Compuestos citotóxicos de origen vegetal y su relación con proteínas inhibidoras de apoptosis (IAP)

Lee KH. Discovery and development of natural product-derived chemotherapeutic agents based on a medicinal chemistry approach. J Nat Prod. 2010;73(3):500-16.

https://doi.org/10.1021/np900821e

Dobbelstein M, Moll U. Targeting tumour-supportive cellular machineries in anticancer drug development. Nat Rev Drug Discov. 2014;13(3):179-96.

https://doi.org/10.1038/nrd4201

Fu H, He J, Mei F, Zhang Q, Hara Y, Ryota S, et al. Lung cancer inhibitory effect of epigallocatechin-3-gallate is dependent on its presence in a complex mixture (polyphenon E). Cancer Prev Res(Phila). 2009;2(6):531-7.

https://doi.org/10.1158/1940-6207.CAPR-08-0185

WHO. World Cancer Report 2014. Lyon (France): International Agency for Research on Cancer; 2014.

Huryn DM, Wipf P. Natural product chemistry and anticancer drug discovery. Cancer Drug Design and Discovery. New York: Academic Press; 2008. p. 107-30.

https://doi.org/10.1016/B978-012369448-5.50008-2

Mazzio E, Soliman K. In vitro screening for the tumoricidal properties of international medicinal herbs. Phytother Res. 2009;23(3):385-98.

https://doi.org/10.1002/ptr.2636

Appendino G, Fontana G, Pollastro F, Lew M, Hung-Wen L. Natural Products Drug Discovery. Comprehensive Natural Products II. Oxford: Elsevier; 2010. p. 205-36.

https://doi.org/10.1016/B978-008045382-8.00064-2

Gyrd-Hansen M, Meier P. IAPs: from caspase inhibitors to modulators of NF- B, inflammation and cancer. Nat Rev Cancer. 2010;10(8):561-74.

https://doi.org/10.1038/nrc2889

Dong FY, Jiang RW. Research progress of the natural products against prostate cancer. Chinese Journal of Natural Medicines. 2011;9(2):81-9.

Cragg GM, Newman DJ. Natural products: A continuing source of novel drug leads. Biochim Biophys Acta. 2013;1830(6):3670-95.

https://doi.org/10.1016/j.bbagen.2013.02.008

Calvert H. Cancer Drug Design and Discovery. En: Neidle S, editor. Cancer Drug Design and Discovery. Second Edition San Diego: Academic Press; 2014. p. 371.

https://doi.org/10.1016/B978-0-12-396521-9.06001-0

Cragg GM, Grothaus PG, Newman DJ. Impact of natural products on developing new anti-cancer agents. Chem Rev. 2009;109(7):3012-43.

https://doi.org/10.1021/cr900019j

Newman DJ, Cragg GM. Natural products as sources of new drugs over the last 25 years. J Nat Prod. 2007;70(3):461-77.

https://doi.org/10.1021/np068054v

Newman DJ, Cragg GM. Natural products as sources of new drugs over the 30 years from 1981 to 2010. J Nat Prod. 2012;75(3):311-35.

https://doi.org/10.1021/np200906s

Rabbani-Chadegani A, Chamani E, Hajihassan Z. The effect of vinca alkaloid anticancer drug, vinorelbine, on chromatin and histone proteins in solution. Eur J Pharmacol. 2009;613(1-3):34-8.

https://doi.org/10.1016/j.ejphar.2009.04.040

Hitt E. Homoharringtonine effective in CML patients. Lancet Oncol. 2002;3(5):259.

https://doi.org/10.1016/S1470-2045(02)00740-4

Cragg GM, Kingston D, Newman DJ. Anticancer Agents from Natural Products. London. 2005.

https://doi.org/10.1201/9781420039658

Barbosa EG, Bega LA, Beatriz A, Sarkar T, Hamel E, do Amaral MS, et al. A diaryl sulfide, sulfoxide, and sulfone bearing structural similarities to combretastatin A-4. Eur J Med Chem. 2009;44(6):2685-8.

