Relationship between p38 mitogen-activated protein kinase and small GTPase Rac for the activation of NADPH oxidase in bovine neutrophils

Tohru Yamamori, Osamu Inanami, Hideki Sumimoto, Takashi Akasaki, Hajime Nagahata, Mikinori Kuwabara

Research output: Contribution to journalArticle

34 Citations (Scopus)

Abstract

Superoxide production by NADPH oxidase is essential for bactericidal properties of neutrophils. However, molecular mechanisms underlying the activation of this enzyme remain largely unknown. Here, using bovine neutrophils we examined the role of p38 mitogen-activated protein kinase (p38 MAPK) in the signaling pathways of the NADPH oxidase activation. Superoxide production was induced by stimulation with serum-opsonized zymosan (OZ) and attenuated by p38 MAPK inhibitor, SB203580. OZ stimulation induced the translocation of p47phox and Rac to the plasma membrane and SB203580 completely blocked the translocation of Rac, but only partially blocked that of p47phox. Furthermore, SB203580 abolished the OZ-elicited activation of Rac, which was assessed by detecting the GTP-bound form of this protein. Phosphatidylinositol 3-kinase (PI3K) inhibitors, wortmannin and LY294002, blocked not only p38 MAPK activation but also Rac activation. However, SB203580 showed no effect on the PI3K activity. These results suggested that PI3K/p38 MAPK/Rac pathway was present in the activation of NADPH oxidase in bovine neutrophils.

Original languageEnglish
Pages (from-to)1571-1578
Number of pages8
JournalBiochemical and Biophysical Research Communications
Volume293
Issue number5
DOIs
Publication statusPublished - Jan 1 2002

All Science Journal Classification (ASJC) codes

  • Biophysics
  • Biochemistry
  • Molecular Biology
  • Cell Biology

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