References
- Siegel RL, Miller KD, Jemal A. Cancer statistics, 2020. CA A Cancer J Clin. 2020; 70(1):7–30. doi:https://doi.org/10.3322/caac.21590
- Perez-Herrero E, Fernandez-Medarde A. Advanced targeted therapies in cancer: Drug nanocarriers, the future of chemotherapy. Eur J Pharm Biopharm. 2015; 93:52–79.
- Pan S-T, Li Z-L, He Z-X, Qiu J-X, Zhou S-F. Molecular mechanisms for tumour resistance to chemotherapy. Clin Exp Pharmacol Physiol. 2016; 43(8):723–37. doi:https://doi.org/10.1111/1440-1681.12581
- Cortes-Funes H, Coronado C. Role of anthracyclines in the era of targeted therapy. Cardiovasc Toxicol. 2007; 7(2):56–60. doi:https://doi.org/10.1007/s12012-007-0015-3
- Momparler RL, Karon M, Siegel SE, Avila F. Effect of adriamycin on DNA, RNA, and protein synthesis in cell-free systems and intact cells. Cancer Res. 1976; 36(8):2891–5.
- Wang S, Kotamraju S, Konorev E, Kalivendi S, Joseph J, Kalyanaraman B. Activation of nuclear factor-kappaB during doxorubicin-induced apoptosis in endothelial cells and myocytes is pro-apoptotic: the role of hydrogen peroxide. Biochem J. 2002; 367(Pt 3):729–40. doi:https://doi.org/10.1042/BJ20020752
- Chatterjee K, Zhang J, Honbo N, Karliner JS. Doxorubicin cardiomyopathy. Cardiology. 2010; 115(2):155–62. doi:https://doi.org/10.1159/000265166
- Dar AA, Arumugam N. Lignans of sesame: purification methods, biological activities and biosynthesis-a review. Bioorg Chem. 2013; 50:1–10. doi:https://doi.org/10.1016/j.bioorg.2013.06.009
- Khan S, Kumar A, Adhikari JS, Rizvi MA, Chaudhury NK. Protective effect of sesamol against 60Co γ-ray-induced hematopoietic and gastrointestinal injury in C57BL/6 male mice. Free Radic Res. 2015; 49(11):1344–61. doi:https://doi.org/10.3109/10715762.2015.1071485
- Wu X-L, Liou C-J, Li Z-Y, Lai X-Y, Fang L-W, Huang W-C. Sesamol suppresses the inflammatory response by inhibiting NF-κB/MAPK activation and upregulating AMP kinase signaling in RAW 264.7 macrophages. Inflamm Res. 2015; 64(8):577–88. doi:https://doi.org/10.1007/s00011-015-0836-7
- Chu P-Y, Srinivasan P, Deng J-F, Liu M-Y. Sesamol attenuates oxidative stress-mediated experimental acute pancreatitis in rats. Hum Exp Toxicol. 2012; 31(4):397–404. doi:https://doi.org/10.1177/0960327111426583
- Geetha T, Deol PK, Kaur IP. Role of sesamol-loaded floating beads in gastric cancers: a pharmacokinetic and biochemical evidence. J Microencapsul. 2015; 32(5):478–87.
