A study of matrix metalloproteinase-9 inhibitor in Hovenia dulcis Thunberg

김은호; 이광수

doi:10.5806/AST.2011.24.2.135

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P-ISSN1225-0163
E-ISSN2288-8985
SCOPUS, ESCI, KCI

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P-ISSN 1225-0163
E-ISSN 2288-8985

e-Submission

Vol.24, No.2

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A study of matrix metalloproteinase-9 inhibitor in Hovenia dulcis Thunberg

Analytical Science and Technology / Analytical Science and Technology, (P)1225-0163; (E)2288-8985

2011, v.24 no.2, pp.135-141

https://doi.org/10.5806/AST.2011.24.2.135

& (2011). A study of matrix metalloproteinase-9 inhibitor in Hovenia dulcis Thunberg. , 24(2), 135-141, https://doi.org/10.5806/AST.2011.24.2.135

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Abstract

MMPs (Matrix metalloproteinases) are enzymes playing an important role to turnover and remodel main protein compositions of extracellular matrix. MMP-2 and MMP-9 of MMPs having a catalytic domain which is apart from a hemopexin-like domain part, are different from the other MMPs pertaining fibronectinlike domain close to hemopexin-like domain. It was reported that the development of MMP-9 restrainer can prevent the transfer of liver cancer. In this study, MMP-9 restrainers were extracted and purified from Hovenia dulcis Thunberg. The each fractionary part was examined to investigate the inhibitory effect on MMPs. Three compounds, compound A and B eluted with ethyl acetate (EA) and compound C with methanol, were identified by ^1H and ^(13)C NMR, GC/MS, and FT-IR. Compound A is considered as a kind of catechine type compound having a benzene ring substituted by hydroxyl and methoxyl groups. Compound B and C are nobiletin type compound pertaining a carbonyl group. Compound A, B and C showed 76%, 66% and 71% of inhibition effect on MMP-9 at 1.0% concentration, respectively. Compound A showed the best inhibition effect on MMP-9.