Sensitization of HER2 Positive Breast Cancer Cells to Lapatinib Using Plants-Derived Isothiocyanates

Nutrition and Cancer

Volumn 67, Issue 6, 2015, Pages 976-986

  Kaczyńska, Angelika ^a   ͆wierczyńska, Joanna ^a   Herman Antosiewicz, Anna ^a  

^a UNIVERSITY OF GDA SK   (Poland)

Author keywords

[No Author keywords available]

Indexed keywords

EPIDERMAL GROWTH FACTOR RECEPTOR 2; ERUCIN; ISOTHIOCYANIC ACID DERIVATIVE; LAPATINIB; PROTEIN KINASE B; PROTEIN S6; SULFORAPHANE; SULFORAPHENE; UNCLASSIFIED DRUG; ANTINEOPLASTIC AGENT; ERBB2 PROTEIN, HUMAN; ISOTHIOCYANIC ACID; MTOR PROTEIN, HUMAN; QUINAZOLINE DERIVATIVE; RIBOSOMAL PROTEIN S6 KINASE, 70KD, POLYPEPTIDE 1; S6 KINASE; SULFIDE; SULFORAFAN; SULPHORAPHENE; TARGET OF RAPAMYCIN KINASE; THIOCYANIC ACID DERIVATIVE;

APOPTOSIS; ARTICLE; AUTOPHOSPHORYLATION; BREAST CANCER CELL LINE; CELL SURVIVAL; CELL VIABILITY; COMPARATIVE STUDY; CONTROLLED STUDY; FLOW CYTOMETRY; IN VITRO STUDY; MTT ASSAY; PROTEIN PHOSPHORYLATION; WESTERN BLOTTING; ANTAGONISTS AND INHIBITORS; BREAST TUMOR; CELL PROLIFERATION; DRUG EFFECTS; FEMALE; GENE EXPRESSION REGULATION; GENETICS; HUMAN; METABOLISM; SIGNAL TRANSDUCTION; TUMOR CELL LINE;

ANTINEOPLASTIC AGENTS, PHYTOGENIC; ANTINEOPLASTIC COMBINED CHEMOTHERAPY PROTOCOLS; APOPTOSIS; BREAST NEOPLASMS; CELL LINE, TUMOR; CELL PROLIFERATION; CELL SURVIVAL; FEMALE; GENE EXPRESSION REGULATION, NEOPLASTIC; HUMANS; ISOTHIOCYANATES; PROTO-ONCOGENE PROTEINS C-AKT; QUINAZOLINES; RECEPTOR, ERBB-2; RIBOSOMAL PROTEIN S6 KINASES, 70-KDA; SIGNAL TRANSDUCTION; SULFIDES; THIOCYANATES; TOR SERINE-THREONINE KINASES;

EID: 84939651574     PISSN: 01635581     EISSN: 15327914     Source Type: Journal    
DOI: 10.1080/01635581.2015.1053498     Document Type: Article

References (50)

