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Tumor necrosis factor-alpha modulation of glycoprotein Ib alpha expression
in human endothelial and erythroleukemia cells
V Rajagopalan, DW Essex, SS Shapiro and BA Konkle
Cardeza Foundation for Hematologic Research, Department of Medicine,
Jefferson Medical College of Thomas Jefferson University, Philadelphia, PA
19107.
Glycoprotein Ib alpha (GpIb alpha) is a platelet membrane Gp that binds von
Willebrand factor and mediates platelet adhesion to subendothelium. We have
found both GpIb alpha mRNA and protein in human umbilical vein endothelial
cells (HUVEC). In previously published work we reported that combined
treatment with interferon-gamma (IFN-gamma) and tumor necrosis factor-alpha
(TNF-alpha) markedly increased the GpIb alpha mRNA level in HUVEC. We have
now documented that TNF-alpha alone induces GpIb alpha mRNA and protein
expression, studied the kinetics of this response, and investigated
potential mechanisms of the TNF-alpha effect. GpIb alpha mRNA induction by
TNF-alpha is detectable as early as 2 hours after exposure to this
cytokine, and reaches a maximal level after 20 to 24 hours. Using a nuclear
run-on assay we found that GpIb alpha gene transcription is increased
approximately 10-fold after 2 hours of TNF-alpha treatment. Furthermore,
using two monoclonal antibodies that recognize different epitopes of GpIb
alpha, we found that the protein expression in endothelial cells is
markedly increased by TNF-alpha. Interleukin-1 (IL-1) and the phorbol ester
phorbol myristate acetate, which mimic many effects of TNF-alpha on
endothelial cells, have no effect on endothelial or human erytholeukemia
(HEL)-cell GpIb alpha mRNA. TNF-alpha treatment for 24 hours increases the
HEL cell GpIb alpha mRNA level approximately fourfold, showing a time- and
dose-dependent effect similar to that seen in HUVEC. TNF-alpha-induced GpIb
alpha mRNA and protein synthesis may play a role in mediating platelet or
other cell interaction with activated endothelium. Unlike other endothelial
pro-thrombotic and pro-adhesive proteins induced by TNF-alpha, GpIb alpha
is not induced by IL-1 treatment, which suggests a novel pathway for
induction of this protein.
Volume 80,
Issue 1,
pp. 153-161,
07/01/1992
Copyright © 1992 by The American Society of Hematology
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