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, Jae Bong Park

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Abstract

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 p47PHOX, 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 p47PHOX.

Original languageEnglish
Pages (from-to)21589-21597
Number of pages9
JournalJournal of Biological Chemistry
Volume279
Issue number20
DOIs
StatePublished - 14 May 2004

Fingerprint

Zymosan
Phagocytosis
Superoxides
NADPH Oxidase
Phosphorylation
Immunoglobulin G
methionyl-leucyl-phenylalanine
Complement C3b
Macrophage Colony-Stimulating Factor
Tetradecanoylphorbol Acetate
Guanosine Triphosphate
Complementary DNA
Serum

Cite this

Kim, Jun Sub ; Diebold, Becky A. ; Kim, Jong-Il ; Kim, Jaebong ; Lee, Jae Yong ; Park, Jae Bong. / Rho is involved in superoxide formation during phagocytosis of opsonized zymosans. In: Journal of Biological Chemistry. 2004 ; Vol. 279, No. 20. pp. 21589-21597.
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abstract = "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 p47PHOX, 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 p47PHOX.",
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Rho is involved in superoxide formation during phagocytosis of opsonized zymosans. / Kim, Jun Sub; Diebold, Becky A.; Kim, Jong-Il; Kim, Jaebong; Lee, Jae Yong; Park, Jae Bong.

In: Journal of Biological Chemistry, Vol. 279, No. 20, 14.05.2004, p. 21589-21597.

Research output: Contribution to journalArticleResearchpeer-review

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AB - 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 p47PHOX, 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 p47PHOX.

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