References
- Aye, M. M., C. Ma, H. Lin, K. A. Bower, R. C. Wiggins, and J. Luo. 2004. Ethanol-induced in vitro invasion of breast cancer cells: The contribution of MMP-2 by fibroblasts. Int. J. Cancer 112: 738-746 https://doi.org/10.1002/ijc.20497
- Bachmeier, B. E., A. G. Nerlich, R. Lichtinghagen, and C. P. Sommerhoff. 2001. Matrix metalloproteinases (MMPs) in breast cancer cell lines of different tumorigenicity. Anticancer Res. 21:3821-3828
- Chen, J. and L. U. Thompson. 2003. Lignans and tamoxifen, alone or in combination, reduce human breast cancer cell adhesion, invasion and migration in vitro. Breast Cancer Res. Treat. 80: 163-170 https://doi.org/10.1023/A:1024513815374
- Cho, E. J., Md. A. Rahman, S. W. Kim, Y. M. Baek, H. J. Hwang, J. Y. Oh, H. S. Hwang, S. H. Lee, and J. W. Yun. 2008. Chitosan oligosaccharides inhibit adipogenesis in 3T3-L1 adipocytes. J. Microbiol. Biotechnol. 18: 80-87
- Friedel, G., U. Pastorino, R. J. Ginsberg, P. Goldstraw, M. Johnston, H. Pass, J. B. Putnam, and H. Toomes. 2002. Results of lung metastasectomy from breast cancer: Prognostic criteria on the basis of 467 cases of the International Registry of Lung Metastases. Eur. J. Cardiothorac. Surg. 22: 335-344 https://doi.org/10.1016/S1010-7940(02)00331-7
- Garibyan, L., C. Lenahan, and S. Pories. 2004. Metalloproteinases:Promising tumor markers for breast cancer management. Curr. Surg. 61: 255-259 https://doi.org/10.1016/j.cursur.2003.12.010
- Gonzalez, L. O., I. Pidal, S. Junquera, M. D. Corte, J. Vazquez, J. C. Rodriguez, et al. 2007. Overexpression of matrix metalloproteinases and their inhibitors in mononuclear inflammatory cells in breast cancer correlates with metastasis-relapse. Br. J. Cancer 97:957-963 https://doi.org/10.1038/sj.bjc.6603963
- Jeon, C. 2005. Mercury ion removal using a packed-bed column with granular aminated chitosan. J. Microbiol. Biotechnol. 15:497-501
- Jones, J. L., J. A. Shaw, J. H. Pringle, and R. A. Walker. 2003. Primary breast myoepithelial cells exert an invasion-suppressor effect on breast cancer cells via paracrine down-regulation of MMP expression in fibroblasts and tumour cells. J. Pathol. 201:562-572 https://doi.org/10.1002/path.1483
- Khasigov, P. Z., O. V. Podobed, T. S. Gracheva, K. D. Salbiev, S. V. Grachev, and T. T. Berezov. 2003. Role of matrix metalloproteinases and their inhibitors in tumor invasion and metastasis. Biochemistry (Mosc.) 68: 711-717 https://doi.org/10.1023/A:1025051214001
- Liotta, L. A., K. Tryggvason, S. Garbisa, I. Hart, C. M. Foltz, and S. Shafie. 1980. Metastatic potential correlates with enzymatic degradation of basement membrane collagen. Nature 284: 67-68 https://doi.org/10.1038/284067a0
- Nam, K. S., M. K. Kim, and Y. H. Shon. 2007. Chemopreventive effect of chitosan oligosaccharide against colon carcinogenesis. J. Microbiol. Biotechnol. 17: 1546-1549
- Nam, K. S., M. K. Kim, and Y. H. Shon. 2007. Inhibition of proinflammatory cytokine-induced invasiveness of HT-29 cells by chitosan oligosaccharide. J. Microbiol. Biotechnol. 17:2042-2045
- Nishimura, K., S. Nishimura, N. Nishi, I. Saiki, S. Tokura, and I. Azuma. 1984. Immunological activity of chitin and its derivatives. Vaccine 2:93-99 https://doi.org/10.1016/S0264-410X(98)90039-1
- Shin, W. S., J. C. Kil, and G. M. Park. 2006. Antiprotozoal activity of deacetylated chitosan oligosaccharide (dp 2-8) on Trichomonas vaginalis. J. Microbiol. Biotechnol. 16: 1984-1989
- Sreenath, T., L. M. Matrisian, W. Stetler-Stevenson, S. Gattoni-Celli, and R. O. Pozzatti. 1992. Expression of matrix metalloproteinases genes in transformed rat cell lines of high and low metastatic potential. Cancer Res. 52: 4942-4947
- Stetler-Stevenson, W. G., S. Aznavoorian, and L. Liotta. 1993. Tumor cell interactions with the extracellular matrix during invasion and metastasis. Annu. Rev. Cell Biol. 9: 541-573 https://doi.org/10.1146/annurev.cb.09.110193.002545
