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http://dx.doi.org/10.4217/OPR.2018.40.4.249

Inhibitory Effects of Carex pumila Extracts on MMP-2 and MMP-9 Activities in HT-1080 Cells  

Kim, Junse (Ocean Science and Technology School, Korea Maritime and Ocean University)
Kong, Chang-Suk (Department of Food and Nutrition, College of Medical & Life Sciences, Silla University)
Seo, Youngwan (Ocean Science and Technology School, Korea Maritime and Ocean University)
Publication Information
Ocean and Polar Research / v.40, no.4, 2018 , pp. 249-257 More about this Journal
Abstract
Matrix metalloproteinases (MMPs) are associated with the invasion and metastasis of malignant tumors composed of cancer cells in an increased state of expression. This study evaluates the inhibitory effect of Carex pumila on MMP-2 and MMP-9 activity in phorbol-12-myristate-13-acetate (PMA)-stimulated HT-1080 human fibrosarcoma cells using gelatin zymography, MMPs enzyme-linked immunosorbent assay (ELISA), reverse transcription-polymerase chain reaction (RT-PCR) and Western blot assay. C. pumila was extracted twice with dichloromethane ($CH_2Cl_2$) and methanol (MeOH). Treatment with $CH_2Cl_2$ extract and MeOH extract in PMA-stimulated HT-1080 cells effectively reduced the production of MMP-2 and 9. Also, the combined crude extracts ($CH_2Cl_2$ and MeOH) significantly inhibited the enzymatic activities and the expression of MMP-2 and MMP-9 in mRNA and protein levels. The combined crude extracts were partitioned between $CH_2Cl_2$ and water. The organic layer was further fractionated with n-hexane, 85% aqueous methanol (85% aq.MeOH) and the aqueous layer was separated into n-butanol and water, successively. Of the fractions, 85% aq.MeOH fraction showed the highest inhibitory activity of MMP-2 and MMP-9 in gelatin zymography and MMP ELISA kit. Furthermore, 85% aq.MeOH fraction most significantly suppressed cell migration. In RT-PCR and Western blot assay, n-butanol and 85% aq.MeOH fractions exerted the greatest inhibition on mRNA and protein expression of MMP-2 and MMP-9, respectively. As a result, C. pumila can be used as a good anti-invasive agent source.
Keywords
Carex pumila; HT-1080; MMP; anti-invasive;
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1 Kim HJ, Kong C-S, Seo YW (2017) Inhibitory activity of Ligustrum japonicum fructus on MMP-2 and MMP-9. KSBB 32:328-334   DOI
2 Min BM (1998) Vegetation on the west coast of Korea. Ocean Res 20:167-178
3 Son JM, Kim HJ, Kong C-S, Seo YW (2018) Anti-invasive effect of the solvent-partitioned fractions from viticis fructus in PMA-induced HT-1080 cells. J Life Sci 28:293-299
4 Oh SH, Kim HJ (2008) The plant resources of the sand dune on southern coast and Jeju island, Korea. Korean J Plant Res 21:374-387
5 Lim HN, Kim YM (2014) Carex pumila extract supresses mast cell activation and IgE-mediated allergic response in mice. J Food Hyg Saf 29:356-362   DOI
6 Cho W, Song H-S, Hong S-C, Choi D-C (2009) Characteristics of the vegetation in the coastal dunes near the swimming beaches on the East Sea coast, South Korea. Kor J Env Eco 23:499-505
7 Abdelly C, Barhoumi Z, Ghnaya T, Debez A, Ben Hamed K, Ksouri R, Talbi O, Zribi F, Ouerghi Z, Smaoui A, Huchzermeyer B, Grignon C (2006) Potential utilisation of halophytes for the rehabilitation and valorisation of salt-affected areas in Tunisia. In: Ozturk M, Waisel Y, Khan MA, Gork G (eds) Biosaline agriculture and salinity tolerance in plants. Birkhauser Verlag, Basel, pp 163-172
8 Amar S, Fields GB (2015) Potential clinical implications of recent matrix metalloproteinase inhibitor design strategies. Expert Rev Proteomics 12:445-447   DOI
9 Brooks PC, Stromblad S, Sanders LC, von Schalscha TL, Aimes RT, Stetler-Stevenson WG, Quigley JP, Cheresh DA (1996) Localization of matrix metalloproteinase MMP-2 to the surface of invasive cells by interaction with integrin ${\alpha}v{\beta}3$. Cell 85:683-693   DOI
10 Kim EK (2013) Halophytes of Korea. Jayeongwa Saengtae, Seuol, 368 p
11 Kong C-S, Kim YA, Kim M-M, Park J-S, Kim J-A, Kim S-K, Lee B-J, Nam TJ, Seo YW (2008) Flavonoid glycosides isolated from Salicornia herbacea inhibit matrix metalloproteinase in HT1080 cells. Toxicol Vitro 22:1742-1748   DOI
12 Jablonska-Trypuc A, Matejczyk M, Rosochacki S (2016) Matrix metalloproteinases (MMPs), the main extracellular matrix (ECM) enzymes in collagen degradation, as a target for anticancer drugs. J Enzyme Inhib Med Chem 31:177-183   DOI
13 Kawabata J, Mishima M, Kurihara H, Mizutani J (1991) Kobophenol B, a tetrastilbene from Carex pumila. Phytochemistry 30:645-647   DOI
14 Kong C-S, Lee JI, Kim YA, Kim J-A, Bak SS, Hong JW, Park HY, Yea SS, Seo YW (2012) Evaluation on anti-adipogenic activity of flavonoid glucopyranosides from Salicornia herbacea. Process Biochem 47:1073-1078   DOI
15 Reznicek AA (1993) Carex pumila (Cyperaceae) in North America. Castanea 58:220-224
16 Ksouri R, Ksouri WM, Jallali I, Debez A, Magne C, Hiroko I, Abdelly C (2012) Medicinal halophytes: potent source of health promoting biomolecules with medical, nutraceutical and food applications. Crit Rev Biotechnol 32:289-326   DOI
17 Kurihara H, Kawabata J, Ichikawa S, Mizutani J (1990) (-)-${\varepsilon}$-Viniferin and related oligostilbenes from Carex pumila Thunb (Cyperaceae). Agric Biol Chem 54:1097-1099
18 Mook ORF, Frederiks WM, Van Noorden CJF (2004) The role of gelatinases in colorectal cancer progression and metastasis. BBA 1705:69-89
19 Senior RM, Griffin GL, Fliszar CJ, Shapiro SD, Goldberg GI, Welgus HG (1991) Human 92- and 72 kilodalton type IV Collagenases are elastases. J Biol Chem 266:7870-7875
20 Shay G, Lynch CC, Fingleton B (2015) Moving targets: emerging roles for MMPs in cancer progression and metastasis. Matrix Biol 44-46:200-206   DOI
21 Xue M, Jackson CJ (2008) Autocrine actions of matrix metalloproteinase (MMP)-2 counter the effects of MMP-9 to promote survival and prevent terminal differentiation of cultured human keratinocytes. J Invest Dermatol 128:2676-2685   DOI
22 Snoek-van Beurden PAM, Von den Hoff JW (2005) Zymographic techniques for the analysis of matrix metalloproteinases and their inhibitors. BioTechniques 38:73-83   DOI
23 Verma RP, Hansch C (2007) Matrix metalloproteinases (MMPs): chemical-biologicalfunctions and (Q)SARs. Bioorg Med Chem 15:2223-2268   DOI
24 Westermarck J, Kahari VM (1999) Regulation of matrix metalloproteinase expression in tumor invasion. FASEB J 13:781-792   DOI