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Biotoxins for Cancer Therapy

  • Liu, Cui-Cui (Department of Scientific Research, Hong Hui Hospital, Xi'an Jiaotong University College of Medicine) ;
  • Yang, Hao (Department of Scientific Research, Hong Hui Hospital, Xi'an Jiaotong University College of Medicine) ;
  • Zhang, Ling-Ling (Department of Scientific Research, Hong Hui Hospital, Xi'an Jiaotong University College of Medicine) ;
  • Zhang, Qian (Department of Scientific Research, Hong Hui Hospital, Xi'an Jiaotong University College of Medicine) ;
  • Chen, Bo (Department of Scientific Research, Hong Hui Hospital, Xi'an Jiaotong University College of Medicine) ;
  • Wang, Yi (Department of Scientific Research, Hong Hui Hospital, Xi'an Jiaotong University College of Medicine)
  • Published : 2014.06.30

Abstract

In recent times, a number of studies have provided evidence that biotoxins present great potential as antitumor agents, such as snake venom, bee venom, some bacteria toxins and plant toxins, and thus could be used as chemotherapeutic agents against tumors. The biodiversity of venoms and toxins make them a unique source from which novel anticancer agent may be developed. Biotoxins, also known as natural toxins, include toxic substances produced by plants, animals and microorganisms. Here, we systematically list representative biological toxins that have antitumor properties, involving animal toxins, plant toxins, mycotoxins as well as bacterial toxins. In this review, we summarize the current knowledge involving biotoxins and the active compounds that have anti-cancer activity to induce cytotoxic, antitumor, immunomodulatory, and apoptotic effects in different tumor cells in vivo or in vitro. We also show insights into the molecular and functional evolution of biotoxins.