https://doi.org/10.1016/j.ejmech.2008.12.018

Gioti K, Tenta R. Bioactive Natural Products against Prostate Cancer: Mechanism of Action and Autophagic/Apoptotic Molecular Pathways. Planta Med. 2015;81(7):543-62.

https://doi.org/10.1055/s-0035-1545845

Singh M, Kaur M, Silakari O. Flavones: An important scaffold for medicinal chemistry. Eur J Med Chem. 2014;84(0):206-39.

https://doi.org/10.1016/j.ejmech.2014.07.013

Alvarez EA, Wolfson AH, Pearson JM, Crisp MP, Mendez LE, Lambrou NC, et al. A phase I study of docetaxel as a radio-sensitizer for locally advanced squamous cell cervical cancer. Gynecol Oncol. 2009;113(2):195-9.

https://doi.org/10.1016/j.ygyno.2008.12.033

Biganzoli L, Licitra S, Moretti E, Pestrin M, Zafarana E, Di Leo A. Taxanes in the elderly: Can we gain as much and be less toxic? Crit Rev Oncol Hematol. 2009;70(3):262-71.

https://doi.org/10.1016/j.critrevonc.2008.07.017

Kingston DG. A natural love of natural products. J Org Chem. 2008;73(11):3975-84.

https://doi.org/10.1021/jo800239a

Shah U, Shah R, Acharya S, Acharya N. Novel anticancer agents from plant sources. Chinese Journal of Natural Medicines. 2013;11(1):16-23.

https://doi.org/10.1016/S1875-5364(13)60002-3

Khazir J, Mir BA, Pilcher L, Riley DL. Role of plants in anticancer drug discovery. Phytochemistry Letters. 2014;7(0):173-81.

https://doi.org/10.1016/j.phytol.2013.11.010

McLaughlin JL. Paw paw and cancer: annonaceous acetogenins from discovery to commercial products. J Natural Prod. 2008;71(7):1311-21.

https://doi.org/10.1021/np800191t

Coothankandaswamy V, Liu Y, Mao SC, Morgan JB, Mahdi F, Jekabsons MB, et al. The alternative medicine pawpaw and its acetogenin constituents suppress tumor angiogenesis via the HIF-1/VEGF pathway. J Nat Prod. 2010;73(5):956-61.

https://doi.org/10.1021/np100228d

Paramasivam A, Sambantham S, Shabnam J, Raghunandhakumar S, Anandan B, Rajiv R, et al. Anti-cancer effects of thymoquinone in mouse neuroblastoma (Neuro-2a) cells through caspase-3 activation with down-regulation of XIAP. Toxicol Lett. 2012;213(2):151-9.

https://doi.org/10.1016/j.toxlet.2012.06.011

Nobili S, Lippi D,Witort E, Donnini M, Bausi L, Mini E, et al. Natural compounds for cancer treatment and prevention. Pharmacol Res. 2009;59(6):365-78.

https://doi.org/10.1016/j.phrs.2009.01.017

NCI. Developmental Therapeutics Program 2014 [consulta el 28 de noviembre de 2014]. Disponible en: http://dtp.nci.nih.gov/dtpstandard/servlet/dwindex?searchtype=NSC&chemnameboolean=and&outputformat=html&searchlist=295156&Submit=Submit:

NCI. Developmental Therapeutics Program 2014 [consulta el 29 de noviembre de 2014]. Disponible en: http://dtp.nci.nih.gov/tpstandard/servlet/dwindex?searchtype=NSC&chemnameboolean=and&outputformat=html&searchlist=698249&Submit=Submit:

Nagaraju GP, Zhu S, Ko JE, Ashritha N, Kandimalla R, Snyder JP, et al. Antiangiogenic effects of a novel synthetic curcumin analogue in pancreatic cancer. Cancer Lett. 2015;357(2):557-65.

https://doi.org/10.1016/j.canlet.2014.12.007

Ferreira AK, de-Sá-Júnior PL, Pasqualoto KFM, de Azevedo RA, Câmara DAD, Costa AS, et al. Cytotoxic effects of dillapiole on MDA-MB-231 cells involve the induction of apoptosis through the mitochondrial pathway by inducing an oxidative stress while altering the cytoskeleton network. Biochimie. 2014;99(0):195-207.

