Journal
BIOSCIENCE BIOTECHNOLOGY AND BIOCHEMISTRY
Volume 69, Issue 11, Pages 2207-2212Publisher
TAYLOR & FRANCIS LTD
DOI: 10.1271/bbb.69.2207
Keywords
neutrophil; cell death; reactive oxygen species; NADPH oxidase; myeloperoxidase
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Stimulation of normal mouse neutrophils with phorbol 12-myristate 13-acetate resulted in an acceleration of chromatin condensation and phosphatidylserine externalization that was not associated with caspase-3 activation. Caspase-independent death was completely inhibited by GF109203X and SB202190, specific inhibitors for protein kinase C and p38 mitogen-activated protein kinase respectively. Activation of p38 mitogenactivated protein kinase was completely suppressed by GF109203X, indicating that this enzyme is regulated by protein kinase C. On the other hand, cell death was abolished in NADPH oxidase-deficient neutrophils lacking superoxide production. Of note, p38 mitogenactivated protein kinase was activated by phorbol 12-myristate 13-acetate in normal and myeloperoxidase-deficient neutrophils lacking production of HOCI, whereas no activation was observed in NADPH oxidase-deficient neutrophils. These results strongly suggest that activation of p38 mitogen-activated protein kinase is regulated by endogenously generated superoxide or its metabolites other than HOCI, a critical regulator of inducer-stimulated death of neutrophils.
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