- Kapadia GJ, Azuine MA, Tokuda H, Takasaki M, Mukainaka T, Konoshima T, Nishino H. Chemopreventive effect of resveratrol, sesamol, sesame oil and sunflower oil in the Epstein-Barr virus early antigen activation assay and the mouse skin two-stage carcinogenesis. Pharmacol Res. 2002; 45(6):499–505. doi:https://doi.org/10.1006/phrs.2002.0992
- Shimizu S, Ishigamori R, Fujii G, Takahashi M, Onuma W, Terasaki M, Yano T, Mutoh M. Involvement of NADPH oxidases in suppression of cyclooxygenase-2 promoter-dependent transcriptional activities by sesamol. J Clin Biochem Nutr. 2015; 56(2):118–22. doi:https://doi.org/10.3164/jcbn.14-89
- Leonard BC, Johnson DE. Signaling by cell surface death receptors: Alterations in head and neck cancer. Adv Biol Regul. 2018; 67:170–8. doi:https://doi.org/10.1016/j.jbior.2017.10.006
- Vanden Berghe T, Kaiser WJ, Bertrand MJ, Vandenabeele P. Molecular crosstalk between apoptosis, necroptosis, and survival signaling. Mol Cell Oncol. 2015; 2(4):e975093 doi:https://doi.org/10.4161/23723556.2014.975093
- Reed JC. Mechanisms of apoptosis. Am J Pathol. 2000; 157(5):1415–30. doi:https://doi.org/10.1016/S0002-9440(10)64779-7
- Hassan M, Watari H, AbuAlmaaty A, Ohba Y, Sakuragi N. Apoptosis and molecular targeting therapy in cancer. BioMed Res Int. 2014;2014:1–23. doi:https://doi.org/10.1155/2014/150845
- Lopez J, Tait S. Mitochondrial apoptosis: killing cancer using the enemy within. Br J Cancer. 2015; 112(6):957–62. doi:https://doi.org/10.1038/bjc.2015.85
- Zhang Y, Zhang B. TRAIL resistance of breast cancer cells is associated with constitutive endocytosis of death receptors 4 and 5. Mol Cancer Res. 2008; 6(12):1861–71. doi:https://doi.org/10.1158/1541-7786.MCR-08-0313
- El-Mesery M, Al-Gayyar M, Salem H, Darweish M, El-Mowafy A. Chemopreventive and renal protective effects for docosahexaenoic acid (DHA): implications of CRP and lipid peroxides. Cell Div. 2009; 4:6 doi:https://doi.org/10.1186/1747-1028-4-6
- Devi PU, Rao BS, Solomon FE. Effect of plumbagin on the radiation induced cytogenetic and cell cycle changes in mouse Ehrlich ascites carcinoma in vivo. Indian J Exp Biol. 1998; 36(9):891–5.
- Sathisha MP, Revankar VK, Pai KS. Synthesis, structure, electrochemistry, and spectral characterization of bis-isatin thiocarbohydrazone metal complexes and their antitumor activity against ehrlich ascites carcinoma in swiss albino mice. Met Based Drugs. 2008; 2008: :362105 doi:https://doi.org/10.1155/2008/362105
- Hemalatha G, Pugalendi KV, Saravanan R. Modulatory effect of sesamol on DOCA-salt-induced oxidative stress in uninephrectomized hypertensive rats. Mol Cell Biochem. 2013; 379(1–2):255–65. doi:https://doi.org/10.1007/s11010-013-1647-1
- Awara WM, El-Sisi AE, El-Sayad ME, Goda AE. The potential role of cyclooxygenase-2 inhibitors in the treatment of experimentally-induced mammary tumour: does celecoxib enhance the anti-tumour activity of doxorubicin? Pharmacol Res. 2004; 50(5):487–98. doi:https://doi.org/10.1016/j.phrs.2004.04.002
- Schirner M, Hoffmann J, Menrad A, Schneider MR. Antiangiogenic chemotherapeutic agents: characterization in comparison to their tumor growth inhibition in human renal cell carcinoma models. Clin Cancer Res. 1998; 4(5):1331–6.
- Agrawal SS, Saraswati S, Mathur R, Pandey M. Antitumor properties of Boswellic acid against Ehrlich ascites cells bearing mouse. Food Chem Toxicol. 2011; 49(9):1924–34. doi:https://doi.org/10.1016/j.fct.2011.04.007
- Goel MK, Khanna P, Kishore J. Understanding survival analysis: Kaplan-Meier estimate. Int J Ayurveda Res. 2010; 1(4):274–8. doi:https://doi.org/10.4103/0974-7788.76794
- Evans T. Chemotherapy in advanced non-small cell lung cancer. Semin Respir Crit Care Med. 2005; 26(3):304–13. doi:https://doi.org/10.1055/s-2005-871989
- Hill GW, Morest DK, Parham K. Cisplatin-induced ototoxicity: effect of intratympanic dexamethasone injections. Otology & Neurotology: official Publication of the American Otological Society, American Neurotology Society [and] European Academy of Otology and Neurotology. 2008; 29(7):1005.
