Issue

Vol. 6 No. 2 (2014)

A Cationic [60] Fullerene Derivative Reduces Invasion and Migration of HT-29 CRC Cells in Vitro at Dose Free of Significant Effects on Cell Survival

https://doi.org/10.1007/BF03353780
Marianna Lucaf`o
Department of Life Sciences, University of Trieste, Via Giorgieri 5, 34127, Trieste (TS), Italy
Chiara Pelillo
Department of Life Sciences, University of Trieste, Via Giorgieri 5, 34127, Trieste (TS), Italy
Marco Carini
Department of Chemical and Pharmaceutical Sciences, University of Trieste, Piazzale Europa 1, 34127, Trieste (TS), Italy
TatianaDa Ros
Department of Chemical and Pharmaceutical Sciences, University of Trieste, Piazzale Europa 1, 34127, Trieste (TS), Italy
Maurizio Prato
Department of Chemical and Pharmaceutical Sciences, University of Trieste, Piazzale Europa 1, 34127, Trieste (TS), Italy
Gianni Sava
Department of Life Sciences, University of Trieste, Via Giorgieri 5, 34127, Trieste (TS), Italy

Corresponding Author: Gianni Sava

gsava@units.it

Nano-Micro Letters, Vol. 6 No. 2 (2014), Article Number: 163-168

Abstract

Nanomaterials with unique characteristics exhibit favorable therapeutic and diagnostic properties, implying their enormous potential as biomedical candidates. C60 has been used in gene- and drug-delivery, as imaging agents, and as photosensitizers in cancer therapy. In this study, the influences of a cationic functionalized fullerene on cellular behavior of human colorectal cancer cell line (HT-29) were investigated. Results indicated that HT-29 treated with the studied compound showed a lower sensitivity but a significant impairment in migration and invasion by interfering with the activities of matrix metalloproteinases (MMP-2 and 9). The presence of fullerene also altered the capacity of adhesion-related proteins to perform their activity, thereby inducing dramatically adverse effects on the cell physiological functions such as cell adhesion. Thus, our study suggests that this compound is a new potential anti-metastatic effector and a therapeutic component for malignant colorectal cancer.

