We have previously shown that TNF (tumour necrosis factor) induces phosphorylation of GLO1 (glyoxalase I), which is required for cell death in L929 cells. In the present paper, we show that the TNF-induced phosphorylation of GLO1 occurs primarily on the NO (nitric oxide)-responsive form of GLO1. In addition, analysis of several cysteine mutants of GLO1 indicated that Cys-138, in combination with either Cys-18 or Cys-19, is a crucial target residue for the NO-mediated modification of GLO1. Furthermore, the NO-donor GSNO (S-nitrosogluthathione) induces NO-mediated modification of GLO1 and enhances the TNF-induced phosphorylation of this NO-responsive form. GSNO also strongly promotes TNF-induced cell death. By the use of pharmacological inhibition of iNOS (inducible NO synthase) and overexpression of mutants of GLO1 that are deficient for the NO-mediated modification, we have shown that the NO-mediated modification of GLO1 is not a requirement for TNF-induced phosphorylation or TNF-induced cell death respectively. In summary, these data suggest that the TNF-induced phosphorylation of GLO1 is the dominant factor for cell death.
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Research Article|
September 12 2007
Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I
Virginie de Hemptinne;
Virginie de Hemptinne
1
*Department of Medical Protein Research, Molecular and Metabolic Signaling Unit, VIB, 9000 Ghent, Belgium
†Department of Biochemistry and Molecular Biology, Faculty of Medicine and Health Sciences, University of Ghent, Albert Baertsoenkaai 3, 9000 Ghent, Belgium
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Dieter Rondas;
Dieter Rondas
1
*Department of Medical Protein Research, Molecular and Metabolic Signaling Unit, VIB, 9000 Ghent, Belgium
†Department of Biochemistry and Molecular Biology, Faculty of Medicine and Health Sciences, University of Ghent, Albert Baertsoenkaai 3, 9000 Ghent, Belgium
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Joël Vandekerckhove;
Joël Vandekerckhove
*Department of Medical Protein Research, Molecular and Metabolic Signaling Unit, VIB, 9000 Ghent, Belgium
†Department of Biochemistry and Molecular Biology, Faculty of Medicine and Health Sciences, University of Ghent, Albert Baertsoenkaai 3, 9000 Ghent, Belgium
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Katia Vancompernolle
Katia Vancompernolle
2
*Department of Medical Protein Research, Molecular and Metabolic Signaling Unit, VIB, 9000 Ghent, Belgium
†Department of Biochemistry and Molecular Biology, Faculty of Medicine and Health Sciences, University of Ghent, Albert Baertsoenkaai 3, 9000 Ghent, Belgium
2To whom correspondence should be addressed (email katia.vancompernolle@UGent.be).
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Publisher: Portland Press Ltd
Received:
March 19 2007
Revision Received:
June 12 2007
Accepted:
June 19 2007
Accepted Manuscript online:
June 19 2007
Online ISSN: 1470-8728
Print ISSN: 0264-6021
© The Authors Journal compilation © 2007 Biochemical Society
2007
Biochem J (2007) 407 (1): 121–128.
Article history
Received:
March 19 2007
Revision Received:
June 12 2007
Accepted:
June 19 2007
Accepted Manuscript online:
June 19 2007
Citation
Virginie de Hemptinne, Dieter Rondas, Joël Vandekerckhove, Katia Vancompernolle; Tumour necrosis factor induces phosphorylation primarily of the nitric-oxide-responsive form of glyoxalase I. Biochem J 1 October 2007; 407 (1): 121–128. doi: https://doi.org/10.1042/BJ20070379
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