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

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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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


Reference

1

1. R. Raghow, FASEB J., 17, 15-19(1994).

2

2. G. Murphy and A. J. Docherty, Am. J. Respir. Cell Mol. Biol. 7, 120-125(1992).

3

3. M. Nguyen, J. Arkell and C. J. Jackson, Inter. J. Biochem. & Cell Biol. 33, 960-970(2001).

4

4. D. E. Kleiner and W. G. Stetler-Stevenson, 43(Suppl), S42-S51(1999).

5

5. Y. Okada, K. Naka, K. Kawamura, T. Matsumoto, I. Nakanishi, N. Fujimoto, H. Sato and M. Seiki, Lab. Invest. 72, 311-322(1995).

6

6. T. E. Cawston, Pharm. Therapeu. 70, 163-182(1996).

7

7. L. Liotta, P. S. Steeg and W. G. Stetler-Stevenson, Cell 64, 327-336(1991).

8

8. S. K. Chandler, R. E. Coates, A. Gearing, J. Lury and E. A. Bone, Neurosci. Lett. 201, 223-226(1995).

9

9. S. Kim, H. S. Park, H. J. Son and W. S. Moon, Korean J. Hepatol. 10 62-72(2004).

10

10. Y. Noji, M. Shimizu, H. Ino, T. Higashikata, M. Yamaguchi, A. Nohara, T. Horita, K. Shimizu, Y. Ito, T. Matsuda, M. Namura and H. Mabuchi, Circ J. 68, 355-360(2004).

11

11. R. P. Beckett and M. Whittaker, Exp. Opin. Ther. Patents 8, 259-282(1998).

12

12. K. H. Kong, K. J. Han, K. S. Lee, S. H. Cho, Analytical Science and Technology 18, 104-111(2005).

13

13. Y. Okuma, H. Ishikawa, Y. Ito, Y. Hayashi, A. Endo, and T. Watanabe. 日本榮養·食糧學會誌, 48(3), 167-172(1995).

14

14. K. Hase and M. Ohsugi. Biological & Pharmaceutical Bulletin 41: 381-385(1997).

15

15. M. Yoshikawa, S. Tumura, K. Yamada, and T. Arihara. Biological & Pharmaceutical Bulletin 40, 2287-2291 (1992).

16

16. C. Heussen and E. B. Dowdle, Anal. Biochem. 102, 196-202(1980).

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