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Matrix metalloproteinase (MMP)‐12 regulates MMP‐9 expression in interleukin‐1β‐treated articular chondrocytes
Author(s) -
Oh Hwanhee,
Yang Siyoung,
Park Meeyoung,
Chun JangSoo
Publication year - 2008
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.21963
Subject(s) - matrix metalloproteinase , microbiology and biotechnology , p38 mitogen activated protein kinases , kinase , matrix metalloproteinase 3 , chemistry , signal transduction , extracellular matrix , mitogen activated protein kinase , protein kinase a , biology , biochemistry
Limited information is available on the expression and role of matrix metalloproteinase (MMP)‐12 in chondrocytes. We characterized the expression mechanism of MMP‐12 and possible function in chondrocytes. Interleukin (IL)‐1β induced the expression and activation of MMP‐12 in primary culture chondrocytes and cartilage explants via mitogen‐activated protein (MAP) kinase signaling pathways. Among MAP kinases, extracellular signal‐regulated kinase and p38 kinase are necessary for MMP‐12 expression, whereas c‐jun N‐terminal kinase is required for the activation of MMP‐12. The possibility that MMP‐12 acts as a modulator of other MMP was examined. MMP‐12 alone did not affect other MMP expressions. However, MMP‐12 enhanced expression and activation of MMP‐9 in the presence of IL‐1β. Our results indicate that IL‐1β in chondrocytes induces the expression and activation of MMP‐12, which, in turn, augments MMP‐9 expression and activation. J. Cell. Biochem. 105: 1443–1450, 2008. © 2008 Wiley‐Liss, Inc.