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BioMed Research International
Volume 2013 (2013), Article ID 642848, 10 pages
http://dx.doi.org/10.1155/2013/642848
Research Article

Combination of Telmisartan with Cisplatin Controls Oral Cancer Cachexia in Rats

Institute of Pharmacy, Nirma University, Sarkhej-Gandhinagar Highway, Ahmedabad, Gujarat 382 481, India

Received 22 April 2013; Revised 9 July 2013; Accepted 1 September 2013

Academic Editor: Vickram Ramkumar

Copyright © 2013 Bhoomika M. Patel and Deepak Damle. This is an open access article distributed under the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original work is properly cited.

Linked References

  1. J. Khalili, “Oral cancer: risk factors, prevention and diagnostic,” Experimental Oncology, vol. 30, no. 4, pp. 259–264, 2008. View at Scopus
  2. K. Fearon, F. Strasser, S. D. Anker et al., “Definition and classification of cancer cachexia: an international consensus,” The Lancet Oncology, vol. 12, no. 5, pp. 489–495, 2011. View at Publisher · View at Google Scholar · View at Scopus
  3. D. Blum, A. Omlin, V. E. Baracos et al., “Cancer cachexia: a systematic literature review of items and domains associated with involuntary weight loss in cancer,” Critical Reviews in Oncology/Hematology, vol. 80, no. 1, pp. 114–144, 2011. View at Publisher · View at Google Scholar · View at Scopus
  4. T. Hirano, “Interleukin 6,” in The Cytokine Handbook, A. W. Thomson, Ed., pp. 145–168, Academic Press, London, UK, 2nd edition, 1994.
  5. T. Tsujinaka, J. Fujita, C. Ebisui et al., “Interleukin 6 receptor antibody inhibits muscle atrophy and modulates proteolytic systems in interleukin 6 transgenic mice,” Journal of Clinical Investigation, vol. 97, no. 1, pp. 244–249, 1996. View at Scopus
  6. K. Black, I. R. Garrett, and G. R. Mundy, “Chinese hamster ovarian cells transfected with the murine interleukin-6 gene cause hypercalcemia as well as cachexia, leukocytosis and thrombocytosis in tumor-bearing nude mice,” Endocrinology, vol. 128, no. 5, pp. 2657–2659, 1991. View at Scopus
  7. A. K. Reka, M. T. Goswami, R. Krishnapuram, T. J. Standiford, and V. G. Keshamouni, “Molecular cross-regulation between PPAR-γ and other signaling pathways: implications for lung cancer therapy,” Lung Cancer, vol. 72, no. 2, pp. 154–159, 2011. View at Publisher · View at Google Scholar · View at Scopus
  8. P. M. Sanders, S. T. Russell, and M. J. Tisdale, “Angiotensin II directly induces muscle protein catabolism through the ubiquitin-proteasome proteolytic pathway and may play a role in cancer cachexia,” British Journal of Cancer, vol. 93, no. 4, pp. 425–434, 2005. View at Publisher · View at Google Scholar · View at Scopus
  9. H. Kakuta, K. Sudoh, M. Sasamata, and S. Yamagishi, “Telmisartan has the strongest binding affinity to angiotensin II type 1 receptor: comparison with other angiotensin II type 1 receptor blockers,” International Journal of Clinical Pharmacology Research, vol. 25, no. 1, pp. 41–46, 2005. View at Scopus
  10. S. C. Benson, H. A. Pershadsingh, C. I. Ho et al., “Identification of telmisartan as a unique angiotensin II receptor antagonist with selective PPARγ-modulating activity,” Hypertension, vol. 43, no. 5, pp. 993–1002, 2004. View at Publisher · View at Google Scholar · View at Scopus