Keywords

References

  1. Al-Sadoon MK, Rabah DM, Badr G (2013). Enhanced anticancer efficacy of snake venom combined with silica nanoparticles in a murine model of human multiple myeloma: molecular targets for cell cycle arrest and apoptosis induction. Cell Immunol, 284, 129-38. https://doi.org/10.1016/j.cellimm.2013.07.016
  2. Bachran C, Morley T, Abdelazim S, et al (2013). Anthrax toxinmediated delivery of the Pseudomonas exotoxin A enzymatic domain to the cytosol of tumor cells via cleavable ubiquitin fusions. MBio, 4, e00201-13.
  3. Badr G, Al-Sadoon MK, Rabah DM, et al (2013). Snake (Walterinnesia aegyptia) venom-loaded silica nanoparticles induce apoptosis and growth arrest in human prostate cancer cells. Apoptosis, 18, 300-14. https://doi.org/10.1007/s10495-012-0787-1
  4. Balamurugan E, Reddy BV, Menon VP (2010). Antitumor and antioxidant role of Chrysaora quinquecirrha (sea nettle) nematocyst venom peptide against Ehrlich ascites carcinoma in Swiss Albino mice. Mol Cell Biochem, 338, 69-76. https://doi.org/10.1007/s11010-009-0339-3
  5. Bandala C, Perez-Santos JL, Lara-Padilla E, et al (2013). Effect of botulinum toxin A on proliferation and apoptosis in the T47D breast cancer cell line. Asian Pac J Cancer Prev, 14 , 891-4. https://doi.org/10.7314/APJCP.2013.14.2.891
  6. Baskar R, Lee KA, Yeo R, et al (2012). Cancer and radiation therapy: current advances and future directions. Int J Med Sci, 9, 193-9. https://doi.org/10.7150/ijms.3635
  7. Bowen CV, DeBay D, Ewart HS, et al (2013). In vivo detection of human TRPV6-rich tumors with anti-cancer peptides derived from soricidin. PLoS One, 8, e58866. https://doi.org/10.1371/journal.pone.0058866
  8. Brigotti M, Arfilli V, Carnicelli D, et al (2013). Shiga toxin 1, as DNA repair inhibitor, synergistically potentiates the activity of the anticancer drug, mafosfamide, on Raji cells. Toxins, 5, 431-44. https://doi.org/10.3390/toxins5020431
  9. Butt AJ, Roberts CG, Seawright AA, et al (2006). A novel plant toxin, persin, with in vivo activity in the mammary gland, induces Bim-dependent apoptosis in human breast cancer cells. Mol Cancer Ther, 5, 2300-9. https://doi.org/10.1158/1535-7163.MCT-06-0170
  10. Chang CH, Chung CH, Hsu CC, et al (2014). Inhibitory effects of polypeptides derived from snake venom C-type lectin, aggretin, on tumour cell-induced platelet aggregation. J Thromb Haemost, [Epub ahead of print].
  11. Das Gupta S, Debnath A, Saha A, et al (2007). Indian black scorpion (Heterometrus bengalensis Koch) venom induced antiproliferative and apoptogenic activity against human leukemic cell lines U937 and K562. Leuk Res, 31, 817-25. https://doi.org/10.1016/j.leukres.2006.06.004
  12. Diaz-Garcia A1, Morier-Diaz L, Frion-Herrera Y, et al (2013). In vitro anticancer effect of venom from Cuban scorpion Rhopalurus junceus against a panel of human cancer cell lines. J Venom Res, 4, 5-12.
  13. Engedal N, Skotland T, Torgersen ML, et al (2011). Shiga toxin and its use in targeted cancer therapy and imaging. Microb Biotechnol, 4, 32-46. https://doi.org/10.1111/j.1751-7915.2010.00180.x
  14. Fedorov S, Dyshlovoy S, Monastyrnaya M, et al (2010). The anticancer effects of actinoporin RTX-A from the sea anemone Heteractis crispa (=Radianthus macrodactylus). Toxicon, 55, 811-7. https://doi.org/10.1016/j.toxicon.2009.11.016
  15. Feng W, Tetsuro I, Mitsuzi Y (1995). The antitumor activities of gnidimacrin isolated from Stellera chamaejasme L. Zhonghua Zhong Liu Za Zhi, 17, 24-6.
  16. Grant MA, Morelli XJ, Rigby AC (2004). Conotoxins and structural biology: a prospective paradigm for drug discovery. Curr Protein Pept Sci, 5, 235-48. https://doi.org/10.2174/1389203043379710
  17. Heinen TE, da Veiga AB (2011). Arthropod venoms and cancer. Toxicon, 57, 497-511. https://doi.org/10.1016/j.toxicon.2011.01.002