1. Eccles SA: The role of c-erbB-2/HER2/neu in breast cancer progression and metastasis. J Mammary Gland Biol Neoplasia 6, 393-406, 2001
2. Moasser MM: The oncogene HER2: its signaling and transforming functions and its role in human cancer pathogenesis. Oncogene 26, 6469-6487, 2007.
3. Ross JS and Fletcher JA: The HER-2/neu oncogene in breast cancer: prognostic factor, predictive factor, and target for therapy. Stem Cells 16, 413-428, 1998.
4. Ross JS, Slodkowska EA, Symmans WF, Pusztai L, Ravdin PM, et al.: The HER-2 receptor and breast cancer: ten years of targeted anti-HER-2 therapy and personalized medicine. Oncologist 14, 320-368, 2009.
5. Klos KS, Wyszomierski SL, Sun M, Tan M, Zhou X, et al.: ErbB2 increases vascular endothelial growth factor protein synthesis via activation of mammalian target of rapamycin/p70S6K leading to increased angiogenesis and spontaneous metastasis of human breast cancer cells. Cancer Res 66, 2028-2037, 2006.
6. Ghosh R, Narasanna A, Wang SE, Liu S, Chakrabarty A, et al.: Trastuzumab has preferential activity against breast cancers driven by HER2 homodimers. Cancer Res 71, 1871-1882, 2011.
7. Browne BC, O'Brien N, Duffy MJ, Crown J, and O'Donovan N: HER-2 signaling and inhibition in breast cancer. Curr Cancer Drug Targets 9, 419-438, 2009.
8. Agus DB, Akita RW, Fox WD, Lewis GD, Higgins B, et al.: Targeting ligand-activated ErbB2 signaling inhibits breast and prostate tumor growth. Cancer Cell 2, 127-137, 2002.
9. Lee-Hoeflich ST, Crocker L, Yao E, Pham T, Munroe X, et al.: A central role for HER3 in HER2-amplified breast cancer: implications for targeted therapy. Cancer Res 68, 5878-5887, 2008.
10. Nelson MH and Dolder CR: A review of lapatinib ditosylate in the treatment of refractory or advanced breast cancer. Ther Clin Risk Manag 3, 665-673, 2007
11. Rusnak DW, Affleck K, Cockerill SG, Stubberfield C, Harris R, et al.: The characterization of novel, dual ErbB-2/EGFR, tyrosine kinase inhibitors: potential therapy for cancer. Cancer Res 61, 7196-7203, 2001
12. Rusnak DW, Lackey K, Affleck K, Wood ER, Alligood KJ, et al.: The effects of the novel, reversible epidermal growth factor receptor/ErbB-2 tyrosine kinase inhibitor, GW2016, on the growth of human normal and tumor-derived cell lines in vitro and in vivo. Mol Cancer Ther 1, 85-94, 2001
13. Mukohara T: Role of HER2-targeted agents in adjuvant treatment for breast cancer. Chemother Res Pract 2011, 730360, 2011.
14. Rana P and Sridhar SS: Efficacy and tolerability of lapatinib in the management of breast cancer. Breast Cancer (Auckl) 6, 67-77, 2012.
15. Wang YC, Morrison G, Gillihan R, Guo J, Ward RM, et al.: Different mechanisms for resistance to trastuzumab versus lapatinib in HER2-positive breast cancers-role of estrogen receptor and HER2 reactivation. Breast Cancer Res 13, R121, 2011.
16. Storniolo AM, Pegram MD, Overmoyer B, Silverman P, Peacock NW, et al.: Phase I dose escalation and pharmacokinetic study of lapatinib in combination with trastuzumab in patients with advanced ErbB2-positive breast cancer. J Clin Oncol 26, 3317-3323, 2008.
17. Melchini A and Traka MH: Biological profile of erucin: a new promising anticancer agent from cruciferous vegetables. Toxins (Basel) 2, 593-612, 2010.
18. Gupta P, Kim B, Kim SH, and Srivastava SK:Molecular targets of isothiocyanates in cancer: Recent advances. Mol Nutr Food Res, 58, 1685-1707, 2014.
19. Barcelo S, Gardiner JM, Gescher A, and Chipman JK: CYP2E1-mediated mechanism of anti-genotoxicity of the broccoli constituent sulforaphane. Carcinogenesis 17, 277-282, 1996.
20. Zhang Y, Talalay P, Cho CG, and Posner GH: A major inducer of anticarcinogenic protective enzymes from broccoli: isolation and elucidation of structure. Proc Natl Acad Sci U S A 89, 2399-2403, 1992.
21. Fahey JW, Zhang Y, and Talalay P: Broccoli sprouts: an exceptionally rich source of inducers of enzymes that protect against chemical carcinogens. Proc Natl Acad Sci U S A 94, 10367-10372, 1997.
22. Munday R and Munday CM: Induction of phase II detoxification enzymes in rats by plant-derived isothiocyanates: comparison of allyl isothiocyanate with sulforaphane and related compounds. J Agric Food Chem 52, 1867-1871, 2004.
23. Clarke JD, Riedl K, Bella D, Schwartz SJ, Stevens JF, et al.: Comparison of isothiocyanate metabolite levels and histone deacetylase activity in human subjects consuming broccoli sprouts or broccoli supplement. J Agric Food Chem 59, 10955-10963, 2011.
24. Singh SV, Srivastava SK, Choi S, Lew KL, Antosiewicz J, et al.: Sulforaphane-induced cell death in human prostate cancer cells is initiated by reactive oxygen species. J Biol Chem 280, 19911-19924, 2005.
25. Xiao D, Powolny AA, Antosiewicz J, Hahm ER, Bommareddy A, et al.: Cellular responses to cancer chemopreventive agent D,L-sulforaphane in human prostate cancer cells are initiated by mitochondrial reactive oxygen species. Pharm Res 26, 1729-1738, 2009.
