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Volume 271, Number 50, Issue of December 13, 1996 pp. 32028-32033
©1996 by The American Society for Biochemistry and Molecular Biology, Inc.

Up-Regulation of Protein Kinase C-epsilon Promotes the Expression of Cytokine-inducible Nitric Oxide Synthase in RAW 264.7 Cells

(Received for publication, April 23, 1996, and in revised form, September, 4, 1996)

María J. M. Díaz-Guerra , Oscar G. Bodelón , Marta Velasco , Richard Whelan , Peter J. Parker and Lisardo Boscá

From the Instituto de Bioquímica (Consejo Superior de Investigaciones Cientifícas), Facultad de Farmacia, Universidad Complutense, 28040 Madrid, Spain and the  Protein Phosphorylation Laboratory, Imperial Cancer Research Fund, Lincoln's Inn Fields, London WC2A 3PX, United Kingdom

Stimulation of the murine macrophage RAW 264.7 cell line with phorbol esters fails to promote nitric oxide synthesis as occurs in rat hepatocytes or peritoneal macrophages. Transfection of RAW 264.7 cells with plasmids harboring protein kinase C (PKC) -epsilon isotype but not with PKC-alpha , -beta 1, -delta , or constitutively active -alpha and -beta 1 isotypes resulted in the expression of nitric oxide synthase type II (iNOS), as reflected by the synthesis of nitric oxide measured in the culture medium of transfected cells. cotransfection of RAW 264.7 cells with the -1592 to +121-base pair promoter region of the murine iNOS gene and PKC isotypes specifically induced the transactivation of this promoter in the case of the plasmids containing the PKC-epsilon isotype. The mechanism by which PKC-epsilon induced iNOS expression involved the activation of nuclear factor binding to kappa B sites (NF-kappa B) as deduced by the suppressive effect of pyrrolidine dithiocarbamate on nitric oxide synthesis, an inhibitor of NF-kappa B activation, and by the activation of kappa B sites in cells transfected with a vector containing a kappa B motif linked to a chloramphenicol acetyltransferase reporter gene. These results suggest that PKC-epsilon can regulate a pathway that promotes iNOS expression in macrophages in response to phorbol ester activation.


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