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J Biol Chem, Vol. 273, Issue 16, 9769-9777, April 17, 1998
From the Departamento de Bioquímica y Biología
Molecular, Facultad de Medicina, Universidad de Oviedo,
33006 Oviedo, Spain
Collagenase-3 (MMP-13) is a matrix
metalloproteinase (MMP) originally identified in breast carcinomas
which is also produced at significant levels during fetal ossification
and in arthritic processes. In this work, we have found that
transforming growth factor
Differential Effects of Transforming Growth Factor-
on the
Expression of Collagenase-1 and Collagenase-3 in Human
Fibroblasts
1 (TGF-1), a growth factor widely
assumed to be inhibitory for MMPs, strongly induces collagenase-3
expression in human KMST fibroblasts. In contrast, this growth factor
down-regulated the expression in these cells of collagenase-1 (MMP-1),
an enzyme highly related to collagenase-3 in terms of structure and
enzymatic properties. The positive effect of TGF-1 on collagenase-3
expression was dose- and time-dependent, but independent of
the effects of this growth factor on cell proliferation rate. Analysis
of the signal transduction mechanisms underlying the up-regulating
effect of TGF-1 on collagenase-3 expression demonstrated that this
growth factor acts through a signaling pathway involving protein kinase C and tyrosine kinase activities. Functional analysis of the
collagenase-3 gene promoter region revealed that the inductive effect
of TGF-1 is partially mediated by an AP-1 site. Comparative analysis
with the promoter region of the collagenase-1 gene which contains an AP-1 site at equivalent position, confirmed that TGF-1 did not have
any effect on CAT activity levels of this promoter. Finally, by using
electrophoretic mobility shift assays and antibody supershift analysis,
we propose that c-Fos, c-Jun, and JunD may play major roles in the
collagenase-3 activation by TGF-1 in human fibroblasts.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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