26. Azarenko O, Okouneva T, Singletary KW, Jordan MA, and Wilson L: Suppression of microtubule dynamic instability and turnover in MCF7 breast cancer cells by sulforaphane. Carcinogenesis 29, 2360-2368, 2008.
27. Mi L, Xiao Z, Hood BL, Dakshanamurthy S, Wang X, et al.: Covalent binding to tubulin by isothiocyanates. A mechanism of cell growth arrest and apoptosis. J Biol Chem 283, 22136-22146, 2008.
28. Pledgie-Tracy A, Sobolewski MD, and Davidson NE: Sulforaphane induces cell type-specific apoptosis in human breast cancer cell lines. Mol Cancer Ther 6, 1013-1021, 2007.
29. Jakubikova J, Sedlak J, Mithen R, and Bao Y: Role of PI3K/Akt and MEK/ERK signaling pathways in sulforaphane-and erucin-induced phase II enzymes and MRP2 transcription, G2/M arrest and cell death in Caco-2 cells. Biochem Pharmacol 69, 1543-1552, 2005.
30. Singh SV, Herman-Antosiewicz A, Singh AV, Lew KL, Srivastava SK, et al.: Sulforaphane-induced G2/M phase cell cycle arrest involves checkpoint kinase 2-mediated phosphorylation of cell division cycle 25C. J Biol Chem 279, 25813-25822, 2004.
31. Pawlik A, Wiczk A, Kaczynska A, Antosiewicz J, and Herman-Antosiewicz A: Sulforaphane inhibits growth of phenotypically different breast cancer cells. Eur J Nutr, 52, 1949-1958, 2013.
32. Chou TC and Talalay P: Quantitative analysis of dose-effect relationships: the combined effects of multiple drugs or enzyme inhibitors. Adv Enzyme Regul 22, 27-55, 1984.
33. Slamon DJ, Clark GM, Wong SG, Levin WJ, Ullrich A, et al.: Human breast cancer: correlation of relapse and survival with amplification of the HER-2/neu oncogene. Science 235, 177-182, 1987.
34. Chen FL, Xia W, and Spector NL: Acquired resistance to small molecule ErbB2 tyrosine kinase inhibitors. Clin Cancer Res 14, 6730-6734, 2008.
35. Melchini A, Costa C, Traka M, Miceli N, Mithen R, et al.: Erucin, a new promising cancer chemopreventive agent from rocket salads, shows antiproliferative activity on human lung carcinoma A549 cells. Food Chem Toxicol 47, 1430-1436, 2009.
36. Kim MJ, Kim SH, and Lim SJ: Comparison of the apoptosis-inducing capability of sulforaphane analogues in human colon cancer cells. Anticancer Res 30, 3611-3619, 2010.
37. Jakubikova J, Bao Y, and Sedlak J: Isothiocyanates induce cell cycle arrest, apoptosis and mitochondrial potential depolarization in HL-60 and multidrug-resistant cell lines. Anticancer Res 25, 3375-3386, 2005.
38. Konecny GE, Pegram MD, Venkatesan N, Finn R, Yang G, et al.: Activity of the dual kinase inhibitor lapatinib (GW572016) against HER-2-overexpressing and trastuzumab-treated breast cancer cells. Cancer Res 66, 1630-1639, 2006.
39. Diermeier-Daucher S, Breindl S, Buchholz S, Ortmann O, and Brockhoff G: Modular anti-EGFR and anti-Her2 targeting of SK-BR-3 and BT474 breast cancer cell lines in the presence of ErbB receptor-specific growth factors. Cytometry A 79, 684-693, 2011.
40. Bordonaro M, Tewari S, Cicco CE, Atamna W, and Lazarova DL: A switch from canonical to noncanonical Wnt signaling mediates drug resistance in colon cancer cells. PLoS One 6, e27308, 2011.
41. Chaudhuri D, Orsulic S, and Ashok BT: Antiproliferative activity of sulforaphane in Akt-overexpressing ovarian cancer cells. Mol Cancer Ther 6, 334-45, 2007.
42. Suppipat K, Park CS, Shen Y, Zhu X, and Lacorazza HD: Sulforaphane induces cell cycle arrest and apoptosis in acute lymphoblastic leukemia cells. PLoS One 7, e51251, 2012.
43. Jin CY, Moon DO, Lee JD, Heo MS, Choi YH, et al.: Sulforaphane sensitizes tumor necrosis factor-related apoptosis-inducing ligand-mediated apoptosis through downregulation of ERK and Akt in lung adenocarcinoma A549 cells. Carcinogenesis 28, 1058-1066, 2007.
44. Manning BD and Cantley LC: AKT/PKB signaling: navigating downstream. Cell 129, 1261-1274, 2007.
45. Gasper AV, Al-Janobi A, Smith JA, Bacon JR, Fortun P, et al.: Glutathione S-transferase M1 polymorphism and metabolism of sulforaphane from standard and high-glucosinolate broccoli. Am J Clin Nutr 82, 1283-1291, 2005.
46. Kassahun K, Davis M, Hu P, Martin B, and Baillie T: Biotransformation of the naturally occurring isothiocyanate sulforaphane in the rat: identification of phase I metabolites and glutathione conjugates. Chem Res Toxicol 10, 1228-1233, 1997.
47. Vermeulen M, van den Berg R, Freidig AP, van Bladeren PJ, and Vaes WH: Association between consumption of cruciferous vegetables and condiments and excretion in urine of isothiocyanate mercapturic acids. J Agric Food Chem 54, 5350-5358, 2006.
48. Zhou C, Poulton EJ, Grun F, Bammler TK, Blumberg B, et al.: The dietary isothiocyanate sulforaphane is an antagonist of the human steroid and xenobiotic nuclear receptor. Mol Pharmacol 71, 220-229, 2007.
49. Teng WC, Oh JW, New LS, Wahlin MD, Nelson SD, et al.: Mechanismbased inactivation of cytochrome P450 3A4 by lapatinib. Mol Pharmacol 78, 693-703, 2010.
50. Masubuchi Y and Horie T: Toxicological significance of mechanismbased inactivation of cytochrome p450 enzymes by drugs. Crit Rev Toxicol 37, 389-412, 2007.