  18. Hidalgo M, Izbicka E, Eckhardt SG, et al (1999). Antitumor activity of MGI 114 (6-hydroxymethylacylfulvene, HMAF), a semisynthetic derivative of illudin S, against adult and pediatric human tumor colony-forming units. Anticancer Drugs, 10, 837-44. https://doi.org/10.1097/00001813-199910000-00007
  19. Hider RC (1988). Honeybee venom: a rich source of pharmacologically active peptides. Endeavour, 12, 60-5. https://doi.org/10.1016/0160-9327(88)90082-8
  20. Hong SY, Lee H, You WK, et al (2003). The snake venom disintegrin salmosin induces apoptosis by disassembly of focal adhesions in bovine capillary endothelial cells. Biochem Biophys Res Comm, 302, 502-8. https://doi.org/10.1016/S0006-291X(03)00213-4
  21. Huang T, Gong WH, Li XC, et al (2012). Efficient killing effect of osteosarcoma cells by cinobufacini and cisplatin in combination. Asian Pac J Cancer Prev, 13, 2847-51. https://doi.org/10.7314/APJCP.2012.13.6.2847
  22. Huh JE, Baek YH, Lee MH, et al (2010). Bee venom inhibits tumor angiogenesis and metastasis by inhibiting tyrosine phosphorylation of VEGFR-2 in LLC-tumor-bearing mice. Cancer Lett, 292, 98-110. https://doi.org/10.1016/j.canlet.2009.11.013
  23. Hui J, Xiao F, Li H, et al (2011). Inhibiting tumor-cell growth by novel truncated staphylococcal enterotoxin C2 mutant. Sheng Wu Gong Cheng Xue Bao, 27, 891-9.
  24. Ip SW, Chu YL, Yu CS, et al (2012). Bee venom induces apoptosis through intracellular Ca2+-modulated intrinsic death pathway in human bladder cancer cells. Int J Urol, 19, 61-70. https://doi.org/10.1111/j.1442-2042.2011.02876.x
  25. Ip SW, Liao SS, Lin SY, et al (2008). The role of mitochondria in bee venom-induced apoptosis in human breast cancer MCF7 cells. In Vivo, 22, 237-45.
  26. Jain D, Kumar S (2012). Snake venom: a potent anticancer agent. Asian Pac J Cancer Prev, 13, 4855-60. https://doi.org/10.7314/APJCP.2012.13.10.4855
  27. Jakubowski P, Calvete JJ, Eble JA, et al (2013). Identification of inhibitors of alpha2beta1 integrin, members of C-lectin type proteins, in Echis sochureki venom. Toxicol Appl Pharmacol, 269, 34-42. https://doi.org/10.1016/j.taap.2013.03.002
  28. Jo M, Park MH, Kollipara PS, et al (2012). Anti-cancer effect of bee venom toxin and melittin in ovarian cancer cells through induction of death receptors and inhibition of JAK2/STAT3 pathway. Toxicol Appl Pharmacol, 258, 72-81. https://doi.org/10.1016/j.taap.2011.10.009
  29. Kobayashi H, Masumoto J (2010). Endotoxin contamination of Agaricus blazei Murrill extract enhances murine immunologic responses and inhibits the growth of sarcoma 180 implants in vivo. J Environ Pathol Toxicol Oncol, 29, 159-68. https://doi.org/10.1615/JEnvironPatholToxicolOncol.v29.i2.80
  30. Kollipara PS, Kim JH, Won D, et al (2014). Co-culture with NK-92MI cells enhanced the anti-cancer effect of bee venom on NSCLC cells by inactivation of NF-kappaB. Arch Pharm Res, 37, 379-89. https://doi.org/10.1007/s12272-013-0319-8
  31. Kreitman RJ (2006). Immunotoxins for targeted cancer therapy. AAPS J, 8, E532-51. https://doi.org/10.1208/aapsj080363
  32. Lai D, Visser-Grieve S, Yang X (2012). Tumour suppressor genes in chemotherapeutic drug response. Biosci Rep, 32, 361-74. https://doi.org/10.1042/BSR20110125
  33. Liberio MS, Joanitti GA, Fontes W, et al (2013). Anticancer peptides and proteins: a panoramic view. Protein Pept Lett, 20, 380-91. https://doi.org/10.2174/092986613805290435
  34. Liu S, Yu M, He Y, et al (2008). Melittin prevents liver cancer cell metastasis through inhibition of the Rac1, dependent pathway. Hepatology, 47, 1964-73. https://doi.org/10.1002/hep.22240
  35. Lucena SE, Romo K, Suntravat M, et al (2014). Anti-angiogenic activities of two recombinant disintegrins derived from the Mohave and Prairie rattlesnakes. Toxicon, 78, 10-7. https://doi.org/10.1016/j.toxicon.2013.11.005
  36. MacDonald JR, Muscoplat CC, Dexter DL, et al (1997). Preclinical antitumor activity of 6-hydroxymethylacylfulvene, a semisynthetic derivative of the mushroom toxin illudin S. Cancer Res, 57, 279-83.