- Petrylak DP. The current role of chemotherapy in metastatic hormone-refractory prostate cancer. Urology. 2005; 65(5 Suppl):3–7. doi:https://doi.org/10.1016/j.urology.2005.03.053
- Bishayee A, Sethi G. Bioactive natural products in cancer prevention and therapy: Progress and promise. Semin Cancer Biol. 2016; 40-41:1–3. doi:https://doi.org/10.1016/j.semcancer.2016.08.006
- Baritaki S, Militello L, Malaponte G, Spandidos DA, Salcedo M, Bonavida B. The anti-CD20 mAb LFB-R603 interrupts the dysregulated NF-κB/Snail/RKIP/PTEN resistance loop in B-NHL cells: role in sensitization to TRAIL apoptosis. Int J Oncol. 2011; 38(6):1683–94. doi:https://doi.org/10.3892/ijo.2011.984
- Pfeffer C, Singh A. Apoptosis: a target for anticancer therapy. Int J Mol Sci. 2018; 19(2):448.
- Wong RS. Apoptosis in cancer: from pathogenesis to treatment. J Exp Clin Cancer Res. 2011; 30:87. [Database] doi:https://doi.org/10.1186/1756-9966-30-87
- Elrod HA, Sun SY. Modulation of death receptors by cancer therapeutic agents. Cancer Biol Ther. 2008; 7(2):163–73. doi:https://doi.org/10.4161/cbt.7.2.5335
- Hata AN, Engelman JA, Faber AC. The BCL2 Family: Key Mediators of the Apoptotic Response to Targeted Anticancer Therapeutics. Cancer Discov. 2015; 5(5):475–87. doi:https://doi.org/10.1158/2159-8290.CD-15-0011
- Ozoren N, El-Deiry WS. Cell surface Death Receptor signaling in normal and cancer cells. Semin Cancer Biol. 2003; 13(2):135–47. doi:https://doi.org/10.1016/S1044-579X(02)00131-1
- Yip KW, Reed JC. Bcl-2 family proteins and cancer. Oncogene. 2008; 27(50):6398–406. doi:https://doi.org/10.1038/onc.2008.307
- El-Mesery M, Shaker ME, Elgaml A. The SMAC mimetic BV6 induces cell death and sensitizes different cell lines to TNF-α and TRAIL-induced apoptosis . Exp Biol Med (Maywood)). 2016; 241(18):2015–22. doi:https://doi.org/10.1177/1535370216661779
- Scheurer M, Brands R, El-Mesery M, Hartmann S, Müller-Richter U, Kübler A, Seher A. The Selection of NFκB Inhibitors to Block Inflammation and Induce Sensitisation to FasL-Induced Apoptosis in HNSCC Cell Lines Is Critical for Their Use as a Prospective Cancer Therapy. IJMS. 2019; 20(6):1306. doi:https://doi.org/10.3390/ijms20061306
- El-Mesery M, Rosenthal T, Rauert-Wunderlich H, Schreder M, Stühmer T, Leich E, Schlosser A, Ehrenschwender M, Wajant H, Siegmund D, et al. The NEDD8-activating enzyme inhibitor MLN4924 sensitizes a TNFR1+ subgroup of multiple myeloma cells for TNF-induced cell death. Cell Death Dis. 2019; 10(8):1–15. doi:https://doi.org/10.1038/s41419-019-1860-2
- Mahmood Z, Shukla Y. Death receptors: targets for cancer therapy. Exp Cell Res. 2010; 316(6):887–99. doi:https://doi.org/10.1016/j.yexcr.2009.12.011
- Lavrik I, Golks A, Krammer PH. Death receptor signaling. J Cell Sci. 2005; 118(Pt 2):265–7. doi:https://doi.org/10.1242/jcs.01610
- Elmore S. Apoptosis: a review of programmed cell death. Toxicol Pathol. 2007; 35(4):495–516. doi:https://doi.org/10.1080/01926230701320337
