Tubulin nitration in human gliomas
Tubulin nitration in human gliomas
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DOI：
10.1016/j.neulet.2005.10.011
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发表时间：
2006-02-06
影响因子：
2.5
通讯作者：
d'Ischia, M
中科院分区：
文献类型：
--
作者：
Fiore, G;Di Cristo, C;d'Ischia, M
免疫组织化学和生物化学研究表明，人脑胶质瘤尤其是IV级胶质母细胞瘤在星形胶质细胞、少突胶质细胞和神经元水平上存在明显的蛋白质硝化现象。在胶质母细胞瘤中，增强的α-微管蛋白免疫反应在相同的成分中共存。用蛋白质组学方法鉴定了55 kDa的硝化蛋白条带为α-微管蛋白。多肽质量指纹图谱程序表明，在IV级肿瘤样本中，微管蛋白在Tyr224处被硝化，但在I级样本和非癌症脑组织中没有修饰。这些结果首次提供了来自人类肿瘤样本的内源性硝化微管蛋白的特征。(C)2005爱思唯尔爱尔兰有限公司。保留所有权利。
immunohistochemical and biochemical investigations showed that significant protein nitration occurs in human gliomas, especially in grade IV glioblastomas at the level of astrocytes and oligodendrocytes and neurones. Enhanced alpha-tubulin immunoreactivity was co-present in the same elements in the glioblastomas. Proteomic methodologies were employed to identify a nitrated protein band at 55 kDa as alpha-tubulin. Peptide mass fingerprinting procedures demonstrated that tubulin is nitrated at Tyr224 in grade IV tumour samples but is unmodified in grade I samples and in non-cancerous brain tissue. These results provide the first characterisation of endogenously nitrated tubulin from human tumour samples. (c) 2005 Elsevier Ireland Ltd. All rights reserved.