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B-
in Endothelial Cell Activation1
*
Vascular Medicine and Atherosclerosis Unit, Cardiovascular Division, Brigham and Women’s Hospital and Harvard Medical School, Boston, MA 02115; and
Medical Clinic II, Johannes Gutenberg University, Mainz, Germany
The NF-
B inhibitor IB-
is a new member of the IB
protein family, but its functional role in regulating NF-B-mediated
induction of adhesion molecule expression is unknown. In vascular
endothelial cells, IB- associates predominantly with the NF-B
subunit Rel A and to a lesser extent with c-Rel, whereas IB-
and
IB-ß associate with Rel A only. Following stimulation with
TNF-, pyrrolidine dithiocarbamate (PDTC),
N-acetylcysteine, and dexamethasone prevented IB
kinase-induced IB-, but not IB-ß or IB-
phosphorylation and degradation. Since the activation of NF-B is
required for the induction of adhesion molecule expression, we examined
the role of IB- in the transactivation of promoters from VCAM-1,
ICAM-1, and E-selectin. Using reporter gene constructs of adhesion
molecule promoters, PDTC inhibited VCAM-1 and E-selectin, but to a
lesser extent, ICAM-1 promoter activity. Subcloning of B
cis-acting elements of VCAM-1, E-selectin, and ICAM-1
into a heterologous promoter construct revealed that PDTC inhibited
VCAM-1 and E-selectin, but to a lesser extent, ICAM-1 B promoter
activity. By electrophoretic mobility shift assay, NF-B heterodimers
containing c-Rel specifically bind to the B motif in the ICAM-1, but
not VCAM-1 or E-selectin promoter. Indeed, overexpression of c-Rel
induced ICAM-1 B promoter activity to a greater extent than that of
E-selectin and overexpression of IB- inhibited ICAM-1 and VCAM-1
promoter activity in endothelial cells. These findings indicate that
c-Rel-associated IB- is involved in the induction of ICAM-1
expression.
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