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首页> 外文期刊>Biochemistry >Apolipoprotein E Inhibits the Depolymerization of #beta#2-Microglobulin-Related Amyloid Fibrils at a Neutral pH
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Apolipoprotein E Inhibits the Depolymerization of #beta#2-Microglobulin-Related Amyloid Fibrils at a Neutral pH

机译：载脂蛋白E在中性pH下抑制＃beta＃2-微球蛋白相关的淀粉样蛋白原纤维的解聚

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摘要

#beta#2-Microglobulin-related (A#beta#2M) amyloidosis is a common and serious complication in patients on long-term hemodialysis, and #beta#2-microglobulin (#beta#2-m) is a major structural component of A#beta#2M amyloid fibrils. Fluorescence spectroscopic analysis with thioflavin T and electron microscopic study revealed that A#beta#2M amyloid fibrils readily depolymerize into monomeric #beta#2-m at a neutral to basic pH. Circular dichroism analysis revealed that soon after the initiation of the depolymerizatioff reaction at pH 7.5, the characteristic spectrum of #beta#2-m in A#beta#2M amyloid fibrils changes to resemble that of monomeric #beta#2-m at pH 7.5. Apolipoprotein E (apoE), a representative amyloid-associated protein, formed a stable complex with A#beta#2M amyloid fibrils and inhibited the depolymerization of A#beta#2M amyloid fibrils dose-dependently in a range of 0-10 .uM. These results showed that apoE could enhance the deposition of amyloid fibrils in vivo, possibly by binding directly to the surface of the fibrils and stabilizing the conformation of#beta#2-m in the fibrils.
机译：＃beta＃2-微球蛋白相关（A＃beta＃2M）淀粉样变性是长期血液透析患者常见且严重的并发症，而＃beta＃2-微球蛋白（＃beta＃2-m）是主要结构成分A＃beta＃2M淀粉样蛋白原纤维。用硫代黄素T进行的荧光光谱分析和电子显微镜研究表明，在中性至碱性pH下，A＃beta＃2M淀粉样蛋白原纤维易于解聚为单体＃beta＃2-m。圆二色性分析表明，在pH 7.5发生解聚反应后不久，A＃beta＃2M淀粉样原纤维中＃beta＃2-m的特征光谱发生变化，类似于在pH 7.5下单体＃beta＃2-m的特征光谱。载脂蛋白E（apoE），一种代表性的淀粉样蛋白相关蛋白，与A＃beta＃2M淀粉样蛋白原纤维形成稳定的复合物，并在0-10 uM范围内剂量依赖性抑制A＃beta＃2M淀粉样蛋白原纤维的解聚。这些结果表明，apoE可能通过直接结合至原纤维的表面并稳定原纤维中的＃beta＃2-m的构象而增强了体内淀粉样原纤维的沉积。

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