- El-Mesery M, Trebing J, Schäfer V, Weisenberger D, Siegmund D, Wajant H. CD40-directed scFv-TRAIL fusion proteins induce CD40-restricted tumor cell death and activate dendritic cells. Cell Death Dis. 2013; 4:e916 doi:https://doi.org/10.1038/cddis.2013.402
- Li H, Zhu H, Xu CJ, Yuan J. Cleavage of BID by caspase 8 mediates the mitochondrial damage in the Fas pathway of apoptosis. Cell. 1998; 94(4):491–501. doi:https://doi.org/10.1016/s0092-8674(00)81590-1
- Luo X, Budihardjo I, Zou H, Slaughter C, Wang X. Bid, a Bcl2 interacting protein, mediates cytochrome c release from mitochondria in response to activation of cell surface death receptors. Cell. 1998; 94(4):481–90. doi:https://doi.org/10.1016/S0092-8674(00)81589-5
- Kluck RM, Bossy-Wetzel E, Green DR, Newmeyer DD. The release of cytochrome c from mitochondria: a primary site for Bcl-2 regulation of apoptosis. Science. 1997; 275(5303):1132–6. doi:https://doi.org/10.1126/science.275.5303.1132
- Danial NN, Korsmeyer SJ. Cell death: critical control points. Cell. 2004; 116(2):205–19. doi:https://doi.org/10.1016/S0092-8674(04)00046-7
- Saelens X, Festjens N, Vande Walle L, van Gurp M, van Loo G, Vandenabeele P. Toxic proteins released from mitochondria in cell death. Oncogene. 2004; 23(16):2861–74. doi:https://doi.org/10.1038/sj.onc.1207523
- Allin KH, Nordestgaard BG, Flyger H, Bojesen SE. Elevated pre-treatment levels of plasma C-reactive protein are associated with poor prognosis after breast cancer: a cohort study. Breast Cancer Res. 2011; 13(3):R55. doi:https://doi.org/10.1186/bcr2891
- Gabay C, Kushner I. Acute-phase proteins and other systemic responses to inflammation. N Engl J Med. 1999; 340(6):448–54. doi:https://doi.org/10.1056/NEJM199902113400607
- Chandrashekara S. C-reactive protein: An inflammatory marker with specific role in physiology, pathology, and diagnosis. IJRCI. 2014; 2(S1):SR3. doi:https://doi.org/10.15305/ijrci/v2iS1/117
- Ansar W, Ghosh S. C-reactive protein and the biology of disease. Immunol Res. 2013; 56(1):131–42. doi:https://doi.org/10.1007/s12026-013-8384-0
- Allin KH, Bojesen SE, Nordestgaard BG. Baseline C-reactive protein is associated with incident cancer and survival in patients with cancer. J Clin Oncol. 2009; 27(13):2217–24. doi:https://doi.org/10.1200/JCO.2008.19.8440
- Gunter MJ, Stolzenberg-Solomon R, Cross AJ, Leitzmann MF, Weinstein S, Wood RJ, Virtamo J, Taylor PR, Albanes D, Sinha R, et al. A prospective study of serum C-reactive protein and colorectal cancer risk in men. Cancer Res. 2006; 66(4):2483–7. doi:https://doi.org/10.1158/0008-5472.CAN-05-3631
- El-Mowafy AM, El-Mesery ME, Salem HA, Al-Gayyar MM, Darweish MM. Prominent chemopreventive and chemoenhancing effects for resveratrol: unraveling molecular targets and the role of C-reactive protein. Chemotherapy. 2010; 56(1):60–5. doi:https://doi.org/10.1159/000298821
- Said UZ, et al. Effects of omega-3 fatty acids against Ehrlich carcinoma-induced hepatic dysfunction. Journal of Cancer Research and Experimental Oncology. 2014; 6(2):20–8.
