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Matrine inhibits PMA‐induced MMP‐1 expression in human dermal fibroblasts
Author(s) -
Jung Eunsun,
Lee Jongsung,
Huh Sungran,
Lee Jienny,
Hwang Hyunjin,
Kim Youngsoo,
Kim YongWoo,
Park Deokhoon,
Yo Byun Sang
Publication year - 2008
Publication title -
biofactors
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.204
H-Index - 94
eISSN - 1872-8081
pISSN - 0951-6433
DOI - 10.1002/biof.5520330204
Subject(s) - matrine , phosphorylation , kinase , p38 mitogen activated protein kinases , signal transduction , protein kinase c , extracellular matrix , microbiology and biotechnology , protein kinase a , chemistry , matrix metalloproteinase , extracellular , fibroblast , biology , biochemistry , in vitro , chromatography
Matrix metalloproteinase‐1 (MMP‐1) plays an important role in the maintenance and turnover of extracellular matrix (ECM) macromolecules. Remodelling of extracellular matrix by MMPs is a hallmark feature of physiological and pathological processes. In this study, in order to establish the therapeutic potential of matrine, we investigated its effect on MMP‐1 expression in human dermal fibroblast cells. We found that matrine inhibited both MMP‐1 mRNA and protein expression induced by PMA (phorbol myristate acetate). Therefore, we characterized the inhibitory mechanism of matrine on PMA‐induced MMP‐1 expression. Matrine inhibited PMA‐induced activation of the AP‐1 promoter, an important nuclear transcription factor in MMP‐1 expression. Additionally, we detected that matrine suppressed the PMA‐induced phosphorylation of two mitogen‐activated protein kinases, extracellular signal‐regulated protein kinase and c‐Jun N‐terminal kinase, but did not suppress the PMA‐induced phosphorylation of p38 kinase. These results suggest that matrine suppresses PMA‐induced MMP‐1 expression through inhibition of the AP‐1 signaling pathway and also may be beneficial for treatment of some inflammatory skin disorders.