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J Biol Chem, Vol. 273, Issue 19, 11583-11588, May 8, 1998
via
5
1 Integrin in HL-60 Cells
From the Center for Mechanistic Biology and Biotechnology, Argonne
National Laboratory, Argonne, Illinois 60439-4833
Tumor necrosis factor-
(TNF-) gene is one
of the early response genes induced by phorbol 12-myristate 13-acetate
(PMA) in human HL-60 myeloid leukemia cells. In the present study, we
examined the role of the TNF- autocrine loop in PMA-induced
macrophage differentiation and gene expression of 92- and 72-kDa
gelatinases (MMP-9 and MMP-2). In HL-60 cells, PMA inhibited cell
proliferation and induced cell adhesion and spreading, expression of
surface maturation marker OKM1 and phagocytic activity, as well as the expression of both gelatinases, which all characterize the macrophage phenotype. In contrast, TNF- alone was only effective in inhibiting cell proliferation. Blocking the endogenous TNF- activity with neutralizing anti-TNF- antibodies abolished all these PMA-induced events with the exception of MMP-2 gene expression. Since
fibronectin (FN)-mediated cell adhesion and spreading are prerequisite
for both macrophage differentiation and MMP-9 gene
expression in HL-60 cells, we hypothesized that TNF- might be
involved in modulating the expression of either the FN or its integrin
receptor genes. Whereas PMA substantially enhanced the steady state
mRNA and protein levels of both FN and
5
1 integrins, TNF- alone had little
effect on the expression of these genes. However, anti-TNF-
antibodies blocked PMA-induced augmentation of both 5
and 1 integrin gene expression without affecting the
expression of the FN gene. Our results suggest that TNF- may
regulate macrophage differentiation and critical matrix-degrading
activities of myeloid progenitor cells in an autocrine manner by
augmenting surface levels of the 51
integrin, thus promoting interactions with the extracellular matrix, a
key event for maturation and migration of these cells during
inflammation.
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