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(Received for publication, January 25, 1996, and in revised form, October 25, 1996)
From the Both astrocytes in the central nervous system and
fibroblasts in somatic tissues are not only the major sources of
extracellular matrix components but also of matrix metalloproteinases
(MMPs), a family of enzymes directly involved in extracellular matrix breakdown. We have analyzed the regulation of the expression of MMPs
and TIMPs (tissue inhibitors of metalloproteinases) in human primary
astrocytes stimulated with oncostatin M (OSM) and other extracellular
mediators in comparison with normal human dermal fibroblasts. It was
found that OSM induced/enhanced transcription of MMP-1 (interstitial
collagenase) and MMP-3 (stromelysin 1) in astrocytes, and MMP-1, MMP-9
(gelatinase B), and TIMP-1 in fibroblasts. Analysis of the signal
transduction leading to activation of the MMP-1 gene revealed the
presence of an OSM-responsive element (OMRE) encompassing the AP-1
binding site and the signal transducer and activator of transcription
(STAT) binding element, which mediate activation by OSM. OMRE is also
present in the TIMP-1 gene promoter and, although there are some
differences in these two motifs, both appear to be targets for the
simultaneous action of OSM-induced nuclear effectors. The induced
enhancement of transcription by synergistically acting AP-1 and STAT
binding elements in response to OSM is Raf-dependent.
Cross-talk between the mitogen-activated protein kinase and JAK-STAT
pathways is required to achieve maximal induction of the OMRE-driven
transcription by OSM.
Volume 272, Number 2,
Issue of January 10, 1997
pp. 1188-1196
©1997 by The American Society for Biochemistry and Molecular Biology, Inc.
,
and
Department of Biochemistry and Molecular
Biology, University of Georgia, Athens, Georgia 30602, the
¶ Department of Biochemistry and Molecular Biology, University of
Kansas Medical Center, Kansas City, Kansas 66160, and 
Athena
Neurosciences, Inc., South San Francisco, California 94080
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