- Waris G, Ahsan H. Reactive oxygen species: role in the development of cancer and various chronic conditions. J Carcinog. 2006; 5:14 doi:https://doi.org/10.1186/1477-3163-5-14
- Tsikas D. Assessment of lipid peroxidation by measuring malondialdehyde (MDA) and relatives in biological samples: Analytical and biological challenges. Anal Biochem. 2017; 524:13–30. doi:https://doi.org/10.1016/j.ab.2016.10.021
- Qin X-J, He W, Hai C-X, Liang X, Liu R. Protection of multiple antioxidants Chinese herbal medicine on the oxidative stress induced by adriamycin chemotherapy. J Appl Toxicol. 2008; 28(3):271–82. doi:https://doi.org/10.1002/jat.1276
- Minotti G, Menna P, Salvatorelli E, Cairo G, Gianni L. Anthracyclines: molecular advances and pharmacologic developments in antitumor activity and cardiotoxicity. Pharmacol Rev. 2004; 56(2):185–229. doi:https://doi.org/10.1124/pr.56.2.6
- Petrioli R, Fiaschi AI, Francini E, Pascucci A, Francini G. The role of doxorubicin and epirubicin in the treatment of patients with metastatic hormone-refractory prostate cancer. Cancer Treat Rev. 2008; 34(8):710–8. doi:https://doi.org/10.1016/j.ctrv.2008.05.004
- Tacar O, Sriamornsak P, Dass CR. Doxorubicin: an update on anticancer molecular action, toxicity and novel drug delivery systems. J Pharm Pharmacol. 2013; 65(2):157–70. doi:https://doi.org/10.1111/j.2042-7158.2012.01567.x
- Carvalho C, Santos RX, Cardoso S, Correia S, Oliveira PJ, Santos MS, Moreira PI. Doxorubicin: the good, the bad and the ugly effect. Curr Med Chem. 2009; 16(25):3267–85. doi:https://doi.org/10.2174/092986709788803312
- Takemura G, Fujiwara H. Doxorubicin-induced cardiomyopathy from the cardiotoxic mechanisms to management. Prog Cardiovasc Dis. 2007; 49(5):330–52. doi:https://doi.org/10.1016/j.pcad.2006.10.002
- Abd Elrazik NA, El-Mesery M, El-Karef A, Eissa LA, El Gayar AM. Chlorogenic acid potentiates antitumor effect of doxorubicin through upregulation of death receptors in solid Ehrlich carcinoma model in mice. Egyptian Journal of Basic and Applied Sciences. 2019;6(1):158–15. doi:https://doi.org/10.1080/2314808X.2019.1682331
- Swamy AV, Gulliaya S, Thippeswamy A, Koti BC, Manjula DV. Cardioprotective effect of curcumin against doxorubicin-induced myocardial toxicity in albino rats. Indian J Pharmacol. 2012; 44(1):73–7. doi:https://doi.org/10.4103/0253-7613.91871
- Helmy S A, El-Mesery M, El-Karef A, Eissa L A, El Gayar A M. Chloroquine upregulates TRAIL/TRAILR2 expression and potentiates doxorubicin anti-tumor activity in thioacetamide-induced hepatocellular carcinoma model. Chem Biol Interact. 2018;279:84–94. doi:https://doi.org/10.1016/j.cbi.2017.11.009. 29133031
- Shaker M E, Shaaban A A, El-Shafey M M, El-Mesery M E. The selective c-Met inhibitor capmatinib offsets cisplatin-nephrotoxicity and doxorubicin-cardiotoxicity and improves their anticancer efficacies. Toxicol Appl Pharmacol. 2020;398:115018 doi:https://doi.org/10.1016/j.taap.2020.115018. PMC: 32333917
- Octavia Y, Tocchetti CG, Gabrielson KL, Janssens S, Crijns HJ, Moens AL. Doxorubicin-induced cardiomyopathy: from molecular mechanisms to therapeutic strategies. J Mol Cell Cardiol. 2012; 52(6):1213–25. doi:https://doi.org/10.1016/j.yjmcc.2012.03.006
- Pecoraro M, Del Pizzo M, Marzocco S, Sorrentino R, Ciccarelli M, Iaccarino G, Pinto A, Popolo A. Inflammatory mediators in a short-time mouse model of doxorubicin-induced cardiotoxicity. Toxicol Appl Pharmacol. 2016; 293:44–52. doi:https://doi.org/10.1016/j.taap.2016.01.006