Quantitative profiling of the pathological prion protein allotypes in bank voles by liquid chromatography-mass spectrometry
Quantitative profiling of the pathological prion protein allotypes in bank voles by liquid chromatography-mass spectrometry
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DOI：
10.1016/j.jchromb.2006.08.016
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发表时间：
2007-04-15
影响因子：
3
通讯作者：
Agrimi, U.
中科院分区：
文献类型：
--
作者：
Cartoni, C.;Schinina, M. E.;Agrimi, U.
细胞朊病毒蛋白（PrPC）转化为错误折叠的同种型（PrPTSE），并在受影响个体的大脑中积累，是传染性海绵状脑病（TSE）的关键特征。对TSE的易感性受朊病毒基因多态性的影响，这表明某些氨基酸残基的存在可能促进病理转化。在这项工作中，我们描述了一种定量、快速且可靠的HPLC-MS方法，该方法可以证明，在感染了小鼠适应性瘙痒症毒株139 A的109只（Met/Ile）杂合银行田鼠的大脑中，存在相当数量的PrPTSE，其中甲硫氨酸或109位的异亮氨酸，这表明在该TSE模型中，两种同种异型具有相似的积累速率。该方法可以很容易地适用于定量测定其他自然或实验TSE模型的大脑中的PrP同种异型。(c)2006 Elsevier B. V.保留所有权利。
The conversion of the cellular prion protein (PrPC) into a misfolded isoform (PrPTSE) that accumulates in the brain of affected individuals is the key feature of transmissible spongiform encephalopaties (TSEs). Susceptibility to TSEs is influenced by polymorphisms of the prion gene suggesting that the presence of certain amino acid residues may facilitate the pathological conversion. In this work, we describe a quantitative, fast and reliable HPLC-MS method that allowed to demonstrate that in the brain of 109(Met/Ile) heterozygous bank voles infected with the mouse adapted scrapie strain 139A, there are comparable amounts of PrPTSE with methionine or isoleucine in position 109, suggesting that in this TSE model the two allotypes have similar rates of accumulation. This method can be easily adapted for the quantitative determination of PrP allotypes in the brain of other natural or experimental TSE models. (c) 2006 Elsevier B.V. All rights reserved.