We have found recently that dendritic spine extension is inhibited through acrolein conjugation with α‐ and β‐tubulin proteins during brain infarction. In this current study, we looked for other acrolein‐conjugated proteins in the 100,000g precipitate fraction, to clarify how cytoskeleton structure is modified by acrolein. Acrolein‐conjugated proteins were sought from acrolein‐treated mouse FM3A and Neuro2a cells and from tissues isolated from mouse brain infarction. It was found that vimentin was conjugated with acrolein, and the conjugated amino acid residue was Cys328, which is the only Cys residue in vimentin. It was also found that Cys207, 257, 285, and Lys118 in actin, another cytoskeleton protein, were conjugated with acrolein. The structure and localization of vimentin and actin filaments were changed greatly in infarct brain in photochemically induced thrombosis model mice and in acrolein‐treated Neuro2a cells. In addition, degradation of cytoskeleton proteins was accelerated in the order vimentin > tubulin > actin in mouse brain infarction. These findings indicate that a dysfunction of the cytoskeleton by acrolein is strongly involved in the tissue damage during brain infarction, together with the apoptosis caused by glyceraldehyde‐3‐phosphate dehydrogenase and protein degradation by matrix metalloproteinase‐9.

中文翻译：

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脑梗塞期间丙烯醛与波形蛋白和肌动蛋白结合导致细胞骨架的结构变化和降解

我们最近发现，在脑梗塞期间，通过丙烯醛与 α- 和 β- 微管蛋白结合，树突棘延伸受到抑制。在当前的这项研究中，我们寻找了 100,000 g中的其他丙烯醛结合蛋白沉淀部分，以阐明细胞骨架结构如何被丙烯醛修饰。从丙烯醛处理的小鼠 FM3A 和 Neuro2a 细胞以及从小鼠脑梗塞中分离的组织中寻找丙烯醛结合蛋白。发现波形蛋白与丙烯醛偶联，偶联的氨基酸残基为Cys328，是波形蛋白中唯一的Cys残基。还发现肌动蛋白（另一种细胞骨架蛋白）中的 Cys207、257、285 和 Lys118 与丙烯醛结合。在光化学诱导的血栓形成模型小鼠和丙烯醛处理的 Neuro2a 细胞的梗死脑中，波形蛋白和肌动蛋白丝的结构和定位发生了很大变化。此外，在小鼠脑梗塞中，细胞骨架蛋白的降解以波形蛋白 > 微管蛋白 > 肌动蛋白的顺序加速。