Keywords

Fullerene Cancer Anti-metastatic drug Nanomedicine
Lucaf`o, Marianna, Chiara Pelillo, Marco Carini, TatianaDa Ros, Maurizio Prato, and Gianni Sava. 2014. “A Cationic [60] Fullerene Derivative Reduces Invasion and Migration of HT-29 CRC Cells in Vitro at Dose Free of Significant Effects on Cell Survival”. Nano-Micro Letters 6 (2):163-68. https://doi.org/10.1007/BF03353780.
Download Citation
Endnote/Zotero/Mendeley (RIS)
BibTeX
References
  1. A. Jemal, R. Siegel, J. Xu and E. Ward, “Cancer statistics, 2010”, CA Cancer J. Clin. 60(5), 277–300 (2010). http://dx.doi.org/10.3322/caac.20073
  2. J. M. Davies and R. M. Goldberg, “Treatment of metastatic colorectal cancer”, Semin. Oncol. 38(4), 552–60 (2011). http://dx.doi.org/10.1053/j.seminoncol.2011.05.009
  3. K. K. Jain, “Nanotechnology in clinical laboratory diagnostics”, Clin. Chim. Acta 358 (1–2), 37–54 (2005). http://dx.doi.org/10.1016/j.cccn.2005.03.014
  4. P. Chaudhuri, R. Harfouche, S. Soni, D. M. Hentschel, and S. Sengupta, “Shape effect of carbon nanovectors on angiogenesis”, ACS Nano 4(1), 574–82 (2010). http://dx.doi.org/10.1021/nn901465h
  5. M. Grodzik, E. Sawosz, M. Wierzbicki, P. Orlowski, A. Hotowy, T. Niemiec, M. Szmidt, K. Mitura and A. Chwalibog, “Nanoparticles of carbon allotropes inhibit glioblastoma multiforme angiogenesis in ovo”, Int. J. Nanomed. 6, 3041–3048 (2011). http://dx.doi.org/10.2147/IJN.S25528
  6. M. Wierzbicki, E. Sawosz, M. Grodzik, M. Prasek, S. Jaworski and A. Chwalibog “Comparison of antiangiogenic properties of pristine carbon nanoparticles”, Nanoscale Res. Lett. 8(1), 195 (2013). http://dx.doi.org/10.1186/1556-276X-8-195
  7. S. V. Prylutska, A. P. Burlaka, Y. I. Prylutskyy, U. Ritter and P. Scharff, “Pristine C(60) fullerenes inhibit the rate of tumor growth and metastasis”, Exp Oncol 33(3), 162–164 (2011).
  8. C. Chen, G. Xing, J. Wang, Y. Zhao, B. Li, J. Tang, G. Jia, T. Wang, J. Sun, L. Xing, H. Yuan, Y. Gao, H. Meng, Z. Chen, F. Zhao, Z. Chai and X. Fang, “Multihydroxylated [Gd@C82(OH)22]n nanoparticles: Antineoplastic activity of high efficiency and low toxi-city”, Nano Lett. 5(10), 2050–2057 (2005). http://dx.doi.org/10.1021/nl051624b
  9. M. Lucafò, S. Pacor, C. Fabbro, T. Da Ros, S. Zorzet, M. Prato and G. Sava, “Study of a potential drug delivery system based on carbon nanoparticles: Effects of fullerene derivatives in MCF7 mammary carcinoma cells”, J. Nanopart. Res. 14, 1–13 (2012). http://dx.doi.org/10.1007/s11051-012-0830-8
  10. M. Lucafò, M. Gerdol, A. Pallavicini, S. Pacor, S. Zorzet, T. Da Ros, M. Prato and G. Sava, “Profiling the molecular mechanism of fullerene cytotoxicity on tumorcells by RNA-seq”, Toxicology 314(1), 183–192 (2013). http://dx.doi.org/10.1016/j.tox.2013.10.001
  11. K. Kordatos, T. Da Ros, S. Bosi, E. Vazquez, M. Bergamin, C. Cusan, F. Pellarini, V. Tomberli, B. Baiti, D. Pantarotto, V. Georgakilas, G. Spalluto and M. Prato, “Novel versatile fullerene synthons”, J. Org. Chem. 66, 4915–4920 (2001). http://dx.doi.org/10.1021/jo015608k
  12. A. Albini, Y. Iwamoto, H. K. Kleinman, G. R. Martin, S. A. Aaronson, J. M. Kozlowski and R. N. McEwan, “A rapid in vitro assay for quantitating the invasive potential of tumor cells”, Cancer Res. 47(12), 3239–45 (1987).
  13. P. Provenzano and P. J. Keely, “Mechanical signaling through the cytoskeleton regulates cell proliferation by coordinated focal adhesion and Rho GTPase signalling”, J. Cell Sci. 124 (Pt8), 1195–1205 (2001). http://dx.doi.org/10.1242/jcs.067009
  14. F. G. Giancotti and E. Ruoslahti, “Integrin signaling”, Science 285(5430), 1028–1032 (1999). http://dx.doi.org/10.1126/science.285.5430.1028
  15. J. D. Hood and D. A. Cheresh, “Role of integrins in cell invasion and migration”, Nature Rev. Cancer 2(2), 91–100 (2002). http://dx.doi.org/10.1038/nrc727
  16. F. Aoudjit and K. Vuori, “Integrin signaling in cancer cell survival and chemoresistance”, Chemother. Res. Pract. 1-16 (2012). http://dx.doi.org/10.1155/2012/283181
  17. M. Millard, S. Odde and N. Neamati, “Integrin targeted therapeutics”, Theranostics 1, 154–188 (2011). http://dx.doi.org/10.7150/thno/v01p0154
  18. S. Hernandez-Barrantes, M. Bernardo, M. Toth, and R. Fridman, “Regulation of membrane type-matrix metalloproteinases”, Semin. Cancer Biol. 12(2), 131–138 (2002). http://dx.doi.org/10.1006/scbi.2001.0421
  19. H. Sato, T. Takino, Y. Okada, J. Cao, A. Shinagawa, E. Yamamoto, and M. Seiki, “A matrix metalloproteinase expressed on the surface of invasive tumour cells”, Nature 370(6484), 61–65 (1994). http://dx.doi.org/10.1038/370061a0
  20. A. Y. Strongin, B. L. Marmer, G. A. Grant and G. I. Goldberg “Plasma membrane-dependent activation of the 72-kDa type IV collagenase is prevented by complex formation with TIMP-2”, J. Biol. Chem. 268(19), 14033–14039 (1993).
  21. Q. Nguyen, F. Willenbrock, M. I. Cockett, M. O’Shea, A. J. Docherty and G. Murphy, “Different domain interactions are involved in the binding of tissue inhibitors of metalloproteinases to stromelysin-1 and gelatinase A”, Biochem. 33(8), 2089–2095 (1994). http://dx.doi.org/10.1021/bi00174a015
  22. M. Bernardo and R. Fridman, “TIMP-2 (tissue inhibitor of metalloproteinase-2) regulates MMP-2 (matrix metalloproteinase-2) activity in the extracellular environment after pro-MMP-2 activation by MT1 (membrane type 1)-MMP”, Biochem. J. 374 (Pt3), 739–745 (2003). http://dx.doi.org/10.1042/BJ20030557
  23. P. Vempati, E. D. Karagiannis and A. S. Popel “A Biochemical Model of Matrix Metalloproteinase 9 Activation and Inhibition”, J. Biol. Chem. 282(52), 37585–37596 (2007). http://dx.doi.org/10.1074/jbc.M611500200
  24. H. Kolkenbrock, D. Orgel, A. Hecker-Kia, W Noack, N. Ulbrich “The complex between a tissue inhibitor of metalloproteinases (TIMP-2) and 72-kDa progelatinase is a metalloproteinase inhibitor”, Eur. J. Biochem. 198(3), 775–781 (1991). http://dx.doi.org/10.1111/j.1432-1033.1991.tb16080.x
  25. N. Fujimoto, R. V. Ward, T. Shinya, K. Iwata, Y. Yamashita and T. Hayakawa, “Interaction between tissue inhibitor of metalloproteinases-2 and progelatinase A: immunoreactivity analyses”, Biochem. J. 313 (Pt3), 827–833 (1996).
Read More
Author biographies are not available.
Download this PDF file
PDF
Statistic
Read Counter : 4437 Download : 3375