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(Journal of Leukocyte Biology. 2003;73:281-288.)
© 2003 by Society for Leukocyte Biology

M-CSF induced differentiation of myeloid precursor cells involves activation of PKC- and expression of Pkare

Ilkka Junttila^*, Roland P. Bourette, Larry R. Rohrschneider and Olli Silvennoinen^*,

^* Laboratory of Molecular Immunology, Institute of Medical Technology, and
Department of Clinical Microbiology, Tampere University Hospital, University of Tampere, Finland;
Centre de Génetique Moléculaire et Cellulaire, Université Claude Bernard Lyon 1, Villeurbanne Cedex, France; and
Fred Hutchinson Cancer Research Center, Division of Basic Sciences, Seattle, Washington

Correspondence: Dr. Olli Silvennoinen, Institute of Medical Technology, University of Tampere Lenkkeilijänkatu 8, 33014 Tampere, Finland. E-mail: olli.silvennoinen{at}uta.fi

Macrophage-colony stimulating factor (M-CSF) regulates proliferation and differentiation of cells belonging to the monocytic lineage. We investigated the mechanisms of M-CSF differentiation signaling in follicular dendritic cell-P1 cells and analyzed the catalytic activation of different protein kinase C (PKC) isoforms. M-CSF induced rapid catalytic activation of PKC- and membrane translocation of the tyrosine phosphorylated form of PKC-. Mutation of tyrosine 807 in the M-CSF receptor (Fms) abrogates cell differentiation but not a proliferative response to M-CSF, and FmsY807F failed to activate PKC-. We also investigated the downstream signaling pathways from PKC-. A cyclic adenosine monophosphate-regulated Ser/Thr kinase gene, protein kinase X (PRKX), has been associated with macrophage differentiation in human cells. We found that M-CSF and PKC- induced the expression of the PRKX murine homologue: PKA-related gene. Taken together, our results indicate that PKC- functions as a critical mediator of M-CSF-induced differentiation signaling.

Key Words: signal transduction • tyrosine phosphorylation • ser/thr kinase

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