  11. T. Ichiki, Q. Tian, I. Imayama, and K. Sunagawa, “Telmisartan manifests powerful anti-inflammatory effects beyond class effects of angiotensin II type 1 blocker by inhibiting tumor necrosis factor alpha-induced interleukin 6 expressions through peroxisome proliferator activated receptory activation,” Circulation, vol. 118, p. 513, 2008.
  12. B. R. Goyal, P. Mesariya, R. K. Goyal, and A. A. Mehta, “Effect of telmisartan on cardiovascular complications associated with streptozotocin diabetic rats,” Molecular and Cellular Biochemistry, vol. 314, no. 1-2, pp. 123–131, 2008. View at Publisher · View at Google Scholar · View at Scopus
  13. B. R. Goyal, K. Parmar, R. K. Goyal, and A. A. Mehta, “Beneficial role of telmisartan on cardiovascular complications associated with STZ-induced type 2 diabetes in rats,” Pharmacological Reports, vol. 63, no. 4, pp. 956–966, 2011. View at Scopus
  14. B. R. Goyal and A. A. Mehta, “Beneficial role of spironolactone, telmisartan and their combination on isoproterenol induced cardiac hypertrophy,” Acta Cardiologica, vol. 67, pp. 203–211, 2012.
  15. B. R. Goyal, S. V. Bhadada, and M. M. Patel, “Comparative evaluation of spironolactone, atenolol, metoprolol, ramipril and perindopril on diabetes-induced cardiovascular complications in type 1 diabetes in rats,” International Journal of Diabetes and Metabolism, vol. 19, no. 1, pp. 11–18, 2011. View at Scopus
  16. B. M. Patel and S. V. Bhadada, “Type 2 diabetes-induced cardiovascular complications: comparative evaluation of spironolactone, atenolol, metoprolol, ramipril and perindopril,” Clinical and Experimental Hypertension, 2013. View at Publisher · View at Google Scholar
  17. H. Ohkawa, N. Ohishi, and K. Yagi, “Assay for lipid peroxides in animal tissues by thiobarbituric acid reaction,” Analytical Biochemistry, vol. 95, no. 2, pp. 351–358, 1979. View at Scopus
  18. E. Beutler, O. Duron, and B. M. Kelly, “Improved method for the determination of blood glutathione,” The Journal of Laboratory and Clinical Medicine, vol. 61, pp. 882–888, 1963. View at Scopus
  19. H. P. Misra and I. Fridovich, “The role of superoxide anion in the autoxidation of epinephrine and a simple assay for superoxide dismutase,” The Journal of Biological Chemistry, vol. 247, no. 10, pp. 3170–3175, 1972. View at Scopus
  20. K. C. H. Fearon and T. Preston, “Body composition in cancer cachexia,” Infusionstherapie, vol. 17, no. 3, pp. 63–66, 1990. View at Scopus
  21. Q. Tian, R. Miyazaki, T. Ichiki et al., “Inhibition of tumor necrosis factor-α-induced interleukin-6 expression by telmisartan through cross-talk of peroxisome proliferator- activated receptor-γ with nuclear factor κB and CCAAT/enhancer- binding protein-β,” Hypertension, vol. 53, no. 5, pp. 798–804, 2009. View at Publisher · View at Google Scholar · View at Scopus
  22. Y. Noguchi, T. Yoshikawa, D. Marat et al., “Insulin resistance in cancer patients is associated with enhanced tumor necrosis factor-α expression in skeletal muscle,” Biochemical and Biophysical Research Communications, vol. 253, no. 3, pp. 887–892, 1998. View at Publisher · View at Google Scholar · View at Scopus
  23. N. Togashi, N. Ura, K. Higashiura, H. Murakami, and K. Shimamoto, “The contribution of skeletal muscle tumor necrosis factor-α to insulin resistance and hypertension in fructose-fed rats,” Journal of Hypertension, vol. 18, no. 11, pp. 1605–1610, 2000. View at Scopus
  24. G. Rose and M. J. Shipley, “Plasma lipids and mortality: a source of error,” The Lancet, vol. 1, no. 8167, pp. 523–526, 1980. View at Scopus
