Antiproliferative activities of Amaryllidaceae alkaloids from Lycoris radiata targeting DNA topoisomerase i

Scientific Reports

Volumn 6, Issue , 2016, Pages

  Chen, Gui Lin ^a,b   Tian, Yong Qiang ^a,b   Wu, Jian Lin ^c   Li, Na ^c   Guo, Ming Quan ^a,d  

^a Wuhan Institute of Botany Chinese Academy of Sciences   (China)

^b UNIVERSITY OF CHINESE ACADEMY OF SCIENCES   (China)

^c MACAU UNIVERSITY OF SCIENCE AND TECHNOLOGY   (Macao)

^d INSTITUTE OF GEOLOGY AND GEOPHYSICS   (China)

Author keywords

[No Author keywords available]

Indexed keywords

AMARYLLIDACEAE ALKALOID; ANTINEOPLASTIC AGENT; DNA TOPOISOMERASE; DNA TOPOISOMERASE INHIBITOR; ESCHERICHIA COLI PROTEIN; HIPPEASTRINE; PROTEIN BINDING;

ALPHA HELIX; BETA SHEET; BINDING SITE; CELL PROLIFERATION; CELL SURVIVAL; CHEMISTRY; DRUG EFFECT; ENZYME ASSAY; ENZYMOLOGY; ESCHERICHIA COLI; HEP-G2 CELL LINE; HT-29 CELL LINE; HUMAN; ISOLATION AND PURIFICATION; KINETICS; LYCORIS; METABOLISM; MOLECULAR DOCKING; PLANT ROOT; PROTEIN DOMAIN; THERMODYNAMICS;

AMARYLLIDACEAE ALKALOIDS; ANTINEOPLASTIC AGENTS, PHYTOGENIC; BINDING SITES; CELL PROLIFERATION; CELL SURVIVAL; DNA TOPOISOMERASES, TYPE I; ENZYME ASSAYS; ESCHERICHIA COLI; ESCHERICHIA COLI PROTEINS; HEP G2 CELLS; HT29 CELLS; HUMANS; KINETICS; LYCORIS; MOLECULAR DOCKING SIMULATION; PLANT ROOTS; PROTEIN BINDING; PROTEIN CONFORMATION, ALPHA-HELICAL; PROTEIN CONFORMATION, BETA-STRAND; PROTEIN INTERACTION DOMAINS AND MOTIFS; THERMODYNAMICS; TOPOISOMERASE I INHIBITORS;

EID: 85003024858     PISSN: None     EISSN: 20452322     Source Type: Journal    
DOI: 10.1038/srep38284     Document Type: Article

References (52)

