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J. Biol. Chem., Vol. 277, Issue 10, 7865-7874, March 8, 2002
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From the Neutral matrix metalloproteinases (MMPs) play an
important role in bone matrix degradation accompanied by bone
remodeling. We herein show for the first time that macrophage migration
inhibitory factor (MIF) up-regulates MMP-13 (collagenase-3) mRNA of
rat calvaria-derived osteoblasts. The mRNA
up-regulation was seen at 3 h in response to MIF (10 µg/ml), reached the maximum level at 6-12 h, and returned to the
basal level at 36 h. MMP-13 mRNA up-regulation was preceded by
up-regulation of c-jun and c-fos mRNA.
Tissue inhibitor of metalloproteinase (TIMP)-1 and MMP-9 (92-kDa type
IV collagenase) were also up-regulated, but to a lesser extent. The
MMP-13 mRNA up-regulation was significantly suppressed by
genistein, herbimycin A and
4-amino-5-(4-chlorophenyl)-7-(t-butyl)pyrazolo[3,4-d]pyrimidine. Similarly, a selective mitogen-activated protein kinase (MAPK) kinase
(MEK)1/2 inhibitor (PD98059) and c-jun/activator protein (AP)-1 inhibitor (curcumin) suppressed MMP-13 mRNA
up-regulation induced by MIF. The mRNA levels of c-jun
and c-fos in response to MIF were also inhibited by
PD98059. Consistent with these results, MIF stimulated phosphorylation
of tyrosine, autophosphorylation of Src, activation of Ras, activation
of extracellular signal-regulated kinases (ERK) 1/2, a MAPK, but not
c-Jun N-terminal kinase or p38, and phosphorylation of c-Jun.
Osteoblasts obtained from calvariae of newborn JunAA mice, defective in
phosphorylation of c-Jun, or newborn c-Fos knockout (Fos
Macrophage Migration Inhibitory Factor Up-regulates Matrix
Metalloproteinase-9 and -13 in Rat Osteoblasts
RELEVANCE TO INTRACELLULAR SIGNALING PATHWAYS*
§,
,,
Department of Orthopaedics, ¶ Central
Research Institute, Department of
Biochemistry, and §§ Department of
Ophthalmology, Hokkaido University Graduate School of Medicine, Sapporo
060-8638, the ** Division of Immunobiology, Institute for
Genetic Medicine, Hokkaido University, Sapporo 060-0815, and the
¶¶ Department of Orthopaedic Surgery, Faculty of Medicine,
University of Tokyo, Tokyo 113-0033, Japan
/) mice,
showed much less induction of MMP-13 with the addition of MIF than
osteoblasts obtained from wild-type or littermate control mice. Taken
together, these results suggest that MIF increases the MMP-13 mRNA
level of rat osteoblasts via the Src-related tyrosine kinase-,
Ras-, ERK1/2-, and AP-1-dependent pathway.
*
This work was supported in part by grants-in aid from the
Hokkaido Foundation for the Promotion of Scientific and Industrial Technology and from the Nakatomi Foundation.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.
To whom correspondence should be addressed: Central
Research Inst., Hokkaido University School of Medicine, Sapporo
060-8638, Japan. Tel.: 81-11-706-6081; Fax: 81-11-706-7864;
E-mail: j_nisihi@med.hokudai.ac.jp.
Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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