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J Biol Chem, Vol. 274, Issue 52, 37292-37300, December 24, 1999
From the Human collagenase-3 (matrix
metalloproteinase 13 (MMP-13)) is characterized by exceptionally wide
substrate specificity and restricted tissue specific expression. Human
skin fibroblasts in culture express MMP-13 only when they are in
three-dimensional collagen (Ravanti, L., Heino, J.,
López-Otín, C., and Kähäri. V.-M. (1999)
J. Biol. Chem. 274, 2446-2455). Here we show that MMP-13 is expressed by fibroblasts during normal human gingival wound
repair. Expression of MMP-13 by human gingival fibroblasts cultured in
monolayer or in collagen gel was induced by transforming growth
factor-
Transforming Growth Factor-
Induces Collagenase-3
Expression by Human Gingival Fibroblasts via p38 Mitogen-activated
Protein Kinase*
§,
,, and§§§
Department of Dermatology, Turku University
Central Hospital, § MediCity Research Laboratory, and
Department of Medical Biochemistry, University of Turku, FIN-20520
Turku, Finland, the ¶ Department of Oral Biological and Medical
Sciences, University of British Columbia, Vancouver, British Columbia,
V6T 1Z3 Canada, the Department of Dermatology, Helsinki
University Central Hospital, FIN-00250 Helsinki, Finland, the
** Department of Internal Medicine, University of Florence, Florence
50134, Italy, and the Department of
Immunology, Scripps Research Institute,
La Jolla, California 92121
1 (TGF-1). Treatment of gingival fibroblasts with TGF-1
activated two distinct mitogen-activated protein kinases (MAPKs):
extracellular signal-regulated kinase 1/2 (ERK1/2) in 15 min and p38
MAPK in 1 and 2 h. Induction of MMP-13 expression by TGF-1 was
blocked by SB203580, a specific inhibitor of p38 MAPK, but not by
PD98059, a selective inhibitor of ERK1/2 activation. Adenovirus-mediated expression of dominant negative p38
and c-Jun potently inhibited induction of MMP-13 expression in gingival fibroblasts by TGF-1. Infection of gingival fibroblasts with adenovirus for constitutively active MEK1 resulted in activation of
ERK1/2 and JNK1 and up-regulation of collagenase-1 (MMP-1) and
stromelysin-1 (MMP-3) production but did not induce MMP-13 expression.
In addition, activation of p38 MAPK by constitutively active MKK6b or
MKK3b was not sufficient to induce MMP-13 expression. These results
show that TGF--elicited induction of MMP-13 expression by
gingival fibroblasts is dependent on the activity of p38 MAPK and
the presence of functional AP-1 dimers. These observations demonstrate
a fundamental difference in the regulation of collagenolytic capacity
between gingival and dermal fibroblasts and suggest a role for MMP-13
in rapid turnover of collagenous matrix during repair of gingival
wounds, which heal with minimal scarring.
*
This work was supported by grants from the Academy of
Finland, the Sigrid Jusélius Foundation, the Cancer Research
Foundation of Finland, Turku University Central Hospital, the Research
and Science Foundation of Farmos, the Finnish Medical Foundation, the
Turku University Foundation, and Turku Graduate School in Biomedical
Sciences.The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Copyright © 1999 by The American Society for Biochemistry and Molecular Biology, Inc.
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