- P-ISSN 1225-0163
- E-ISSN 2288-8985
- P-ISSN1225-0163
- E-ISSN2288-8985
- SCOPUS, ESCI, KCI
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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
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(2011). A study of matrix metalloproteinase-9 inhibitor in Hovenia dulcis Thunberg. Analytical Science and Technology, 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.
- keywords
- Hovenia dulcis Thunberg., MMPs, GC/MS, IR, NMR, Nobiletin
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