Tubulin nitration in human gliomas

Fiore, Gabriella; Cristo, Carlo Di; Monti, Gianluca; Amoresano, Angela; Columbano, Laura; Pucci, Piero; Cioffi, F. A.; Cosmo, Anna Di; Palumbo, Anna; d’Ischia, Marco

doi:10.1016/j.neulet.2005.10.011

Cited by 24 publications

(13 citation statements)

References 19 publications

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“…2, lane 7) demonstrates that this unidentified protein can be selectively nitrated. Similar selective nitration has been reported previously for p130(cas) (130 kDa) from human neuroblastoma SH-SY5Y cells (Saeki and Maeda, 1999), alpha-tubulin (50-55 kDa) from human gliomas and rat brain (Dremina et al, 2005;Fiore et al, 2006), alpha-actinin (100 kDa) from human myocardium (Borbely et al, 2005), and prostaglandin endoperoxide synthase-2 (72 kDa) from RAW 264.7 macrophages (Schildknecht et al, 2006). Yet, although our data indicate that selective nitration by peroxynitrite targets one protein product also in honey bee brain, the cumulative data from the immunohistochemical (Fig.…”

Section: Resultssupporting

confidence: 84%

Cellular senescence in honey bee brain is largely independent of chronological age

Seehuus

Krekling

Amdam

2006

Experimental Gerontology

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Accumulation of oxidative stress-induced damage in brain tissue plays an important role in the pathogenesis of normal aging and neurodegenerative diseases. Neuronal oxidative damage typically increases with age in humans, and also in the invertebrate and vertebrate model species most commonly used in aging research. By use of quantitative immunohistochemistry and Western blot, we show that this aspect of brain senescence is largely decoupled from chronological age in the honey bee (Apis mellifera). The bee is a eusocial insect characterized by the presence of a reproductive queen caste and a caste of functionally sterile female workers that performs various alloparental tasks such as nursing and foraging. We studied patterns of oxidative nitration and carbonylation damage in the brain of worker bees that performed nurse tasks as 8-and 200-day-olds and foraging tasks as 20-and 200-day-olds. In addition, we examined 180-day-old diutinus bees, a stress-resistant temporal worker form that survives unfavorable periods. Our results indicate that nitration damage occurs only at low levels in vivo, but that a 60-kDa protein from honey bee brain is selectively nitrated by peroxynitrite in vitro. Oxidative carbonylation is present at varying levels in the visual and chemosensory neuropiles of worker bees, and this inter-individual variation is better explained by social role than by chronological age.

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Section: Resultssupporting

confidence: 84%

Cellular senescence in honey bee brain is largely independent of chronological age

Seehuus

Krekling

Amdam

2006

Experimental Gerontology

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“…Both tyrosines were found by Tedeschi et al (36) to play an important role during nerve growth factorinduced neuronal differentiation. In addition, nitration of Tyr 224 found here was previously described by Fiore et al (37), specifically during grade IV human glioma. Haqqani et al (38) reported histone nitration, and we confirmed Tyr 72 of histone H4 and Tyr 43 of histone H2B as nitration spots upon in vitro peroxynitrite treatment.…”

Section: Fig 1 Reduction Of 3-nitrotyrosine To 3-aminotyrosine Caussupporting

confidence: 84%

In Vitro and in Vivo Protein-bound Tyrosine Nitration Characterized by Diagonal Chromatography

Ghesquière

Colaert

Helsens

et al. 2009

Molecular & Cellular Proteomics

102

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A new proteomics technique for analyzing 3-nitrotyrosine-containing peptides is presented here. This technique is based on the combined fractional diagonal chromatography peptide isolation procedures by which specific classes of peptides are isolated following a series of identical reverse-phase HPLC separation steps. Here dithionite is used to reduce 3-nitrotyrosine to 3-aminotyrosine peptides, which thereby become more hydrophilic. Our combined fractional diagonal chromatography technique was first applied to characterize tyrosine nitration in tetranitromethane-modified BSA and further led to a high quality list of 335 tyrosine nitration sites in 267 proteins in a peroxynitrite-treated lysate of human Jurkat cells. We then analyzed a serum sample of a C57BL6/J mouse in which septic shock was induced by intravenous Salmonella infection and identified six in vivo nitration events in four serum proteins, thereby illustrating that our technique is sufficiently sensitive to identify rare in vivo tyrosine nitration sites in a very complex background.

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“…Other important targets of NO toxicity are microtubules, because tubulin is highly susceptible to nitration on tyrosine residues (Dremina et al, 2005;Eiserich et al, 1999;Fiore et al, 2006). We investigated by fluorescent microscopy the possible effect of BSO treatment on microtubule lattices.…”

Section: Bso-mediated Cell Growth Arrest Results In Cell Death and Ismentioning

confidence: 99%

Nitric oxide is the primary mediator of cytotoxicity induced by GSH depletion in neuronal cells

Aquilano

Baldelli

Cardaci

et al. 2011

Journal of Cell Science

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Glutathione (GSH) levels progressively decline during aging and in neurodegenerative disorders. However, the contribution of such event in mediating neuronal cell death is still uncertain. In this report, we show that, in neuroblastoma cells as well as in primary mouse cortical neurons, GSH decrease, induced by buthionine sulfoximine (BSO), causes protein nitration, S-nitrosylation and DNA strand breaks. Such alterations are also associated with inhibition of cytochrome c oxidase activity and microtubule network disassembly, which are considered hallmarks of nitric oxide (NO) toxicity. In neuroblastoma cells, BSO treatment also induces cell proliferation arrest through the ERK1/2-p53 pathway that finally results in caspase-independent apoptosis, as evident from the translocation of apoptosis-inducing factor from mitochondria towards nuclei. A deeper analysis of the signaling processes indicates that the NO-cGMP pathway is involved in cell proliferation arrest and death. In fact, these events are completely reversed by L-NAME, a specific NO synthase inhibitor, indicating that NO, rather than the depletion of GSH per se, is the primary mediator of cell damage. In addition, the guanylate cyclase (GC) inhibitor LY83583 is able to completely block activation of ERK1/2 and counteract BSO toxicity. In cortical neurons, NMDA (N-methyl-D-aspartic acid) treatment results in GSH decrease and BSO-mediated NO cytotoxicity is enhanced by either epidermal growth factor (EGF) or NMDA. These findings support the idea that GSH might represent the most important buffer of NO toxicity in neuronal cells, and indicate that the disruption of cellular redox buffering controlled by GSH makes neuronal cells susceptible to endogenous physiological flux of NO.

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Tubulin nitration in human gliomas

Cited by 24 publications

References 19 publications

Cellular senescence in honey bee brain is largely independent of chronological age

Cellular senescence in honey bee brain is largely independent of chronological age

In Vitro and in Vivo Protein-bound Tyrosine Nitration Characterized by Diagonal Chromatography

Nitric oxide is the primary mediator of cytotoxicity induced by GSH depletion in neuronal cells

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