Browse > Article
http://dx.doi.org/10.5352/JLS.2019.29.3.287

Anti-invasion Effects of Calystegia soldanella Solvent Extracts and Partitioned Fractions on PMA-stimulated Fibrosarcoma Cells  

Son, Jaemin (Ocean Science and Technology School, Korea Maritime and Ocean University)
Kim, Junse (Ocean Science and Technology School, Korea Maritime and Ocean University)
Kim, Hojun (Division of Marine Bioscience, Korea Maritime and Ocean University)
Seo, Youngwan (Ocean Science and Technology School, Korea Maritime and Ocean University)
Publication Information
Journal of Life Science / v.29, no.3, 2019 , pp. 287-294 More about this Journal
Abstract
Calystegia soldanella is distributed in coastal sand dunes and has high environmental adaptability; it is also known to be effective for anti-oxidant, anti-pyretic, anti-septic, and diuretic action. This study investigated the effect of crude extracts and organic solvent fractions of C. soldanella on MMP-2 and MMP-9 expression, MMP activity, and cell mobility in phorbol-12-myristate-13-acetate (PMA)-induced fibrosarcoma HT-1080 cells. C. soldanella was twice extracted, once with methylene chloride (MC) and once with methanol (MeOH). After the MC and MeOH extracts were combined, their suppressive effects on MMP-2 and MMP-9 expression, MMP enzymatic activity, and gene and protein expression were measured by gelatin zymography, enzyme-linked immunosorbent assay, reverse-transcription polymerase chain reaction, and western blot method. Cell mobility for the HT-1080 cells was observed by wound healing assay. The combined crude extracts showed a significant suppressive effects on MMP-2 and MMP-9 expression. To explore active inhibitory elements, the combined extracts were fractionated according to polarity into with n-hexane, 85% aqueous methanol, n-butanol, and water. Across these four solvent fractions, MMP-2 and MMP-9 activity and cell mobility in the HT-1080 cells were all strongly inhibited by the n-hexane fraction. These results suggest that C. soldanella extract and organic solvent fractions could be used as potent MMP inhibitors for effective anti-cancer treatments to suppress cancer invasion and metastasis.
Keywords
Anti-invasive; anti-metastasis; Calystegia soldanella; HT-1080; MMP activity;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Ahn, N. R., Ko, J. M. and Cha, H. C. 2012. Comparison of flavonoid profiles between leaves and stems of Calystegia soldanella and Calystegia japonica. Am. J. Plant Sci. 3, 1073-1076.   DOI
2 Brown, P. D., Bioxidge, R. E., Anderson, E. and Howll, A. 1993. Expression of activated gelatinase in human invasive breast carcinoma. Clin. Exp. Metastasis 11, 183-189.   DOI
3 Chambers, A. F. and Matrisian, L. M. 1997. Changing views of the role of matrix metalloproteinases in metastasis. J. Natl. Cancer Inst. 89, 1260-1270.   DOI
4 Kato, Y., Yamashita, T. and Ishikawa, M. 2002. Relationship between expression of matrix metalloproteinase-2 and matrix metalloproteinase-9 and invasion ability of cervical cancer cells. Oncol. Rep. 9, 565-569.
5 Gentile, E. and Liuzzi, G. M. 2017. Marine pharmacology: therapeutic targeting of matrix metalloproteinases in neuroinflammation. Drug Discov. Today 22, 299-313.   DOI
6 Gialeli, C., Theocharis, A. D. and Karamanos, N. K. 2011. Roles of matrix metalloproteinases in cancer progression and their pharmacological targeting. FEBS J. 278, 16-27.   DOI
7 John, A. and Tuszynski, G. 2001. The role of matrix metalloproteinases in tumor angiogenesis and tumor metastasis. Pathol. Oncol. Res. 7, 14-23.   DOI
8 Kim, E. K., Yun, S. J., Do, K. H., Kim, M. S., Cho, M., Suh, D. S., Kim, C. D., Kim, J. H., Birnbaum, M. J. and Bae, S. S. 2008. Lysophosphatidic acid induces cell migration through the selective activation of Akt1. Exp. Mol. Med. 40, 445-452.   DOI
9 Lee, J. I., Kim, I. H. and Nam, T. J. 2017. Crude extract and solvent fractions of Calystegia soldanella induce G1 and S phase arrest of the cell cycle in HepG2 cells. Int. J. Oncol. 50, 414-420.   DOI
10 Mook, O. R., Frederiks, W. M. and Van Noorden, C. J. 2004. The role of gelatinases in colorectal cancer progression and metastasis. Biochim. Biophys. Acta Rev. Cancer 1705, 69-89.   DOI
11 Pavlovic, S., Du, B., Sakamoto, K., Khan, K. M., Natarajan, C., Breyer, R. M., Dannenberg, A. J. and Falcone, D. J. 2006. Targeting prostaglandin E2 receptors as an alternative strategy to block cyclooxygenase-2-dependent extracellular matrix-induced matrix metalloproteinase-9 expression by macrophages. J. Biol. Chem. 281, 3321-3328.   DOI
12 Stetler-Stevenson, W. G. 1990. Type IV collagenases in tumor invasion and metastasis. Cancer Metastasis Rev. 9, 289-303.   DOI
13 Pezzuto, J. M. 1997. Plant-derived anticancer agents. Biochem. Pharmacol. 53, 121-133.   DOI
14 Ramos-DeSimone, N., Hahn-Dantona, E., Sipley, J., Nagase, H., French, D. L. and Quigley, J. P. 1999. Activation of matrix metalloproteinase-9 (MMP-9) via a converging plasmin/ stromelysin-1 cascade enhances tumor cell invasion. J. Biol. Chem. 274, 13066-13076.   DOI
15 Siegel, R. L., Miller, K. D. and Jemal, A. 2017. Cancer statistics 2017. CA Cancer J. Clin. 67, 7-30.   DOI
16 Soreide, K., Janssen, E. A., Korner, H. and Baak, J. P. 2006. Trypsin in colorectal cancer: molecular biological mechanisms of proliferation, invasion, and metastasis. J. Pathol. 209, 147-156.   DOI
17 Spano, C., Bruno, M. and Bottega, S. 2013. Calystegia soldanella: dune versus laboratory plants to highlight key adaptive physiological trait. Acta Physiol. Plant. 35, 1329-1336   DOI
18 Tori, M., Ohara, Y., Nakashima, K. and Sono, M. 2000. Caffeic and courmaric acid esters from Calystegia soldanella. Fitoterapia 71, 353-359.   DOI
19 Vanmeter, T. E., Rooprai, H. K., Kibble, M. M., Fillmore, H. L., Broaddus, W. C. and Pilkington, G. J. 2001. The role of matrix metalloproteinase genes in glioma invasion: co-dependent and interactive proteolysis. J. Neurooncol. 53, 213-235.   DOI
20 Yang, Y. H. 2002. The relationship of symptoms of side effects, fatigue and quality of life in stomach cancer patients receiving chemotherapy. J. Korea Acad. Nurs. 14, 205-212.
21 Zeng, Z. S., Cohen, A. M. and Guillem, J. G. 1999. Loss of basement membrane type IV collagen is associated with increased expression of metalloproteinases 2 and 9 (MMP-2 and MMP-9) during human colorectal tumorigenesis. Carcinogenesis 20, 749-755.   DOI