Browse > Article
http://dx.doi.org/10.5352/JLS.2010.20.2.275

Effect of Sulforaphane on LPS-Induced Matrix Metalloproteinase-9 (MMP-9) Expression  

Lee, Jung-Tae (Department of Immunology, School of Medicine, Keimyung University)
Woo, Kyung-Jin (Department of Immunology, School of Medicine, Keimyung University)
Kwon, Taeg-Kyu (Department of Immunology, School of Medicine, Keimyung University)
Publication Information
Journal of Life Science / v.20, no.2, 2010 , pp. 275-280 More about this Journal
Abstract
Sulforaphane is a naturally occurring member of the iosothiocyanate family, which reveals chemopreventive capacities including anti-cancer, anti-inflammation and inhibition of MMP-9 activities. In this study, we investigated the effect of sulforaphane on the expression of matrix metalloproteinase-9 (MMP-9) in lipopolysaccharide (LPS)-induced Raw 264.7 cells. Sulforaphane strikingly suppressed the LPS-induced MMP-9 activity and mRNA expression in a dose-dependent manner. In addition, sulforaphane inhibited not only the LPS-induced MMP-9 promoter activity but also LPS-mediated activator protein-1 (AP-1) and nuclear factor-kB (NF-${\kappa}B$) promoter activity. Transient transfection by MMP-9 constructs, in which specific transcriptional factors were mutagenized, indicated that the effects of LPS and sulforaphane were mediated via AP-1 and NF-${\kappa}B$ response elements. We found that sulforaphane had the ability to suppress LPS-induced invasion in vitro. Taken together, these results demonstrated that sulforaphane effectively suppressed LPS-induced MMP-9 expression via modulation of promoter elements (AP-1 and NF-${\kappa}B$) in MMP-9 transcriptional activation.
Keywords
Sulforaphane; matrix metalloproteinase-9 (MMP-9); lipopolysaccharide (LPS); nuclear factor-${\kappa}B$ (NF-${\kappa}B$); Raw 264.7 cells;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Sato, H., M. Kita, and M. Seiki. 1993. v-Src activates the expression of 92-kDa type IV collagenase gene through the AP-1 site and the GT box homologous to retinoblastoma control elements. A mechanism regulating gene expression independent of that by inflammatory cytokines. J. Biol. Chem. 268, 23460-23468.
2 Simon, C., H. Goepfert, and D. Boyd. 1998. Inhibition of the p38 mitogen-activated protein kinase by SB 203580 blocks PMA-induced Mr 92,000 type IV collagenase secretion and in vitro invasion. Cancer Res. 58, 1135-1139.
3 Stetler-Stevenson, W. G. and A. E. Yu. 2001. Proteases in invasion: matrix metalloproteinases. Semin. Cancer Biol. 11, 143-152.   DOI
4 Thejass, P. and G. Kuttan. 2006. Antimetastatic activity of Sulforaphane. Life Sci. 78, 3043-3050.   DOI
5 Woo, J. H., J. H. Lim, Y. H. Kim, S. I. Suh, D. S. Min, J. S. Chang, Y. H. Lee, J. W. Park, and T. K. Kwon. 2004. Resveratrol inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting JNK and PKC delta signal transduction. Oncogene 23, 1845-1853.   DOI
6 Woo, J. H., J. W. Park, S. H. Lee, Y. H. Kim, I. K. Lee, E. Gabrielson, S. H. Lee, H. J. Lee, Y. H. Kho, and T. K. Kwon. 2003. Dykellic acid inhibits phorbol myristate acetate-induced matrix metalloproteinase-9 expression by inhibiting nuclear factor kappa B transcriptional activity. Cancer Res. 63, 3430-3434.
7 Brooks, J. D., V. G. Paton, and G. Vidanes. 2001. Potent induction of phase 2 enzymes in human prostate cells by sulforaphane. Cancer Epidemiol. Biomarkers Prev. 10, 949-954.
8 Gum, R., H. Wang, E. Lengyel, J. Juarez, and D. Boyd. 1997. Regulation of 92 kDa type IV collagenase expression by the jun aminoterminal kinase-and the extracellular signal-regulated kinase-dependent signaling cascades. Oncogene 14, 1481-1493.   DOI
9 Juge, N., R. F. Mithen, and M. Traka. 2007. Molecular basis for chemoprevention by sulforaphane: a comprehensive review. Cell Mol. Life Sci. 64, 1105-1127.   DOI
10 Kerkela, E, and U. Saarialho-Kere. 2003. Matrix metalloproteinases in tumor progression: focus on basal and squamous cell skin cancer. Exp. Dermatol. 12, 109-125.   DOI
11 Lee, P. P., J. J. Hwang, G. Murphy, and M. M. Ip. 2000. Functional significance of MMP-9 in tumor necrosis factor-induced proliferation and branching morphogenesis of mammary epithelial cells. Endocrinology 141, 3764-3773.   DOI
12 Nelson, A. R., B. Fingleton, M. L. Rothenberg, and L. M. Matrisian. 2000. Matrix metalloproteinases: biologic activity and clinical implications. J. Clin. Oncol. 18, 1135-1149.
13 Rose, P., Q. Huang, C. N. Ong, and M. Whiteman. 2005. Broccoli and watercress suppress matrix metalloproteinase-9 activity and invasiveness of human MDA-MB-231 breast cancer cells. Toxicol. Appl. Pharmacol. 209, 105-113.   DOI
14 Roy, R., J. Yang, and M. A. Moses. 2009. Matrix metalloproteinases as novel biomarkers and potential therapeutic targets in human cancer. J. Clin. Oncol. 27, 5287-5297.   DOI
15 Sato, H. and M. Seiki. 1993. Regulatory mechanism of 92 kDa type IV collagenase gene expression which is associated with invasiveness of tumor cells. Oncogene 8, 395-405.
16 Annabi, B., S. Rojas-Sutterlin, M. Laroche, M. P. Lachambre, R. Moumdjian, and R. Beliveau. 2008. The diet-derived sulforaphane inhibits matrix metalloproteinase-9-activated human brain microvascular endothelial cell migration and tubulogenesis. Mol. Nutr. Food Res. 52, 692-700.   DOI
17 Asakage, M., N. H. Tsuno, J. Kitayama, T. Tsuchiya, S. Yoneyama, J. Yamada, Y. Okaji, S. Kaisaki, T. Osada, K. Takahashi, and H. Nagawa. 2006. Sulforaphane induces inhibition of human umbilical vein endothelial cells proliferation by apoptosis. Angiogenesis 9, 83-91.   DOI
18 Basset, P., A. Okada, M. P. Chenard, R. Kannan, I. Stoll, P. Anglard, J. P. Bellocq, and M. C. Rio. 1997. Matrix metalloproteinases as stromal effectors of human carcinoma progression: therapeutic implications. Matrix Biol. 15, 535-541.   DOI   ScienceOn