  37. Moon DO, Park SY, Heo MS, et al (2006). Key regulators in bee venom-induced apoptosis are Bcl-2 and caspase-3 in human leukemic U937 cells through downregulation of ERK and Akt. Int immunopharmacol, 6, 1796-807. https://doi.org/10.1016/j.intimp.2006.07.027
  38. Orsolic N (2012). Bee venom in cancer therapy. Cancer Metastasis Rev, 31, 173-94. https://doi.org/10.1007/s10555-011-9339-3
  39. Park MH, Choi MS, Kwak DH, et al (2011). Anti-cancer effect of bee venom in prostate cancer cells through activation of caspase pathway via inactivation of NF-$\kappa{B}$. The Prostate, 71, 801-12. https://doi.org/10.1002/pros.21296
  40. Polito L, Bortolotti M, Mercatelli D, et al (2013). Saporin-S6: a useful tool in cancer therapy. Toxins, 5, 1698-722. https://doi.org/10.3390/toxins5101698
  41. Reis LO, Ferreira U, Billis A, et al (2012). Anti-angiogenic effects of the superantigen staphylococcal enterotoxin B and bacillus Calmette-Guerin immunotherapy for nonmuscle invasive bladder cancer. J Urol, 187, 438-45. https://doi.org/10.1016/j.juro.2011.10.022
  42. Riede I (2010). Tumor therapy with Amanita phalloides (death cap): stabilization of B-cell chronic lymphatic leukemia. J Altern Complement Med, 16, 1129-32. https://doi.org/10.1089/acm.2010.0035
  43. Sadraeian M, Rasoul-Amini S, Mansoorkhani MJ, et al (2013). Induction of antitumor immunity against cervical cancer by protein HPV-16 E7 in fusion with ricin B chain in tumorbearing mice. Int J Gynecol Cancer, 23, 809-14. https://doi.org/10.1097/IGC.0b013e3182907989
  44. Sandvig K (2001). Shiga toxins. Toxicon, 39, 1629-35. https://doi.org/10.1016/S0041-0101(01)00150-7
  45. Soletti RC, de Faria GP, Vernal J, et al (2008). Potentiation of anticancer-drug cytotoxicity by sea anemone pore-forming proteins in human glioblastoma cells. Anticancer Drugs, 19, 517-25. https://doi.org/10.1097/CAD.0b013e3282faa704
  46. Son DJ, Lee JW, Lee YH, et al (2007). Therapeutic application of anti-arthritis, pain-releasing, and anti-cancer effects of bee venom and its constituent compounds. Pharmacol Ther, 115, 246-70. https://doi.org/10.1016/j.pharmthera.2007.04.004
  47. Son DJ, Park MH, Chae SJ, et al (2007). Inhibitory effect of snake venom toxin from Vipera lebetina turanica on hormone-refractory human prostate cancer cell growth: induction of apoptosis through inactivation of nuclear factor kappaB. Mol Cancer Ther, 6, 675-83.
  48. Stewart JM, Steeves BJ, Vernes K (2009). Paralytic peptide for use in neuromuscular therapy. US, US7485622 B2.
  49. Swenson S, Costa F, Minea R, et al (2004). Intravenous liposomal delivery of the snake venom disintegrin contortrostatin limits breast cancer progression. Mol Cancer Ther, 3, 499-511.
  50. Takai N, Kira N, Ishii T, et al (2012). Bufalin, a traditional oriental medicine, induces apoptosis in human cancer cells. Asian Pac J Cancer Prev, 13, 399-402. https://doi.org/10.7314/APJCP.2012.13.1.399
  51. Wang H, Ke M, Tian Y, et al (2013). BF-30 selectively inhibits melanoma cell proliferation via cytoplasmic membrane permeabilization and DNA-binding in vitro and in B16F10-bearing mice. Eur J Pharmacol, 707, 1-10. https://doi.org/10.1016/j.ejphar.2013.03.028
  52. White J (2005). Snake venoms and coagulopathy. Toxicon, 45, 951-67. https://doi.org/10.1016/j.toxicon.2005.02.030
  53. Wood DP (2014). Re: Diphtheria toxin-epidermal growth factor fusion protein DAB389EGF for the treatment of bladder cancer. J Urol, 191, 556. https://doi.org/10.1016/j.juro.2013.10.136
  54. Xie Q, Tang N, Lin Y, et al (2013). Recombinant adenovirus snake venom cystatin inhibits the growth, invasion, and metastasis of B16F10 cells in vitro and in vivo. Melanoma Res, 23, 444-51. https://doi.org/10.1097/CMR.0000000000000031
  55. Zhang C, Zhou SS, Feng LY, et al (2013). In vitro anti-cancer activity of chamaejasmenin B and neochamaejasmin C isolated from the root of Stellera chamaejasme L. Acta Pharmacol Sin, 34, 262-70. https://doi.org/10.1038/aps.2012.158

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