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J. Biol. Chem., Vol. 278, Issue 9, 6976-6984, February 28, 2003
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From the We recently demonstrated that thrombin induces
the expression of vascular adhesion molecule-1 (VCAM-1) in endothelial
cells by an NF-
Thrombin Stimulation of Vascular Adhesion Molecule-1 in
Endothelial Cells Is Mediated by Protein Kinase C (PKC)-
-NF-
B
and PKC-
-GATA Signaling Pathways*
§,,,
Department of Molecular Medicine, Beth
Israel Deaconess Medical Center, Harvard Medical School, Boston,
Massachusetts 02215, the § Laboratory for Systems Biology
and Medicine at Research Center for Advanced Science and
Technology, the University of Tokyo, Tokyo 153-8904, Japan, and
the ¶ Joslin Diabetes Center, Harvard Medical School, Boston,
Massachusetts 02215
B- and GATA-dependent mechanism. In the
present study, we describe the signaling pathways that mediate this
response. Thrombin stimulation of the VCAM-1 gene and promoter in human umbilical vein endothelial cells was inhibited by preincubation with
the phosphatidylinositol 3-kinase inhibitor, LY294002, the protein
kinase C (PKC)-
inhibitor, rottlerin, a PKC-
peptide inhibitor,
or by overexpression of dominant negative (DN)-PKC-. In
electrophoretic mobility shift assays, thrombin-mediated induction of
NF-B p65 binding to two NF-B motifs in the upstream promoter region of VCAM-1 was blocked by LY294002 and rottlerin, whereas the
inducible binding of GATA-2 to a tandem GATA motif was inhibited by
LY294002 and the PKC- peptide inhibitor. In co-transfection assays,
thrombin stimulation of a minimal promoter containing multimerized
VCAM-1 NF-B sites was inhibited by DN-PKC- but not DN-PKC-. In
contrast, thrombin-mediated transactivation of a minimal promoter
containing tandem VCAM-1 GATA motifs was inhibited by DN-PKC- but
not DN-PKC-. Finally, thrombin failed to induce VCAM-1 expression in
vascular smooth muscle cells. Taken together, these data suggest that
the endothelial cell-specific effect of thrombin on VCAM-1 expression
involves the coordinate activity of PKC--NF-B and
PKC--GATA signaling pathways.
*
This work was supported by National Institutes of Health
Grants HL 60585-04, HL 63609-02, and HL 65216-03.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
To whom correspondence should be addressed: Beth Israel
Deaconess Medical Center, RW-663, Boston, MA 02215. Tel.: 617-667-1031; Fax: 617-667-2913; E-mail: waird@caregroup.harvard.edu.
Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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