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

헛개나무내의 Matrix Metalloproteinase-9 활성 억제제에 관한 연구

  • Kim, Eun-Ho (Chemical Analysis Division, National Forensic Service) ;
  • Lee, Kwang-Soo (Department of Food & Nutrition, Jangan University)
  • 김은호 (국립과학수사연구원 법과학부 화학분석과) ;
  • 이광수 (장안대학교 건강과학부 식품영양과)
  • Received : 2011.02.09
  • Accepted : 2011.02.25
  • Published : 2011.04.25


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.


Hovenia dulcis Thunberg.;MMPs;GC/MS;IR;NMR;Nobiletin


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