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(Received for publication, August 5, 1996, and in revised form, January 8, 1997)
and§
From the Urokinase-type plasminogen activator (uPA) and
92-kDa matrix metalloproteinase (MMP-9) expression by RAW264.7
macrophages were up-regulated when plated on extracellular matrices.
Collagen IV, fibronectin, and tenascin stimulated macrophages' MMP-9
expression. In contrast, laminin stimulated both uPA and MMP-9
expression in a dose- and time-dependent manner. The
increase in macrophage uPA activity was preceded by an increase in
their steady state levels of uPA mRNA. Laminin-induced uPA
expression was most pronounced in RAW264.7 macrophages followed by
THP-1 monocytes, J774A.1 macrophages, and bone marrow-derived
macrophages. Neither laminin nor matrix induced alterations in THP-1
monocyte expression of plasminogen activator inhibitor, tissue
inhibitor of metalloproteinase (TIMP)-1 or TIMP-2. Synthetic laminin
peptides were utilized to identify the laminin domain(s) responsible
for induction of uPA expression. Peptides derived from the 
Department of Pathology, the
§ Department of Cell Biology & Anatomy and the Center of
Vascular Biology, Cornell University Medical College,
New York, New York 10021
1 chain
of laminin had no effect on macrophage uPA expression, whereas SIKVAV,
derived from 
1 chain, stimulated uPA expression 20-fold.
Preincubation of THP-1 monocytes with a monoclonal antibody directed
against the 6 subunit of the 61 laminin receptor blocked
matrix induction of uPA without affecting the induction of MMP-9. These
results demonstrate that macrophage binding to laminin plays an
important role in the regulation of their degradative phenotype via the
up-regulation of uPA and MMP-9.
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