https://doi.org/10.1016/j.biochi.2013.12.008

Greenshields AL, Doucette CD, Sutton KM, Madera L, Annan H, Yaffe PB, et al. Piperine inhibits the growth and motility of triple-negative breast cancer cells. Cancer Lett. 2015;357(1):129-40.

https://doi.org/10.1016/j.canlet.2014.11.017

Bezerra DP, Pessoa C, de Moraes MO, Saker-Neto N, Silveira ER, Costa-Lotufo LV. Overview of the therapeutic potential of piplartine (piperlongumine). Eur J Pharm Sci. 2013;48(3): 453-63.

https://doi.org/10.1016/j.ejps.2012.12.003

Li S, Lei Y, Jia Y, Li N, Wink M, Ma Y. Piperine, a piperidine alkaloid from Piper nigrum re-sensitizes P-gp, MRP1 and BCRP dependent multidrug resistant cancer cells. Phytomedicine. 2011;19(1):83-7.

https://doi.org/10.1016/j.phymed.2011.06.031

Raj L, Ide T, Gurkar AU, Foley M, Schenone M, Li X, et al. Selective killing of cancer cells by a small molecule targeting the stress response to ROS. Nature. 2011;475(7355):231-4.

https://doi.org/10.1038/nature10167

Rao CV, Kurkjian CD, Yamada HY. Mitosis-targeting natural products for cancer prevention and therapy. Curr Drug Targets. 2012;13(14):1820-30.

https://doi.org/10.2174/138945012804545533

Pommier Y, Leo E, Zhang H, Marchand C. DNA Topoisomerases and their poisoning by anticancer and antibacterial drugs. Chem Biol. 2010;17(5):421-33.

https://doi.org/10.1016/j.chembiol.2010.04.012

Bailly C. Contemporary challenges in the design of topoisomerase II inhibitors for cancer chemotherapy. Chem Rev. 2012;112(7):3611-40.

https://doi.org/10.1021/cr200325f

Negi AS, Gautam Y, Alam S, Chanda D, Luqman S, Sarkar J, et al. Natural antitubulin agents: importance of 3,4,5-trimethoxyphenyl fragment. Bioorg Med Chem. 2015;23(3):373-89.

https://doi.org/10.1016/j.bmc.2014.12.027

Chaplin DJ, Hill SA. The development of combretastatin A4 phosphate as a vascular targeting agent. Int J Radiat Oncol Biol Phys. 2002;54(5):1491-6.

https://doi.org/10.1016/S0360-3016(02)03924-X

Patterson DM, Rustin GJ. Vascular damaging agents. Clin Oncol. 2007;19(6):443-56.

https://doi.org/10.1016/j.clon.2007.03.014

Lippert JW 3rd. Vascular disrupting agents. Bioorg Med Chem. 2007;15(2):605-15.

https://doi.org/10.1016/j.bmc.2006.10.020

Yang T, Wang Y, Li Z, Dai W, Yin J, Liang L, et al. Targeted delivery of a combination therapy consisting of combretastatin A4 and low-dose doxorubicin against tumor neovasculature. Nanomedicine: Nanomedicine. 2012;8(1):81-92.

https://doi.org/10.1016/j.nano.2011.05.003

Siemann DW. The unique characteristics of tumor vasculature and preclinical evidence for its selective disruption by Tumor- Vascular Disrupting Agents. Cancer Treat Rev. 2011;37(1):63-74.

https://doi.org/10.1016/j.ctrv.2010.05.001

Hinnen P, Eskens FALM. Vascular disrupting agents in clinical development. Br J Cancer. 2007;96(8):1159-65.

https://doi.org/10.1038/sj.bjc.6603694

Wu XY, Ma W, Gurung K, Guo CH. Mechanisms of tumor resistance to small-molecule vascular disrupting agents: treatment and rationale of combination therapy. J Formos Med Assoc. 2013;112(3):115-24.

