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B Site of the Promoter Mediates Endothelial ICAM-1 Expression and Neutrophil Adhesion1
Department of Pharmacology, College of Medicine, University of Illinois, Chicago, IL 60612
We investigated the mechanisms by which proinflammatory mediator,
thrombin, released during intravascular coagulation and tissue injury,
induces ICAM-1 (CD54) expression in endothelial cells. Stimulation of
HUVEC with thrombin resulted in dose- and time-dependent increases in
ICAM-1 mRNA and cell surface expression and in ICAM-1-dependent
endothelial adhesivity toward polymorphonuclear leukocytes. Transient
transfection of endothelial cells with ICAM-1 promoter luciferase
reporter gene (ICAM-1LUC) constructs indicated that deletion of
upstream NF-
B site (-533 bases from translation start site) had no
effect on thrombin responsiveness, whereas mutation/deletion of
downstream NF-B site (-223 bases from the translation start site)
prevented the activation of ICAM-1 promoter, indicating that the
downstream NF-B site is critical for thrombin inducibility.
NF-B-directed luciferase activity increased 
3-fold when cells
transfected with the plasmid pNF-BLUC containing five copies of
consensus NF-B site linked to a minimal adenovirus E1B
promoter-luciferase gene were exposed to thrombin, indicating that
activation of NF-B was essential for thrombin response. Gel
supershift assays demonstrated that thrombin induced binding of
NF-Bp65 (Rel A) to downstream NF-B site of the ICAM-1 promoter.
Thrombin receptor activation peptide, a 14-amino-acid peptide
representing the new NH2 terminus of proteolytically
activated receptor-1, mimicked thrombin’s action in inducing ICAM-1
expression. These data indicate that thrombin activates endothelial
ICAM-1 expression and polymorphonuclear leukocyte adhesion by
NF-Bp65 binding to the downstream NF-B site of ICAM-1 promoter
after proteolytically activated receptor-1
activation.
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