Affiliations: Biospectrum Life Science Institute, Gunpo City,
Republic of Korea | Department of Applied Biotechnology, Ajou University,
Suwon City, Republic of Korea
Note: [] Address for correspondence: Deokhoon Park, Biospectrum Life
Science Institute, 101-701 SK Ventium, 522 Dangjung Dong, Gunpo City, 435-833
Gyunggi Do, Republic of Korea. Fax: +82 31 436 0605; E-mail:
pdh@biospectrum.com
Abstract: 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.
