Tyrosine Nitration is a Novel Post-translational Modification Occurring on the Neural Intermediate Filament Protein Peripherin

Tedeschi, Gioacchino; Cappelletti, Graziella; Nonnis, Simona; Taverna, Francesca; Negri, Armando; Rabascio, Cristina; Ronchi, Severino

doi:10.1007/s11064-006-9244-2

Cited by 21 publications

(10 citation statements)

References 42 publications

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“…From this point of view it is very interesting to note that we found in the same peptide nitrated Tyr 197 and one (in brain) or two (in PC12 cells) residues phosphorylated at Ser or Thr suggesting that nitration does not prevent tau protein to be phosphorylated in keeping with our previous observations on peripherin [26] and with the data reported by Monteiro [38] and Di Stasi et al [39] who proposed a possible cooperation in signaling processes between nitration and phosphorylation. On the other hand, Tyr 197 is predicted to be a phosphorylation site for tyrosine kinases consistent with the data reported by Sacksteder et al [13] who found that nitration in the brain involves many tyrosine residues that are predicted to be phosphorylated.…”

Section: Discussionsupporting

confidence: 90%

“…Nitrated peaks were identified by an increase in mass of 45 (NO 2 ), 29 (NO), 13 (N) and 15 (NH 2 ) units [29][30]. To further confirm the nitration, nitrotyrosine was converted to aminotyrosine by reduction with Na 2 S 2 O 4 resulting in a single mass shift corresponding to amination of tyrosine [29,26]. In details, after in gel tryptic digestion and peptides extraction, the peptide mixture was split in two aliquots.…”

Section: Western Blot Analysismentioning

confidence: 99%

“…We found that the cytoskeleton becomes the main cellular fraction containing nitrated proteins and alpha tubulin and tau are two of the major targets for this post-translational modification [12,[23][24][25]. Moreover, very recently, we reported that nitration of tyrosines occurs in the neural intermediate filament protein peripherin and its nitration is not restricted to PC12 cells but it is also present in vivo in rat brain [26]. In the present paper it is described for the first time that tau is nitrated in vivo in normal mouse brain and one tyrosine residue is modified both in vivo and in PC12 cells.…”

Section: Introductionmentioning

confidence: 96%

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Tau is Endogenously Nitrated in Mouse Brain: Identification of a Tyrosine Residue Modified In vivo by NO

et al. 2007

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Nitration of tau protein is normally linked to neurodegeneration but, until now, no comprehensive information is available regarding tau nitration in healthy subjects. It has been previously reported that in differentiated PC12 cells, tau co-immunoprecipitated with alpha-tubulin is nitrated at tyrosine residues and that this post-translation modification doesn't impair the association of tau with the cytoskeleton. The present paper is focused on the identification of tyrosine residues endogenously modified in tau from PC12 cells and reports for the first time that tau is also nitrated in vivo in normal mouse brain and that one tyrosine is endogenously modified.

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Section: Discussionsupporting

confidence: 90%

Section: Western Blot Analysismentioning

confidence: 99%

Section: Introductionmentioning

confidence: 96%

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Tau is Endogenously Nitrated in Mouse Brain: Identification of a Tyrosine Residue Modified In vivo by NO

et al. 2007

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“…NO triggers a switch to growth arrest and neuronal differentiation [29] and it modulates neuritogenesis by regulating signaling pathways through several mechanisms [52] such as binding to heme or iron sulphur sites in regulatory proteins [53] or by modifying tyrosines in cytoskeletal proteins [37,54-56]. Unlike most other endogenous messengers that are deposited in vesicles, NO cannot be stored inside the cells, rather its signaling capacity must be controlled at the level of biosynthesis and local availability [57].…”

Section: Resultsmentioning

confidence: 99%

Nitric oxide synthase mediates PC12 differentiation induced by the surface topography of nanostructured TiO2

et al. 2013

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BackgroundSubstrate nanoscale topography influences cell proliferation and differentiation through mechanisms that are at present poorly understood. In particular the molecular mechanism through which cells 'sense’ and adapt to the substrate and activate specific intracellular signals, influencing cells survival and behavior, remains to be clarified.ResultsTo characterize these processes at the molecular level we studied the differentiation of PC12 cells on nanostructured TiO2 films obtained by supersonic cluster beam deposition.Our findings indicate that, in PC12 cells grown without Nerve Growth Factor (NGF), the roughness of nanostructured TiO2 triggers neuritogenesis by activating the expression of nitric oxide synthase (NOS) and the phospho-extracellular signal-regulated kinase 1/2 (pERK1/2) signaling. Differentiation is associated with an increase in protein nitration as observed in PC12 cells grown on flat surfaces in the presence of NGF. We demonstrate that cell differentiation and protein nitration induced by topography are not specific for PC12 cells but can be regarded as generalized effects produced by the substrate on different neuronal-like cell types, as shown by growing the human neuroblastoma SH-SY5Y cell line on nanostructured TiO2.ConclusionOur data provide the evidence that the nitric oxide (NO) signal cascade is involved in the differentiation process induced by nanotopography, adding new information on the mechanism and proteins involved in the neuritogenesis triggered by the surface properties.

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“…We recently demonstrated that some of the major cytoskeletal proteins, including actin and tubulin, are nitrated in PC12 cells (Tedeschi et al, 2005) and in vivo in rat and mouse brain (Tedeschi et al, 2007; Nonnis et al 2008) under physiological conditions.…”

Section: Resultsmentioning

confidence: 99%

Protein pattern ofXenopus laevisembryos grown in simulated microgravity

et al. 2011

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Numerous studies indicate that microgravity affects cell growth and differentiation in many living organisms, and various processes are modified when cells are placed under conditions of weightlessness. However, until now, there is no coherent explanation for these observations, and little information is available concerning the biomolecules involved. Our aim has been to investigate the protein pattern of Xenopus laevis embryos exposed to simulated microgravity during the first 6 days of development. A proteomic approach was applied to compare the protein profiles of Xenopus embryos developed in simulated microgravity and in normal conditions. Attention was focused on embryos that do not present visible malformations in order to investigate if weightlessness has effects at protein level in the absence of macroscopic alterations. The data presented strongly suggest that some of the major components of the cytoskeleton vary in such conditions. Three major findings are described for the first time: (i) the expression of important factors involved in the organization and stabilization of the cytoskeleton, such as Arp (actin-related protein) 3 and stathmin, is heavily affected by microgravity; (ii) the amount of the two major cytoskeletal proteins, actin and tubulin, do not change in such conditions; however, (iii) an increase in the tyrosine nitration of these two proteins can be detected. The data suggest that, in the absence of morphological alterations, simulated microgravity affects the intracellular movement system of cells by altering cytoskeletal proteins heavily involved in the regulation of cytoskeleton remodelling.

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Tyrosine Nitration is a Novel Post-translational Modification Occurring on the Neural Intermediate Filament Protein Peripherin

Cited by 21 publications

References 42 publications

Tau is Endogenously Nitrated in Mouse Brain: Identification of a Tyrosine Residue Modified In vivo by NO

Tau is Endogenously Nitrated in Mouse Brain: Identification of a Tyrosine Residue Modified In vivo by NO

Nitric oxide synthase mediates PC12 differentiation induced by the surface topography of nanostructured TiO2

Protein pattern ofXenopus laevisembryos grown in simulated microgravity

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