1. Jin, Z. Amaryllidaceae and Sceletium alkaloids. Nat. Prod. Rep. 30, 849-868 (2013).
2. Katoch, D., Kumar, S., Kumar, N., Singh, B. Simultaneous quantification of Amaryllidaceae alkaloids from Zephyranthes grandiflora by UPLC-DAD/ESI-MS/MS. J. Pharmaceut. Biomed. 71, 187-192 (2012).
3. Nair, J. J., Aremu, A. O., van Staden, J. Isolation of narciprimine from Cyrtanthus contractus (Amaryllidaceae) and evaluation of its acetylcholinesterase inhibitory activity. J. Ethnopharmacol. 137, 1102-1106 (2011).
4. Lamoral-Theys, D. et al. Lycorine, the main phenanthridine Amaryllidaceae alkaloid, exhibits significant antitumor activity in cancer cells that display resistance to proapoptotic stimuli: an investigation of structure-activity relationship and mechanistic insight. J. Medi. Chem. 52, 6244-6256 (2009).
5. Kang, M. R. et al. Methanolic Extract Isolated from Root of Lycoris aurea Inhibits Cancer Cell Growth and Endothelial Cell Tube Formation In Vitro. Toxicol. Res. 28, 33-38 (2012).
6. Cedron, J. C., Gutierrez, D., Flores, N., Ravelo, A. G., Estevez-Braun, A. Preparation and antimalarial activity of semisynthetic lycorenine derivatives. Eur. J. Med. Chem. 63, 722-730 (2013).
7. Jin, A. et al. Four new compounds from the bulbs of Lycoris aurea with neuroprotective effects against CoCl(2) and H(2)O(2)-induced SH-SY5Y cell injuries. Arch. Pharm. Res. 37, 315-323 (2014).
8. Li, C. Y. et al. Molecular mechanisms of Lycoris aurea agglutinin-induced apoptosis and G2/M cell cycle arrest in human lung adenocarcinoma A549 cells, both in vitro and in vivo. Cell Proliferat. 46, 272-282 (2013).
9. Goietsenoven, G. V. et al. Targeting of eEF1A with Amaryllidaceae isocarbostyrils as a strategy to combat melanomas. Faseb. J. 24, 4575-4584 (2010).
10. Goietsenoven, G. V. et al. Narciclasine as well as other Amaryllidaceae isocarbostyrils are promising GTP-ase targeting agents against brain cancers. Med. Res. Rev. 33, 439-455 (2013).
11. Yao, C., Na, N., Huang, L., He, D., Ouyang, J. High-throughput detection of drugs binding to proteins using desorption electrospray ionization mass spectrometry. Anal. Chim. Acta. 794, 60-66 (2013).
12. Zhu, H. et al. Bioactivity fingerprint analysis of cyclooxygenase-2 ligands from radix Aconiti by ultrafiltration-UPLC-MSn. Anal. Bioanal. Chem. 405, 7437-7445 (2013).
13. Qin, S. et al. Multiple ligand detection and affinity measurement by ultrafiltration and mass spectrometry analysis applied to fragment mixture screening. Anal. Chim. Acta. 886, 98-106 (2015).
14. Chowdhury, A. R. et al. Luteolin, an emerging anti-cancer flavonoid, poisons eukaryotic DNA topoisomerase I. Biochem. J. 365, 653-661 (2002).
15. Champoux, J. J. DNA Topoisomerases: Structure, Function, Mechanism. Annu. Rev. Biochem. 70, 369-413 (2001).
16. Kim, N. et al. Mutagenic processing of ribonucleotides in DNA by yeast topoisomerase I. science 332, 1561-1564 (2011).
17. Pommier, Y. Topoisomerase I inhibitors: camptothecins and beyond. Nat. Rev. Cancer. 6, 789-802 (2006).
18. Puc, J. et al. Ligand-dependent enhancer activation regulated by topoisomerase-I activity. Cell 160, 367-380 (2015).
19. Chaudhuri, A. R. et al. Topoisomerase I poisoning results in PARP-mediated replication fork reversal. Nat. Struct. Mol. Biol. 19, 417-423 (2012).
20. Li, T. K., Liu, L. F. Tumor cell death induced by topoisomerasetargeting drugs. Annu. Rev. Pharmacol. 41, 53-77 (2001).
21. Holleran, L. J. L. et al. Liquid chromatography-tandem mass spectrometric assay for the quantitation in human plasma of the novel indenoisoquinoline topoisomerase I inhibitors, NSC 743400 and NSC 725776. J. Pharmaceut. Biome. 52, 714-720 (2010).
22. Schovanek, J. et al. Inhibitory Effect of the Noncamptothecin Topoisomerase I Inhibitor LMP-400 on Female Mice Models and Human Pheochromocytoma Cells. Endocrinology 156, 4094-4104 (2015).
23. Majumdar, P. et al. Design, synthesis and evaluation of thiohydantoin derivatives as potent topoisomerase I (Top1) inhibitors with anticancer activity. Eur. J. Med. Chem. 102, 540-551 (2015).
24. Tian, Y. Q., Zhang, C. Y., Guo, M. Q. Comparative Analysis of Amaryllidaceae Alkaloids from Three Lycoris Species. Molecules 20, 21854-21869 (2015).
25. Li, S. N., Tang, Y., Liu, C. M., Zhang, Y. C. Development of a method to screen and isolate potential alpha-glucosidase inhibitors from Panax japonicus C. A. Meyer by ultrafiltration, liquid chromatography, counter-current chromatography. J. Sep. Sci. 38, 2014-2023 (2015).
26. Zhou, M. et al. Mass Spectrometry of Intact V-Type ATPases Reveals Bound Lipids and the Effects of Nucleotide Binding. Science 334, 380-385 (2011).
27. Liao, N., Ao, M. Z., Zhang, P., Yu, L. J. Extracts of Lycoris aurea induce apoptosis in murine sarcoma S180 cells. Molecules 17, 3723-3735 (2012).
