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2, Shc Adapter Protein, and p38 Mitogen-Activated Protein Kinase1
Department of Medical Microbiology, Linköping University, Linköping, Sweden
Recent studies have shown that human neutrophils play a significant
protective role in mycobacteria infection. When encountered with
mycobacteria, neutrophils exhibit the typical early bactericidal
responses including phagocytosis and generation of reactive oxygen
intermediates (ROI), but the underlying mechanisms are largely unknown.
The present study shows that stimulation of neutrophils with an
attenuated strain of Mycobacterium tuberculosis H37Ra
(Mtb) led to a tyrosine kinase-dependent ROI production in these cells.
Stimulation with Mtb induces a rapid and transient tyrosine
phosphorylation of several proteins, one of which was identified as
phospholipase C
2 (PLC2). Several tyrosine-phosphorylated proteins
were associated with the PLC2 precipitates from Mtb-stimulated
neutrophils, of which pp46 was characterized as the Shc adapter
protein. A role for PLC2-Shc association in the generation of ROI is
supported by the observations that stimulation with Mtb causes the
activation of p38 mitogen-activated protein kinase (MAPK), a downstream
target of the Shc/Ras signaling cascade, and that the effect of
genistein on ROI production coincided with its ability to inhibit both
PLC2-Shc association and p38 MAPK activation. Moreover, pretreatment
of neutrophils with a PLC inhibitor markedly suppresses the
Mtb-stimulated ROI production as well as p38 MAPK activation in these
cells. Taken together, these results indicate that stimulation of
neutrophils with Mtb triggers the tyrosine phosphorylation of PLC2
and its association with Shc, and that such association is critical for
the Mtb-stimulated ROI production through activating p38
MAPK.
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