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Autoimmunity Volume 42, 2009 - Issue 4
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Brief Definite Report

Oxidation of the alarmin high-mobility group box 1 protein (HMGB1) during apoptosis

Brief Definite Report

Vilma Urbonaviciute IZKF, Research Group N2, Nikolaus Fiebiger Center of Molecular Medicine, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany
,
Silke Meister IZKF, Research Group N2, Nikolaus Fiebiger Center of Molecular Medicine, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany
,
Barbara G. Fürnrohr IZKF, Research Group N2, Nikolaus Fiebiger Center of Molecular Medicine, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany
,
Benjamin Frey Department of Radiation Oncology, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany
,
Eva Gückel IZKF, Research Group N2, Nikolaus Fiebiger Center of Molecular Medicine, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany
,
Georg Schett Department of Internal Medicine 3, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany
,
Martin Herrmann Department of Internal Medicine 3, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany
&
Reinhard E. Voll IZKF, Research Group N2, Nikolaus Fiebiger Center of Molecular Medicine, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, Germany; Department of Internal Medicine 3, University Hospital Erlangen, University of Erlangen-Nuremberg, Erlangen, GermanyCorrespondence[email protected]
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Pages 305-307 | Received 11 Dec 2008, Accepted 07 Jan 2009, Published online: 13 Aug 2009
 
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Abstract

The architectural chromosomal protein high-mobility group box 1 protein (HMGB1) acts as an alarmin when released from cells. It is involved in the pathogenesis of inflammatory and autoimmune diseases. HMGB1 can undergo post-translational modifications including oxidation. However, the mechanisms and functional relevance of HMGB1 oxidation are not yet understood. Increased concentrations of reactive oxygen species (ROS) have been reported during apoptosis and necrosis. Hence, we investigated the oxidative status of HMGB1 in dead cells. Immunoblot analyses under reducing and non-reducing conditions revealed that HMGB1 is oxidized in dead cells. Moreover, tagging of oxidized cysteine residues by a maleimide moiety linked to polyethylene glycol showed that HMGB1 passively released from primary and secondary necrotic cells was predominantly oxidized. Also HMGB1 in plasma of patients with systemic lupus was reversibly oxidized. In conclusion, HMGB1 undergoes reversible oxidative modifications at cysteine residues during cell death, which may modulate its biological properties.

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