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Is Required for the Induction of Mitogen-Activated Protein Kinase Phosphatase-1 in Lipopolysaccharide-Stimulated Macrophages1
Departament de Fisiologia (Biologia del Macròfag), Facultat de Biologia and Fundació August Pi i Sunyer, Campus Bellvitge, Universitat de Barcelona, Barcelona, Spain
LPS induces in bone marrow macrophages the transient expression of
mitogen-activated protein kinase (MAPK) phosphatase-1 (MKP-1). Because
MKP-1 plays a crucial role in the attenuation of different MAPK
cascades, we were interested in the characterization of the signaling
mechanisms involved in the control of MKP-1 expression in
LPS-stimulated macrophages. The induction of MKP-1 was blocked by
genistein, a tyrosine kinase inhibitor, and by two different protein
kinase C (PKC) inhibitors (GF109203X and calphostin C). We had
previously shown that bone marrow macrophages express the isoforms
PKCßI, 
, and 
. Of all these, only PKCßI and are inhibited
by GF109203X. The following arguments suggest that PKC is required
selectively for the induction of MKP-1 by LPS. First, in macrophages
exposed to prolonged treatment with PMA, MKP-1 induction by LPS
correlates with the levels of expression of PKC but not with that of
PKCßI. Second, Gö6976, an inhibitor selective for conventional
PKCs, including PKCßI, does not alter MKP-1 induction by LPS. Last,
antisense oligonucleotides that block the expression of PKC, but not
those selective for PKCßI or PKC, inhibit MKP-1 induction and lead
to an increase of extracellular-signal regulated kinase activity during
the macrophage response to LPS. Finally, in macrophages stimulated with
LPS we observed significant activation of PKC. In conclusion, our
results demonstrate an important role for PKC in the induction of
MKP-1 and the subsequent negative control of MAPK activity in
macrophages.
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