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Papers In Press, published online ahead of print April 29, 2005
J. Biol. Chem, 10.1074/jbc.M503512200
Submitted on March 31, 2005
Accepted on April 28, 2005

Mitochondrial respiratory chain and NAD(P)H oxidase are targets for the antiproliferative effect of carbon monoxide in human airway smooth muscle

Camille Taillé, Jamel El-Benna, Sophie Lanone, Jorge Boczkowski, and Roberto Motterlini

INSERM U700, Paris 75018

Corresponding Author: jbb2{at}bichat.inserm.fr

Carbon monoxide (CO), one of the end products of heme oxygenase activity, inhibits smooth muscle proliferation by decreasing ERK1/2 phosphorylation and cyclin D1 expression, a signaling pathway that is known to be modulated by reactive oxygen species (ROS) in airway smooth muscle cells (ASMC). Two important sources of ROS involved in cell signaling are the membrane NAD(P)H oxidase and the mitochondrial respiratory chain. Thus, that CO could modulate redox signaling in ASMC by interacting with the heme moiety of NAD(P)H oxidase and/or the respiratory chain is a plausible hypothesis. Here we show that a recently identified carbon monoxide-releasing molecule, [Ru(CO)3Cl2]2 (or CORM-2): 1) inhibits NAD(P)H oxidase cytochrome b558 activity, 2) increases oxidants production by the mitochondria; and 3) inhibits ASMC proliferation and phosphorylation of the ERK 1/2 MAP Kinase and expression of cyclin D1, two critical pathways involved in muscle proliferation. No such effects were observed with the negative control (Ru(DMSO)4Cl2), which does not contain CO groups. Since both DPI or apocynin (inhibitors of NAD(P)H oxidase) and rotenone (a molecule which increases mitochondrial ROS production by blocking the respiratory chain) mimicked the effect of CORM-2 on cyclin D1 expression and ASMC proliferation, the antiproliferative effect of CORM-2 is probably related to inhibition of cytochromes on both NAD(P)H oxidase and the respiratory chain. The involvement of increased mitochondrial-derived oxidants is substantiated by the findings showing that the antioxidant N-acetylcysteine partially inhibited the effects of CORM-2. This study provides a new mechanism to explain redox signaling by CO.


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