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The Journal of Immunology, 1999, 163: 2452-2462.
Copyright © 1999 by The American Association of Immunologists

Macrophage Colony-Stimulating Factor Induces the Expression of Mitogen-Activated Protein Kinase Phosphatase-1 Through a Protein Kinase C-Dependent Pathway1

Annabel F. Valledor, Jordi Xaus, Laura Marquès and Antonio Celada2

Departament de Fisiologia (Biologia del Macròfag), Facultat de Biologia and Fundació August Pi i Sunyer, Universitat de Barcelona, Barcelona, Spain

M-CSF triggers the activation of extracellular signal-regulated protein kinases (ERK)-1/2. We show that inhibition of this pathway leads to the arrest of bone marrow macrophages at the G0/G1 phase of the cell cycle without inducing apoptosis. M-CSF induces the transient expression of mitogen-activated protein kinase phosphatase-1 (MKP-1), which correlates with the inactivation of ERK-1/2. Because the time course of ERK activation must be finely controlled to induce cell proliferation, we studied the mechanisms involved in the induction of MKP-1 by M-CSF. Activation of ERK-1/2 is not required for this event. Therefore, M-CSF activates ERK-1/2 and induces MKP-1 expression through different pathways. The use of two protein kinase C (PKC) inhibitors (GF109203X and calphostin C) revealed that M-CSF induces MKP-1 expression through a PKC-dependent pathway. We analyzed the expression of different PKC isoforms in bone marrow macrophages, and we only detected PKCßI, PKC{epsilon}, and PKC{zeta}. PKC{zeta} is not inhibited by GF109203X/calphostin C. Of the other two isoforms, PKC{epsilon} is the best candidate to mediate MKP-1 induction. Prolonged exposure to PMA slightly inhibits MKP-1 expression in response to M-CSF. In bone marrow macrophages, this treatment leads to a complete depletion of PKCßI, but only a partial down-regulation of PKC{epsilon}. Moreover, no translocation of PKCßI or PKC{zeta} from the cytosol to particulate fractions was detected in response to M-CSF, whereas PKC{epsilon} was constitutively present at the membrane and underwent significant activation in M-CSF-stimulated macrophages. In conclusion, we remark the role of PKC, probably isoform {epsilon}, in the negative control of ERK-1/2 through the induction of their specific phosphatase.




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