  25. S. Dessi, B. Batetta, D. Pulisci et al., “Altered pattern of lipid metabolism in patients with lung cancer,” Oncology, vol. 49, no. 6, pp. 436–441, 1992. View at Scopus
  26. H. Cai, K. K. Griendling, and D. G. Harrison, “The vascular NAD(P)H oxidases as therapeutic targets in cardiovascular diseases,” Trends in Pharmacological Sciences, vol. 24, no. 9, pp. 471–478, 2003. View at Publisher · View at Google Scholar · View at Scopus
  27. G. Nickenig and D. G. Harrison, “The AT1-type angiotensin receptor in oxidative stress and atherogenesis—part I: oxidative stress and atherogenesis,” Circulation, vol. 105, no. 3, pp. 393–396, 2002. View at Publisher · View at Google Scholar · View at Scopus
  28. J. P. Granger, “An emerging role for inflammatory cytokines in hypertension,” American Journal of Physiology—Heart and Circulatory Physiology, vol. 290, no. 3, pp. H923–H924, 2006. View at Publisher · View at Google Scholar · View at Scopus
  29. A. Hyltander, C. Drott, U. Körner, R. Sandström, and K. Lundholm, “Elevated energy expenditure in cancer patients with solid tumours,” European Journal of Cancer, vol. 27, no. 1, pp. 9–15, 1991. View at Publisher · View at Google Scholar · View at Scopus
  30. D. R. Oliveira, R. A. S. Santos, G. F. F. Santos, M. C. Khosla, and M. J. Campagnole-Santos, “Changes in the baroreflex control of heart rate produced by central infusion of selective angiotensin antagonists in hypertensive rats,” Hypertension, vol. 27, no. 6, pp. 1284–1290, 1996. View at Scopus
  31. A. Wysong, M. Couch, S. Shadfar et al., “NF-κB inhibition protects against tumor-induced cardiac atrophy in vivo,” American Journal of Pathology, vol. 178, no. 3, pp. 1059–1068, 2011. View at Publisher · View at Google Scholar · View at Scopus
  32. B. R. Goyal, N. Solanki, R. K. Goyal, and A. A. Mehta, “Investigation into the cardiac effects of spironolactone in the experimental model of type 1 diabetes,” Journal of Cardiovascular Pharmacology, vol. 54, no. 6, pp. 502–509, 2009. View at Publisher · View at Google Scholar · View at Scopus
  33. B. M. Patel, J. Kakadiya, R. K. Goyal, and A. A. Mehta, “Effect of spironolactone on cardiovascular complications associated with type-2 diabetes in rats,” Experimental and Clinical Endocrinology & Diabetes, vol. 121, no. 8, pp. 441–447, 2013. View at Publisher · View at Google Scholar
  34. K. C. H. Fearon, “Cancer cachexia: developing multimodal therapy for a multidimensional problem,” European Journal of Cancer, vol. 44, no. 8, pp. 1124–1132, 2008. View at Publisher · View at Google Scholar · View at Scopus
  35. M. Honors and K. Kinzig, “The role of insulin resistance in the development of muscle wasting during cancer cachexia,” Journal of Cachexia, Sarcopenia and Muscle, vol. 3, pp. 5–11, 2012.
  36. J. Kodama, S. Katayama, K. Tanaka, A. Itabashi, S. Kawazu, and J. Ishii, “Effect of captopril on glucose concentration: possible role of augmented postprandial forearm blood flow,” Diabetes Care, vol. 13, no. 11, pp. 1109–1111, 1990. View at Scopus
  37. F. Folli, M. J. A. Saad, L. Velloso et al., “Crosstalk between insulin and angiotensin II signalling systems,” Experimental and Clinical Endocrinology and Diabetes, vol. 107, no. 2, pp. 133–139, 1999. View at Scopus
  38. K. Higashiura, N. Ura, T. Takada et al., “The effects of an angiotensin-converting enzyme inhibitor and an angiotensin II receptor antagonist on insulin resistance in fructose-fed rats,” American Journal of Hypertension, vol. 13, no. 3, pp. 290–297, 2000. View at Publisher · View at Google Scholar · View at Scopus
