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J. Biol. Chem., Vol. 279, Issue 27, 28681-28688, July 2, 2004
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¶
From the
INSERM, Unité 408 and Unité 479, Institut Fédératif de Recherche 02, Faculté de Médecine Xavier Bichat, 75018 Paris, France
Heme-oxygenase-1 (HO-1), the rate-limiting enzyme of heme degradation, has powerful anti-oxidant properties related to the production of the reactive oxygen species scavenger bilirubin. However, some data suggest that HO-1 could also inhibit the cellular production of reactive oxygen species. Therefore, we investigated whether the anti-oxidant properties of HO-1 could be mediated by modulation of the activity and/or expression of the heme-containing NAD(P)H oxidase, the main source of the superoxide anion (
) in phagocytic cells. Increasing HO-1 expression in RAW 264.7 macrophages effectively decreased NAD(P)H oxidase activity and expression of gp91phox, its heme-containing catalytic component, because of deficient protein maturation and increased degradation. Loading cells with heme reversed the decrease in production and gp91phox expression induced by HO-1 overexpression. Similar results were obtained in vivo in rat alveolar macrophages after pharmacological modulation of HO-1 expression or activity. These results show that a decrease in heme content due to HO-1 activation limits heme availability for maturation of the gp91phox subunit and assembly of the functional NAD(P)H oxidase. This study provides a new mechanism to explain HO-1 anti-oxidant properties.
Received for publication, September 26, 2003 , and in revised form, March 3, 2004.
* 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.
¶ To whom correspondence should be addressed: INSERM, U408, Faculté X. Bichat, BP416, 75870 Paris Cedex 18, France. Tel.: 33-1-44856251; Fax: 33-1-42263330; E-mail: jbb2{at}bichat.inserm.fr.
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