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J. Biol. Chem., Vol. 279, Issue 20, 21589-21597, May 14, 2004

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Rho Is Involved in Superoxide Formation during Phagocytosis of Opsonized Zymosans^*

Jun-Sub Kim, Becky A. Diebold, Jong-Il Kim, Jaebong Kim, Jae-Yong Lee, and Jae-Bong Park¶

From the Department of Biochemistry, College of Medicine, Hallym University, Chunchon, Kangwon-Do 200-702, South Korea and the Department of Immunology and Cell Biology, The Scripps Research Institute, La Jolla, California 92037

Phagocytosis is accompanied by the production of superoxide by the NADPH oxidase complex, for which GTP-bound Rac is essential. We wanted to determine whether Rho is also involved in the production of superoxide during phagocytosis. Inhibition of Rho by Tat-C3 exoenzyme (Tat-C3) blocked superoxide formation and curtailed the phagocytosis of serum- (SOZ), C3bi- (COZ), and IgG-opsonized zymosan (IOZ) particles. Tat-C3 did not affect superoxide formation in response to phorbol myristate acetate (PMA), formyl Met-Leu-Phe (fMLP), or macrophage colony-stimulating factor (M-CSF). Superoxide formation was also reduced in J774 cells transfected with a cDNA expressing dominant-negative form of RhoA (N19RhoA). However, purified prenylated recombinant RhoA did not activate NADPH oxidase in vitro, suggesting that Rho does not interact directly with NADPH oxidase. Tat-C3 inhibited the activity of RhoA, but did not affect that of Rac in vitro or in vivo. It also inhibited the phosphorylation of p47^PHOX, one of the cytosolic components of NADPH oxidase. Taken together, these results suggest that Rho plays an important role in superoxide formation during phagocytosis of SOZ, COZ, and IOZ via phosphorylation of p47^PHOX.

Received for publication, July 31, 2003 , and in revised form, January 26, 2004.

^* This study was supported by Grant 02-PJ10-PG6-AG01-0003 from the Korea Health 21 R&D Project, Ministry of Health & Welfare, Republic of Korea. 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.

The on-line version of this article (available at http://www.jbc.org) contains Supplementary Data.

^¶ To whom correspondence should be addressed: Dept. of Biochemistry, College of Medicine, Hallym University, Chunchon, Kangwon-Do 200-702, South Korea. Tel.: 82-33-248-2542; Fax: 82-33-244-8425; E-mail: jbpark{at}hallym.ac.kr.

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