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In vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatography

Bart Ghesquière (UGent) , Niklaas Colaert (UGent) , Kenny Helsens (UGent) , Lien Dejager (UGent) , Caroline Vanhaute, Katleen Verleysen, Koen Kas (UGent) , Evy Timmerman (UGent) , Marc Goethals (UGent) , Claude Libert (UGent) , et al.
(2009) MOLECULAR & CELLULAR PROTEOMICS. 8(12). p.2642-2652
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Abstract
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. Molecular & Cellular Proteomics 8: 2642-2652, 2009.
Keywords
NITRIC-OXIDE, PEROXYNITRITE, NITROTYROSINE, ALZHEIMERS-DISEASE, CONTAINING PEPTIDES, APOLIPOPROTEIN-A-I, CATALYZED OXIDATION, MASS-SPECTROMETRIC CHARACTERIZATION, PROTEOMIC IDENTIFICATION, SITES

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MLA
Ghesquière, Bart, et al. “In Vitro and in Vivo Protein-Bound Tyrosine Nitration Characterized by Diagonal Chromatography.” MOLECULAR & CELLULAR PROTEOMICS, vol. 8, no. 12, 2009, pp. 2642–52, doi:10.1074/mcp.M900259-MCP200.
APA
Ghesquière, B., Colaert, N., Helsens, K., Dejager, L., Vanhaute, C., Verleysen, K., … Gevaert, K. (2009). In vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatography. MOLECULAR & CELLULAR PROTEOMICS, 8(12), 2642–2652. https://doi.org/10.1074/mcp.M900259-MCP200
Chicago author-date
Ghesquière, Bart, Niklaas Colaert, Kenny Helsens, Lien Dejager, Caroline Vanhaute, Katleen Verleysen, Koen Kas, et al. 2009. “In Vitro and in Vivo Protein-Bound Tyrosine Nitration Characterized by Diagonal Chromatography.” MOLECULAR & CELLULAR PROTEOMICS 8 (12): 2642–52. https://doi.org/10.1074/mcp.M900259-MCP200.
Chicago author-date (all authors)
Ghesquière, Bart, Niklaas Colaert, Kenny Helsens, Lien Dejager, Caroline Vanhaute, Katleen Verleysen, Koen Kas, Evy Timmerman, Marc Goethals, Claude Libert, Joël Vandekerckhove, and Kris Gevaert. 2009. “In Vitro and in Vivo Protein-Bound Tyrosine Nitration Characterized by Diagonal Chromatography.” MOLECULAR & CELLULAR PROTEOMICS 8 (12): 2642–2652. doi:10.1074/mcp.M900259-MCP200.
Vancouver
1.
Ghesquière B, Colaert N, Helsens K, Dejager L, Vanhaute C, Verleysen K, et al. In vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatography. MOLECULAR & CELLULAR PROTEOMICS. 2009;8(12):2642–52.
IEEE
[1]
B. Ghesquière et al., “In vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatography,” MOLECULAR & CELLULAR PROTEOMICS, vol. 8, no. 12, pp. 2642–2652, 2009.
@article{828083,
  abstract     = {{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. Molecular & Cellular Proteomics 8: 2642-2652, 2009.}},
  author       = {{Ghesquière, Bart and Colaert, Niklaas and Helsens, Kenny and Dejager, Lien and Vanhaute, Caroline and Verleysen, Katleen and Kas, Koen and Timmerman, Evy and Goethals, Marc and Libert, Claude and Vandekerckhove, Joël and Gevaert, Kris}},
  issn         = {{1535-9476}},
  journal      = {{MOLECULAR & CELLULAR PROTEOMICS}},
  keywords     = {{NITRIC-OXIDE,PEROXYNITRITE,NITROTYROSINE,ALZHEIMERS-DISEASE,CONTAINING PEPTIDES,APOLIPOPROTEIN-A-I,CATALYZED OXIDATION,MASS-SPECTROMETRIC CHARACTERIZATION,PROTEOMIC IDENTIFICATION,SITES}},
  language     = {{eng}},
  number       = {{12}},
  pages        = {{2642--2652}},
  title        = {{In vitro and in vivo protein-bound tyrosine nitration characterized by diagonal chromatography}},
  url          = {{http://doi.org/10.1074/mcp.M900259-MCP200}},
  volume       = {{8}},
  year         = {{2009}},
}

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