Tubulin nitration in human gliomas

被引：21

作者：

Fiore, G

Di Cristo, C

Monti, G

Amoresano, A

Columbano, L

Pucci, P

Cioffi, FA

Di Cosmo, A

Palumbo, A

d'Ischia, M

机构：

[1] Staz Zool Anton Dohrn, Biochem & Mol Biol Lab, I-80121 Naples, Italy

[2] Univ Sannio, Dept Biol & Environm Sci, I-82100 Benevento, Italy

[3] Univ Naples Federico 2, Dept Organ Chem & Biochem, I-80126 Naples, Italy

[4] Univ Naples 2, Dept Neurosurg, I-80131 Naples, Italy

来源：

NEUROSCIENCE LETTERS | 2006年 / 394卷 / 01期

关键词：

gliomas; nitrotyrosine; immunohistochemistry; proteomics; tubulin;

D O I：

10.1016/j.neulet.2005.10.011

中图分类号：

Q189 [神经科学];

学科分类号：

071006 ;

摘要：

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.

引用

页码：57 / 62

页数：6

共 22 条

[1] Incorporation of 3-nitrotyrosine into the C-terminus of α-tubulin is reversible and not detrimental to dividing cells [J].