Activation of the neutrophil NADPH oxidase is inhibited by SB 203580, a specific inhibitor of SAPK2/p38

Aroon S. Lal, Andrew D. Clifton, John Rouse, Anthony W. Segal, Philip Cohen

Research output: Contribution to journalArticle

59 Citations (Scopus)

Abstract

Activation of the neutrophil NADPH oxidase by either the bacterial peptide fMLP or phorbol myristate acetate (PMA) is partially suppressed by SB 203580, a specific inhibitor of the MAP kinase family member, SAPK2/p38. The concentration of SB 203580 that suppresses activation of NADPH oxidase is similar to that which inhibits SAPK2/p38 in vitro, and both fMLP and PMA induce an extremely rapid and potent activation of SAPK2/p38 in neutrophils. SB 203580 does not exert its effect by preventing the neutrophil priming reaction, by suppressing the phosphorylation of p47(phax), or by preventing the translocation of p47(phax)/67(phax) to the plasma membrane.

Original languageEnglish
Pages (from-to)465-470
Number of pages6
JournalBiochemical and Biophysical Research Communications
Volume259
Issue number2
DOIs
Publication statusPublished - 7 Jun 1999

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