Upregulation of 3-MST Relates to Neuronal Autophagy After Traumatic Brain Injury in Mice
Upregulation of 3-MST Relates to Neuronal Autophagy After Traumatic Brain Injury in Mice
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DOI：
10.1007/s10571-016-0369-9
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发表时间：
2017-03
影响因子：
4
通讯作者：
Mingyang Zhang;H. Shan;P. Chang;Lu Ma;Y. Chu;Xi Shen;Qiong Wu;Zufeng Wang;Chengliang Luo;Tao Wang;Xi-ping Chen;L. Tao
中科院分区：
文献类型：
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作者：
Mingyang Zhang;H. Shan;P. Chang;Lu Ma;Y. Chu;Xi Shen;Qiong Wu;Zufeng Wang;Chengliang Luo;Tao Wang;Xi-ping Chen;L. Tao
3-巯基丙酮酸硫转移酶（3-MST）是一种新的硫化氢（H2S）合成酶，可能参与氰化物的降解和硫代硫酸盐的生物合成。近年来，硫化氢合成酶的生物化学和分子生物学研究受到了广泛关注。与此相反，已经有一些协调一致的尝试，以调查的H2S合成酶的表达与疾病状态的变化。为探讨3-MST在创伤性脑损伤（TBI）后的变化及其可能的作用，本研究采用可控皮质撞击系统建立小鼠TBI模型，观察3-MST在TBI后的表达及细胞定位。Western blot分析表明3-MST存在于正常小鼠大脑皮层。TBI后第1天达高峰，第3天降至低谷。重要的是，3-MST与神经元共定位。此外，Western blot检测显示，损伤后第一天也是自噬高峰，表明LC 3的表达升高。重要的是，免疫组化分析显示，损伤诱导的3-MST表达部分由LC 3共同标记。然而，3-MST与碘化丙啶（细胞死亡标志物）没有共定位，LC 3阳性细胞与碘化丙啶部分共定位。提示3-MST主要定位于存活神经元中，可能参与了脑损伤后神经元的自噬，并参与了脑损伤后的病理生理过程。
3-mercaptopyruvate sulfurtransferase (3-MST) was a novel hydrogen sulfide (H2S)-synthesizing enzyme that may be involved in cyanide degradation and in thiosulfate biosynthesis. Over recent years, considerable attention has been focused on the biochemistry and molecular biology of H2S-synthesizing enzyme. In contrast, there have been few concerted attempts to investigate the changes in the expression of the H2S-synthesizing enzymes with disease states. To investigate the changes of 3-MST after traumatic brain injury (TBI) and its possible role, mice TBI model was established by controlled cortical impact system, and the expression and cellular localization of 3-MST after TBI was investigated in the present study. Western blot analysis revealed that 3-MST was present in normal mice brain cortex. It gradually increased, reached a peak on the first day after TBI, and then reached a valley on the third day. Importantly, 3-MST was colocalized with neuron. In addition, Western blot detection showed that the first day post injury was also the autophagic peak indicated by the elevated expression of LC3. Importantly, immunohistochemistry analysis revealed that injury-induced expression of 3-MST was partly colabeled by LC3. However, there was no colocalization of 3-MST with propidium iodide (cell death marker) and LC3 positive cells were partly colocalized with propidium iodide. These data suggested that 3-MST was mainly located in living neurons and may be implicated in the autophagy of neuron and involved in the pathophysiology of brain after TBI.