Immunohistochem. and biochem. investigations showed that significant protein nitration occurs in human gliomas, esp. in grade IV glioblastomas at the level of astrocytes and oligodendrocytes and neurons. 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 tumor samples but is unmodified in grade I samples and in non-cancerous brain tissue. These results provide the first characterization of endogenously nitrated tubulin from human tumor samples.
Tubulin nitration in human gliomas / Fiore, G.; DI CRISTO, C.; Monti, G.; Amoresano, Angela; Columbano, L.; Pucci, Pietro; Cioffi, F. A.; DI COSMO, Anna; Palumbo, A.; D'Ischia, Marco. - In: NEUROSCIENCE LETTERS. - ISSN 0304-3940. - STAMPA. - 394:1(2006), pp. 57-62. [10.1016/j.neulet.2005.10.011]
Tubulin nitration in human gliomas
AMORESANO, ANGELA;PUCCI, PIETRO;DI COSMO, ANNA;D'ISCHIA, MARCO
2006
Abstract
Immunohistochem. and biochem. investigations showed that significant protein nitration occurs in human gliomas, esp. in grade IV glioblastomas at the level of astrocytes and oligodendrocytes and neurons. 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 tumor samples but is unmodified in grade I samples and in non-cancerous brain tissue. These results provide the first characterization of endogenously nitrated tubulin from human tumor samples.File | Dimensione | Formato | |
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