28. Hao, B., Shen, S. F., Zhao, Q. J. Cytotoxic and antimalarial amaryllidaceae alkaloids from the bulbs of Lycoris radiata. Molecules 18, 2458-2468 (2013).
29. Li, Z. X. et al. Novel insights into the apoptosis mechanism of DNA topoisomerase I inhibitor isoliquiritigenin on HCC tumor cell. Biochem. Bioph. Res. Co. 464, 548-553 (2015).
30. Gilbert, D. C., Chalmers, A. J., El-Khamisy, S. F. Topoisomerase I inhibition in colorectal cancer: biomarkers and therapeutic targets. Brit. J. cancer. 106, 18-24 (2012).
31. Lee, Y. C. et al. Targeting of Topoisomerase I for Prognoses and Therapeutics of Camptothecin-Resistant Ovarian Cancer. PloS One 10, e0132579 (2015).
32. Miyata, S. et al. Mechanism of the inhibition of leukemia cell growth and induction of apoptosis through the activation of ATR and PTEN by the topoisomerase inhibitor 3EZ, 20Ac-ingenol. Leukemia. Res. 39, 927-932 (2015).
33. Su, H. et al. Supramolecular Crafting of Self-Assembling Camptothecin Prodrugs with Enhanced Efficacy against Primary Cancer Cells. Theranostics 6, 1065-1074 (2016).
34. Sharma, K. N. et al. Nitric Oxide Down-Regulates Topoisomerase I and Induces Camptothecin Resistance in Human Breast MCF-7 Tumor Cells. PloS one 10, e0141897 (2015).
35. Yu, L. M. et al. Synthesis and biological evaluation of 6-substituted indolizinoquinolinediones as catalytic DNA topoisomerase I inhibitors. Eur. J. Med. Chem. 101, 525-533 (2015).
36. Piao, D. G. et al. DNA Topoisomerase Inhibitory Activity of Constituents from the Flowers of Inula japonica. Chem. Pharm. Bull. 64, 276-281 (2016).
37. Liu, X. S. et al. Lycorine induces apoptosis and down-regulation of Mcl-1 in human leukemia cells. Cancer letters 274, 16-24 (2009).
38. Kang, J. et al. Lycorine inhibits lipopolysaccharide-induced iNOS and COX-2 up-regulation in RAW264. 7 cells through suppressing P38 and STATs activation and increases the survival rate of mice after LPS challenge. Int. Immunopharmaco. 12, 249-256 (2012).
39. Evidente, A., Kornienko, A. Anticancer evaluation of structurally diverse Amaryllidaceae alkaloids and their synthetic derivatives. Phytochem. Rev. 8, 449-459 (2009).
40. Takos, M. A., Rook, F. Towards a molecular understanding of the biosynthesis of amaryllidaceae alkaloids in support of their expanding medical use. Int. J. Mol. Sci. 14, 11713-11741 (2013).
41. Kornienko, A., Evidente, A. Chemistry, Biology, Medicinal Potential of Narciclasine and its Congeners. Chem. Rev 108, 1982-2014 (2008).
42. Marks, E. I. et al. Regorafenib with a fluoropyrimidine for metastatic colorectal cancer after progression on multiple 5-FUcontaining combination therapies and regorafenib monotherapy. Cancer Biol. Ther. 16, 1710-1719 (2015).
43. Launay, M. et al. Beating the odds: efficacy and toxicity of dihydropyrimidine dehydrogenase-driven adaptive dosing of 5-FU in patients with digestive cancer. Brit. J. Clin. Pharmaco. 81, 124-130 (2016).
44. Aklilu, M., Eng, C. The current landscape of locally advanced rectal cancer. Nat. Rev. Clin. Oncol. 8, 649-659 (2011).
45. Goietsenoven, V. G. et al. Amaryllidaceae Alkaloids Belonging to Different Structural Subgroups Display Activity against Apoptosis-Resistant Cancer Cells. J. Nat. Prod. 73, 1223-1227 (2010).
46. Boonsong, A. et al. Topoisomerase I protein expression in primary colorectal cancer and lymph node metastases. Hum. Pathol. 33, 1114-1119 (2002).
47. Griffin, C. et al. Selective cytotoxicity of pancratistatin-related natural Amaryllidaceae alkaloids: evaluation of the activity of two new compounds. Cancer. Cell. Int. 7, 10 (2007).
48. Djouina, M., Esquerre, N., Desreumaux, P., Vignal, C., Body-Malapel, M. Toxicological consequences of experimental exposure to aluminum in human intestinal epithelial cells. Food Chem. Toxicol. 91, 108-116 (2016).
49. Hajiaghaalipour, F., Kanthimathi, M. S., Sanusi, J., Rajarajeswaran, J. White tea (Camellia sinensis) inhibits proliferation of the colon cancer cell line, HT-29, activates caspases and protects DNA of normal cells against oxidative damage. Food Chem. 169, 401-410 (2015).
50. Zhang, H., Gu, Q., Liang, X., Pan, Y. J. Screening for topoisomerase I binding compounds by high-performance liquid chromatography-mass spectrometry. Anal. Biochem. 329, 173-179 (2004).
51. Mulabagal, V., Calderon, I. A. Development of an Ultrafiltration-Liquid Chromatography/Mass Spectrometry (UF-LC/MS) Based Ligand-Binding Assay and an LC/MS Based Functional Assay for Mycobacterium tuberculosis Shikimate Kinase. Anal. Chem. 82, 3616-3621 (2010).
52. Majumdar, P. et al. Design, synthesis and evaluation of thiohydantoin derivatives as potent topoisomerase I (Top1) inhibitors with anticancer activity. Eur. J. Med. Chem. 102, 540-551 (2015).