  39. F. A. Mahmoud and N. I. Rivera, “The role of C-reactive protein as a prognostic indicator in advanced cancer,” Current Oncology Reports, vol. 4, no. 3, pp. 250–255, 2002. View at Scopus
  40. H. Iwagaki, A. Hizuta, N. Tanaka, and K. Orita, “Plasma neopterin/C-reactive protein ratio as an adjunct to the assessment of infection and cancer cachexia,” Immunological Investigations, vol. 24, no. 3, pp. 479–487, 1995. View at Scopus
  41. H. R. Scott, D. C. McMillan, A. Crilly, C. S. McArdle, and R. Milroy, “The relationship between weight loss and interleukin 6 in non-small-cell lung cancer,” British Journal of Cancer, vol. 73, no. 12, pp. 1560–1562, 1996. View at Scopus
  42. G. Strassmann, M. Fong, J. S. Kenney, and C. O. Jacob, “Evidence for the involvement of interleukin 6 in experimental cancer cachexia,” The Journal of Clinical Investigation, vol. 89, no. 5, pp. 1681–1684, 1992. View at Scopus
  43. H. K. van Halteren, G. P. A. Bongaerts, C. A. M. Verhagen et al., “Recombinant human erythropoietin attenuates weight loss in a murine cancer cachexia model,” Journal of Cancer Research and Clinical Oncology, vol. 130, no. 4, pp. 211–216, 2004. View at Publisher · View at Google Scholar · View at Scopus
  44. C. P. Woodbury, Biochemistry for Pharmaceutical Sciences, Jones & Bartlett Learning, Sudbury, Mass, USA, 2012.
  45. T. Yoshikawa, Y. Noguchi, C. Doi, T. Makino, T. Okamoto, and A. Matsumoto, “Insulin resistance was connected with the alterations of substrate utilization in patients with cancer,” Cancer Letters, vol. 141, no. 1-2, pp. 93–98, 1999. View at Publisher · View at Google Scholar · View at Scopus
  46. D. Mock, B. Whitestone, and J. Freeman, “Gamma-glutamyl transpeptidase activity in human oral squamous cell carcinoma,” Oral Surgery, Oral Medicine, Oral Pathology, vol. 64, no. 2, pp. 197–201, 1987. View at Scopus
  47. J. B. Whitfield, “Gamma glutamyl transferase,” Critical Reviews in Clinical Laboratory Sciences, vol. 38, no. 4, pp. 263–355, 2001. View at Scopus
  48. D. M. Townsend, K. D. Tew, and H. Tapiero, “The importance of glutathione in human disease,” Biomedicine and Pharmacotherapy, vol. 57, no. 3, pp. 145–155, 2003. View at Publisher · View at Google Scholar · View at Scopus
  49. W. Zhong, L. W. Oberley, T. D. Oberley, and D. K. St Clair, “Suppression of the malignant phenotype of human glioma cells by overexpression of manganese superoxide dismutase,” Oncogene, vol. 14, no. 4, pp. 481–490, 1997. View at Scopus
  50. N. Li, T. Oberley, L. Oberley, and W. Zhong, “Inhibition of cell growth in NIH/3T3 fibroblasts by overexpression of manganese superoxide dismutase: mechanistic studies,” Journal of Cellular Physiology, vol. 175, pp. 359–369, 1998.
  51. C. Culmsee and J. Krieglstein, “Mechanisms of neuronal degeneration after ischemic stroke—emerging targets for novel therapeutic strategies,” Drug Discovery Today: Disease Mechanisms, vol. 2, no. 4, pp. 463–470, 2005. View at Publisher · View at Google Scholar · View at Scopus
  52. D. A. Ribeiro, D. M. Fávero Salvadori, R. N. da Silva, B. Ribeiro Darros, and M. E. Alencar Marques, “Genomic instability in non-neoplastic oral mucosa cells can predict risk during 4-nitroquinoline 1-oxide-induced rat tongue carcinogenesis,” Oral Oncology, vol. 40, no. 9, pp. 910–915, 2004. View at Publisher · View at Google Scholar · View at Scopus