https://doi.org/10.1016/j.jfma.2012.09.017

Patil SA, Patil R, Pfeffer LM, Miller DD. Chromenes: potential new chemotherapeutic agents for cancer. Future Med Chem. 2013;5(14):1647-60.

https://doi.org/10.4155/fmc.13.126

Mooney CJ, Nagaiah G, Fu P, Wasman JK, Cooney MM, Savvides PS, et al. A phase II trial of fosbretabulin in advanced anaplastic thyroid carcinoma and correlation of baseline serum-soluble intracellular adhesion molecule-1 with outcome. Thyroid. 2009;19(3):233-40.

https://doi.org/10.1089/thy.2008.0321

Oxigene. http://www.oxigene.com: Oxigene; 2014 [consulta el 4 de junio de 2015]. Disponible en: http://www.oxigene.com/product-development

Fulda S. Inhibitor of Apoptosis (IAP) proteins as therapeutic targets for radiosensitization of human cancers. Cancer Treat Rev. 2012;38(6):760-6.

https://doi.org/10.1016/j.ctrv.2012.01.005

Dai Y, Desano J, Qu Y, Tang W, Meng Y, Lawrence TS, et al. Natural IAP inhibitor Embelin enhances therapeutic efficacy of ionizing radiation in prostate cancer. Am J Cancer Res. 2011;1(2):128-43.

Cheng YJ, Jiang HS, Hsu SL, Lin LC, Wu CL, Ghanta VK, et al. XIAP-mediated protection of H460 lung cancer cells against cisplatin. Eur J Pharmacol. 2010;627(1-3):75-84.

https://doi.org/10.1016/j.ejphar.2009.11.003

Szakács G, Paterson JK, Ludwig JA, Booth-Genthe C, Gottesman MM. Targeting multidrug resistance in cancer. Nat Rev Drug Dis. 2006;5(3):219-34.

https://doi.org/10.1038/nrd1984

Dynek JN, Vucic D. Antagonists of IAP proteins as cancer therapeutics. Cancer Lett. 2013;332(2):206-14.

https://doi.org/10.1016/j.canlet.2010.06.013

Creagh EM. Caspase crosstalk: integration of apoptotic and innate immune signalling pathways. Trends Immunol. 2014;35(12):631-40.

https://doi.org/10.1016/j.it.2014.10.004

Rojas M, Salmen S, Berrueta L. Muerte celular programada: I. Activación y mecanismos de regulación. Revista Médica de la Extensión Portuguesa. 2009;4(3):92-106.

Radogna F, Dicato M, Diederich M. Cancer-type-specific crosstalk between autophagy, necroptosis and apoptosis as a pharmacological target. Biochem Pharmacol. 2015;94(1):1-11.

https://doi.org/10.1016/j.bcp.2014.12.018

Fulda S, Debatin KM. Extrinsic versus intrinsic apoptosis pathways in anticancer chemotherapy. Oncogene. 2006;25(34):4798-811.

https://doi.org/10.1038/sj.onc.1209608

Igney FH, Krammer PH. Death and anti-death: tumour resistance to apoptosis. Nat Rev Cancer. 2002;2(4):277-88.

https://doi.org/10.1038/nrc776

LaCasse EC, Mahoney DJ, Cheung HH, Plenchette S, Baird S, Korneluk RG. IAP-targeted therapies for cancer. Oncogene. 2008;27(48):6252-75.

https://doi.org/10.1038/onc.2008.302

Mannhold R, Fulda S, Carosati E. IAP antagonists: promising candidates for cancer therapy. Drug Discov Today. 2010;15(5-6):210-9.

https://doi.org/10.1016/j.drudis.2010.01.003

Fulda S, Vucic D. Targeting IAP proteins for therapeutic intervention in cancer. Nat Rev Drug Discov. 2012;11(4):331.

https://doi.org/10.1038/nrd3698

Lukacs C, Belunis C, Crowther R, Danho W, Gao L, Goggin B, et al. The structure of XIAP BIR2: understanding the selectivity of the BIR domains. Acta Crystallogr Section D Biol Crystallogr. 2013;69 Pt 9:1717-25.

