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J. Biol. Chem., Vol. 280, Issue 48, 40310-40318, December 2, 2005

This Article Full Text Full Text (PDF) All Versions of this Article: 280/48/40310    most recent M503644200v1 Submit a Letter to Editor Alert me when this article is cited Alert me when eLetters are posted Alert me if a correction is posted Citation Map Services Email this article to a friend Similar articles in this journal Similar articles in PubMed Alert me to new issues of the journal Download to citation manager Request Permissions Citing Articles Citing Articles via HighWire Citing Articles via Google Scholar Google Scholar Articles by Billiet, L. Articles by Rouis, M. Search for Related Content PubMed PubMed Citation Articles by Billiet, L. Articles by Rouis, M. Social Bookmarking                      What's this?

Extracellular Human Thioredoxin-1 Inhibits Lipopolysaccharide-induced Interleukin-1 Expression in Human Monocyte-derived Macrophages^*

Ludivine Billiet, Christophe Furman, Guilhem Larigauderie, Corinne Copin, Korbinian Brand, Jean-Charles Fruchart, and Mustapha Rouis1

From the U-545 INSERM, Institut Pasteur de Lille and Université Lille 2, 59019 Lille, France and the Institute of Clinical Chemistry and Pathobiochemistry Klinikum rechts der Isar, Technische Universität München, Ismaninger Strasse 22, 81675 München, Germany

Oxidative stress plays an important role in atherosclerotic vascular disease, and several recent studies were focused on thioredoxin-1 (Trx-1) and its potential protective role against oxidative stress. Since human monocyte-derived macrophages (HMDM) are important cells in several inflammatory diseases including atherosclerosis, we conducted this study to evaluate the impact of extracellular recombinant human Trx-1 (rhTrx-1) on gene expression in lipopolysaccharide-activated HMDM. Our results showed that rhTrx-1 was capable of reducing interleukin (IL)-1 mRNA and protein synthesis in a dose-dependent manner. This effect was partly mediated through a reduction of NF-B activation as analyzed by transient transfection and gel shift assays. In addition, we showed that the attenuation of NF-B activity was the result of the reduction of both p50 and p65 subunit mRNA and protein synthesis on one hand and of the induction of I-B mRNA and protein expression on the other hand. Moreover, inhibition of endogenous Trx-1 mRNA was also observed, suggesting a contribution to the diminution of NF-B activity since endogenous Trx-1, in contrast to the exogenous Trx-1, activates the NF-B system. Finally, H₂O₂-oxidized rhTrx-1 reduced IL-1 mRNA synthesis in lipopolysaccharide-activated HMDM. This result highly suggested that the rhTrx-1 used in this study could be oxidized in the culture medium and, in turn, reduced IL-1 mRNA and protein synthesis. Taken together, these data indicated a potential new mechanism through which extracellular rhTrx-1 exerts an anti-inflammatory function in HMDM.

Received for publication, April 4, 2005 , and in revised form, October 3, 2005.

^* This work was supported by grants from Fondation Leducq (to C. F. and G. L.) and Contrat d'interface INSERM-CHRU Lille (to M. R.). The costs of publication of this article were defrayed in part by the payment of page charges. This article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

¹ To whom correspondence should be addressed: INSERM U545, Dept. of Atherosclerosis, Pasteur Institute of Lille, 1 rue du Professeur Calmette, 59019 Lille, France. Tel.: 33-3-20-87-73-79; Fax: 33-3-20-87-73-60; E-mail: mustapha.rouis{at}pasteur-lille.fr.

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