- Suzuki, K., T. Mikami, Y. Okawa, A. Tokoro, S. Suzuki, and M. Suzuki. 1986. Antitumor effect of hexa-N-acetylchitohexaose and chitohexaose. Carbohydr. Res. 151: 403-408 https://doi.org/10.1016/S0008-6215(00)90359-8
- Yilmaz, M., G. Christofori, and F. Lehembre. 2007. Distinct mechanisms of tumor invasion and metastasis. Trends Mol. Med. 13: 535-541 https://doi.org/10.1016/j.molmed.2007.10.004
- Yu, A. E., R. E. Hewitt, D. E. Kleiner, and W. G. Stetler-Stevenson. 1996. Molecular regulation of cellular invasion - role of gelatinase A and TIMP-2. Biochem. Cell Biol. 74: 823-831 https://doi.org/10.1139/o96-088
Cited by
- Antitumor properties of nonstarch polysaccharides: Fucoidans and chitosans vol.36, pp.5, 2009, https://doi.org/10.1134/s1063074010050019
- Antiproliferative activity of nanofibers containing quaternized chitosan and/or doxorubicin against MCF-7 human breast carcinoma cell line by apoptosis vol.26, pp.6, 2009, https://doi.org/10.1177/0883911511424655
- Chitosan oligosaccharide decreases very-low-density lipoprotein triglyceride and increases high-density lipoprotein cholesterol in high-fat-diet-fed rats vol.236, pp.9, 2009, https://doi.org/10.1258/ebm.2011.011032
- Inhibition of Bladder Tumor Growth by Chitooligosaccharides in an Experimental Carcinogenesis Model vol.10, pp.12, 2009, https://doi.org/10.3390/md10122661
- Resveratrol induces MMP-9 and cell migration via the p38 kinase and PI-3K pathways in HT1080 human fibrosarcoma cells vol.29, pp.2, 2009, https://doi.org/10.3892/or.2012.2151
- Downregulation of CD147 by chitooligosaccharide inhibits MMP-2 expression and suppresses the metastatic potential of human gastric cancer vol.8, pp.1, 2009, https://doi.org/10.3892/ol.2014.2115
- How to target small cell lung cancer vol.2, pp.8, 2015, https://doi.org/10.18632/oncoscience.212
- Total saponins isolated from Radix et Rhizoma Leonticis suppresses tumor cells growth by regulation of PI3K/Akt/mTOR and p38 MAPK pathways vol.41, pp.None, 2009, https://doi.org/10.1016/j.etap.2015.10.008
- Latest research progress in the correlation between baicalein and breast cancer invasion and metastasis vol.4, pp.4, 2016, https://doi.org/10.3892/mco.2016.750
- Knockdown of Cripto-1 inhibits the proliferation, migration, invasion, and angiogenesis in prostate carcinoma cells vol.42, pp.3, 2009, https://doi.org/10.1007/s12038-017-9700-y
- Anticancer Activity of Chitosan, Chitosan Derivatives, and Their Mechanism of Action vol.2018, pp.None, 2009, https://doi.org/10.1155/2018/2952085
- Cisplatin-Loaded Graphene Oxide/Chitosan/Hydroxyapatite Composite as a Promising Tool for Osteosarcoma-Affected Bone Regeneration vol.3, pp.11, 2018, https://doi.org/10.1021/acsomega.8b02090
- Potential Analysis and Preparation of Chitosan Oligosaccharides as Oral Nutritional Supplements of Cancer Adjuvant Therapy vol.20, pp.4, 2019, https://doi.org/10.3390/ijms20040920
- Inhibition of Liver Tumor Cell Metastasis by Partially Acetylated Chitosan Oligosaccharide on A Tumor-Vessel Microsystem vol.17, pp.7, 2009, https://doi.org/10.3390/md17070415
- Anti-aging Effect of Agar Oligosaccharide on Male Drosophila melanogaster and its Preliminary Mechanism vol.17, pp.11, 2009, https://doi.org/10.3390/md17110632
- Effect of chitosan oligosaccharide-conjugated selenium on improving immune function and blocking gastric cancer growth vol.891, pp.None, 2009, https://doi.org/10.1016/j.ejphar.2020.173673
- Plausible role of chitosan in drug and gene delivery against resistant breast cancer cells vol.506, pp.None, 2009, https://doi.org/10.1016/j.carres.2021.108357
- Evaluating the Anticarcinogenic Activity of Surface Modified/Functionalized Nanochitosan: The Emerging Trends and Endeavors vol.13, pp.18, 2021, https://doi.org/10.3390/polym13183138