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J Biol Chem, Vol. 273, Issue 19, 11576-11582, May 8, 1998
From the Center for Mechanistic Biology and Biotechnology, Argonne
National Laboratory, Argonne, Illinois 60439-4833
Induction of the 92-kDa gelatinase
(MMP-9) gene expression is associated with macrophage
differentiation. In this study, we explored the regulatory mechanisms
underlying this differentiation-associated MMP-9 gene
expression in human HL-60 myeloid leukemia cells and human peripheral
blood monocytes. Phorbol 12-myristate 13-acetate (PMA) markedly induced
MMP-9 gene expression in HL-60 cells; the induction closely
paralleled the timing and extent of PMA-induced cell adhesion and
spreading, a hallmark of macrophage differentiation. Similarly,
treatment with PMA or macrophage-colony stimulating factor stimulated
adherence and spreading of blood monocytes with a concurrent 7- or
5-fold increase in MMP-9 production, respectively. In protein kinase C
(PKC)--deficient HL-60 variant cells (HL-525), PMA failed to induce
cell adhesion and MMP-9 gene expression. Transfecting
HL-525 cells with a PKC- expression plasmid restored PKC- levels
and PMA inducibility of cell adhesion and spreading as well as
MMP-9 gene expression. Induction of cell adhesion and MMP-9 gene expression in HL-60 cells and blood monocytes
was strongly inhibited by neutralizing monoclonal antibodies to
fibronectin (FN) and its receptor 
51
integrin. HL-525 cells, which constitutively display high levels of
surface 51 integrin, adhered and spread on immobilized FN with concomitant induction of MMP-9 gene
expression. Cytochalasins B and D were each a potent inhibitor of MMP-9
production. Our results suggest that 51
integrin-mediated interaction of immature hematopoietic cells with FN
plays a critical role in modulating matrix-degrading activities during
macrophage differentiation.
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