https://doi.org/10.1107/S0907444913016284

Wu G, Chai J, Suber TL, Wu JW, Du C, Wang X, et al. Structural basis of IAP recognition by Smac/DIABLO. Nature. 2000;408(6815):1008-12.

https://doi.org/10.1038/35050012

Shi Y. A conserved tetrapeptide motif: potentiating apoptosis through IAP-binding. Cell Death Differ. 2002;9(2), 93-35.

https://doi.org/10.1038/sj.cdd.4400957

Riedl SJ, Shi Y. Molecular mechanisms of caspase regulation during apoptosis. Nat Rev Mol Cell Biol. 2004;5(11):897-907.

https://doi.org/10.1038/nrm1496

Hunter AM, LaCasse EC, Korneluk RG. The inhibitors of apoptosis (IAPs) as cancer targets. Apoptosis. 2007;12(9):1543-68.

https://doi.org/10.1007/s10495-007-0087-3

Elsawy MA, Martin L, Tikhonova IG, Walker B. Solid phase synthesis of Smac/DIABLO-derived peptides using a 'Safety-Catch' resin: Identification of potent XIAP BIR3 antagonists. Bioorg Med Chem. 2013;21(17):5004-11.

https://doi.org/10.1016/j.bmc.2013.06.055

Fulda S. Smac mimetics as IAP antagonists. Semin Cell Dev Biol. 2015;39:132-8.

https://doi.org/10.1016/j.semcdb.2014.12.005

Kim KS, Zhang L, Williams D, Perez HL, Stang E, Borzilleri RM, et al. Discovery of tetrahydroisoquinoline-based bivalent heterodimeric IAP antagonists. Bioorg Med Chem Lett. 2014;24(21):5022-9.

https://doi.org/10.1016/j.bmcl.2014.09.022

Sun H, Nikolovska-Coleska Z, Yang C-Y, Qian D, Lu J, Qiu S, et al. Design of small-molecule peptidic and non-peptidic smac mimetics. Acc Chem Res. 2008;41(10):1264-77.

https://doi.org/10.1021/ar8000553

Chessari G, Buck IM, Day JE, Day PJ, Iqbal A, Johnson CN, et al. Fragment-Based Drug Discovery Targeting Inhibitor of Apoptosis Proteins: Discovery of a Non-Alanine Lead Series with Dual Activity Against cIAP1 and XIAP. J Med Chem. 2015;58(16): 6574-88.

https://doi.org/10.1021/acs.jmedchem.5b00706

Nikolovska-Coleska Z, Xu L, Hu Z, Tomita Y, Li P, Roller PP, et al. Discovery of embelin as a cell-permeable, small-molecular weight inhibitor of XIAP through structure-based computational screening of a traditional herbal medicine three-dimensional structure database. J Med Chem. 2004;47(10):2430-40.

https://doi.org/10.1021/jm030420+

Chen J, Nikolovska-Coleska Z, Wang G, Qiu S, Wang S. Design, synthesis, and characterization of new embelin derivatives as potent inhibitors of X-linked inhibitor of apoptosis protein. Bioorg Med Chem Lett. 2006;16(22):5805-8.

https://doi.org/10.1016/j.bmcl.2006.08.072

Poojari R. Embelin - a drug of antiquity: shifting the paradigm towards modern medicine. Expert Opinion on Investigational Drugs. 2014;23(3):427-44.

https://doi.org/10.1517/13543784.2014.867016

Singh B, Guru SK, Sharma R, Bharate SS, Khan IA, Bhushan S, et al. Synthesis and anti-proliferative activities of new derivatives of embelin. Bioorg Med Chem Lett. 2014;24(20):4865-70.

https://doi.org/10.1016/j.bmcl.2014.08.052

Cragg GM, Grothaus PG, Newman DJ. New Horizons for old drugs and drug leads. J Nat Prod. 2014;77(3):703-23.

https://doi.org/10.1021/np5000796

Hong Y, Sengupta S, Hur W, Sim T. Identification of novel ROS inducers: quinone derivatives tethered to long hydrocarbon chains. J Med Chem. 2015;58(9):3739-50.

https://doi.org/10.1021/jm501846y