiliation  

Objectives: Beta-amyloid (Aβ) peptides are most toxic to cells in oligomeric form. It is commonly accepted that oligomers can form ion channels in cell membranes and allow calcium and other ions to enter cells. The activation of other mechanisms, such as apoptosis or lipid peroxidation, aggravates the toxicity, but it itself can result from the same initial point, that is, ion disturbance due to an increased permeability of membranes. However, experimental studies of membrane channels created by Aβ are surprisingly limited.

Methods: Here, we report a novel flow cytometry technique which can be used to detect increased permeability of membranes to calcium induced by the exposure to amyloid peptides. Calcium entry into the liposome is monitored using calcium-sensitive fluorescent probe. Undamaged lipid membranes are not permeable to calcium. Liposomes that are prepared in a calcium-free medium become able to accumulate calcium in a calcium-containing medium only after the formation of channels.


中文翻译:

淀粉样蛋白的降解产物:它们是罪魁祸首吗?

目的:β-淀粉样蛋白 (Aβ) 肽对寡聚形式的细胞毒性最大。人们普遍认为,低聚物可以在细胞膜中形成离子通道并允许钙和其他离子进入细胞。其他机制的激活,如细胞凋亡或脂质过氧化,会加剧毒性,但它本身可能来自相同的起始点,即由于膜通透性增加引起的离子干扰。然而,由 Aβ 产生的膜通道的实验研究令人惊讶地有限。

方法:在这里,我们报告了一种新的流式细胞术技术,该技术可用于检测由暴露于淀粉样肽引起的膜对钙的渗透性增加。使用钙敏感荧光探针监测钙进入脂质体的情况。未损坏的脂质膜不能渗透钙。在无钙培养基中制备的脂质体只有在通道形成后才能在含钙培养基中积累钙。
更新日期:2020-08-31
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