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In human polymorphonuclear leukocytes (PMNs), mitogen-activated
protein kinases (MAPKs), also known as extracellular signal-regulated
kinases (Erks), are activated within minutes upon stimulation with
either chemoattractant formyl-Met-Leu-Phe (fMLP) or phorbol
12-myristate 13-acetate (PMA). This activation of MAPKs coincides with
the formation of superoxide anion, which occurs through the activation
of a multiple-component NADPH oxidase pathway. MAPKs have thus been
suggested to be involved in signal transduction leading to the
oxidative burst. To investigate whether MAPK activation plays a central
role in the oxidative burst, we evaluated the effect of cAMP on MAPK
activation induced by fMLP and PMA. cAMP inhibits many PMN functional
responses, including the oxidative burst, and has recently been shown
to reduce growth factor- and PMA-induced MAPK activities in a variety
of cells. We found that in differentiated, neutrophil-like HL-60 cells,
while cAMP reduced PMA-induced MAPK activation, it had no effect on
fMLP-induced MAPK activation. Despite the presence of unchanged levels
of activated MAPKs, the fMLP-induced oxidative burst was substantially
diminished by cAMP. By contrast, O
Volume 270,
Number 26,
Issue of June 30, pp. 15719-15724, 1995
©1995 by The American Society for Biochemistry and Molecular Biology, Inc.
production induced by PMA remained the same even though MAPK
activation was inhibited. In PMNs, although the levels of
O
induced by either 10 ng/ml or 100 ng/ml
PMA were similar, only 100 ng/ml could stimulate MAPK activation,
suggesting that the oxidative burst could occur in the absence of
detectable activation of MAPKs. As in HL-60 cells, cAMP inhibited the
O
production in fMLP-stimulated PMNs but
had no effect on MAPK activity. These results demonstrate that, while
MAPK activation coincides with PMN activation, it can be dissociated
from the oxidative burst.
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