Article ID | Journal | Published Year | Pages | File Type |
---|---|---|---|---|
4351196 | Neuroscience Letters | 2006 | 6 Pages |
Abstract
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 55Â 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.
Keywords
ES/MSMALDI-TOFTFANOSLC/MS/MSSDS–PAGEElectrospray mass spectrometryElectrospray tandem mass spectrometryTrifluoroacetic acidsodium dodecyl sulfate–polyacrylamide gel electrophoresisImmunohistochemistrytubulinnitrotyrosinenitric oxide synthaseProteomicshigh-performance liquid chromatographyHPLCGliomas
Related Topics
Life Sciences
Neuroscience
Neuroscience (General)
Authors
Gabriella Fiore, Carlo Di Cristo, Gianluca Monti, Angela Amoresano, Laura Columbano, Pietro Pucci, Fernando A. Cioffi, Anna Di Cosmo, Anna Palumbo, Marco d'Ischia,