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International Journal of Hepatology
Volume 2011, Article ID 736581, 6 pages
http://dx.doi.org/10.4061/2011/736581
Research Article

Hepatocyte Lysosomal Membrane Stabilization by Olive Leaves against Chemically Induced Hepatocellular Neoplasia in Rats

1Department of Biochemistry, College of Pharmacy, Minia University, Minia, Egypt
2Department of Pharmacology, College of Pharmacy, Minia University, Minia, Egypt
3Department of Medical Biochemistry, College of Medicine, Mansura University, Mansura, Egypt

Received 1 July 2010; Revised 29 September 2010; Accepted 17 October 2010

Academic Editor: Masahiko Hirota

Copyright © 2011 N. M. Abdel-Hamid et al. 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. D. E. Goll, W. C. Kleese, and A. Szpacinko, “Skeletal muscle proteases and protein turnover,” in Animal Growth Regulation, D. R. Campion, G. J. Hausman , and R. J. Martin, Eds., pp. 141–182, Plenum Publishing, New York, NY, USA, 1989. View at Google Scholar
  2. S. Johari, Y. Maeda, S. Okamoto, and T. Hashiguchi, “Comparison of calpain and calpastatin activities in skeletal muscle of broiler and layer chickens,” British Poultry Science, vol. 34, no. 4, pp. 819–824, 1993. View at Google Scholar
  3. M. G. Thompson and R. M. Palmer, “Signalling pathways regulating protein turnover in skeletal muscle,” Cellular Signalling, vol. 10, no. 1, pp. 1–11, 1998. View at Publisher · View at Google Scholar
  4. D. J. Millward, P. C. Bates, and S. Rosochacki, “The extent and nature of protein degradation in the tissues during development,” Reproduction Nutrition Developpement, vol. 21, no. 2, pp. 265–277, 1981. View at Google Scholar
  5. N. Gebbia, G. Leto, and M. Gagliano, “Lysosomal alterations in heart and liver of mice treated with doxorubicin,” Cancer Chemotherapy and Pharmacology, vol. 15, no. 1, pp. 26–30, 1985. View at Google Scholar
  6. R. Subashini, A. Gnanapragasam, S. Senthilkumar, S. K. Yogeeta, and T. Devaki, “Protective efficacy of Nardostachys jatamansi (Rhizomes) on mitochondrial respiration and lysosomal hydrolases during doxorubicin induced myocardial injury in rats,” Journal of Health Science, vol. 53, no. 1, pp. 67–76, 2007. View at Publisher · View at Google Scholar
  7. R. K. Murray, D. K. A. Granner, P. Mayes, and V. W. Rodwell, “Cell diseases resulting from faulty targeting of lysosomal enzymes and genetic deficiencies of glycoprotein lysosomal hydrolases cause diseases such as mannosidosis,” in Harper's Biochemistry, pp. 691–692, Appleton and Lange, San Mateo, Calif, USA, 1999. View at Google Scholar
  8. T. Torimura, T. Ueno, S. Inuzuka, M. Tanaka, H. Abe, and K. Tanikawa, “Mechanism of fibrous capsule formation surrounding hepatocellular carcinoma: immunohistochemical study,” Archives of Pathology and Laboratory Medicine, vol. 115, no. 4, pp. 365–371, 1991. View at Google Scholar
  9. I. O. L. Ng, E. C. S. Lai, M. M. T. Ng, and S. T. Fan, “Tumor encapsulation in hepatocellular carcinoma: a pathologic study of 189 cases,” Cancer, vol. 70, no. 1, pp. 45–49, 1992. View at Publisher · View at Google Scholar
  10. W. G. Stetler-Stevenson, S. Aznavoorian, and L. A. Liotta, “Tumor cell interactions with the extracellular matrix during invasion and metastasis,” Annual Review of Cell Biology, vol. 9, pp. 541–573, 1993. View at Google Scholar
  11. C. H. Anna, R. R. Maronpot, M. A. Pereira, J. F. Foley, D. E. Malarkey, and M. W. Anderson, “Ras proto-oncogene activation in dichloroacetic acid-, trichloroethylene- and tetrachloroethylene-induced liver tumors in B6C3F1 mice,” Carcinogenesis, vol. 15, no. 10, pp. 2255–2261, 1994. View at Google Scholar
  12. A. Ferreira-Gonzalez, A. B. DeAngelo, S. Nasim, and C. T. Garrett, “Ras oncogene activation during hepatocarcinogenesis in B6C3F1 male mice by dichloroacetic and trichloroacetic acids,” Carcinogenesis, vol. 16, no. 3, pp. 495–500, 1995. View at Google Scholar
  13. J. C. Caldwell and N. Keshava, “Key issues in the modes of action and effects of trichloroethylene metabolites for liver and kidney tumorigenesis,” Environmental Health Perspectives, vol. 114, no. 9, pp. 1457–1463, 2006. View at Publisher · View at Google Scholar · View at Scopus
  14. L. Melillo, “Diuretic plants in the paintings of Pompeii degli Studi di Napoli, Italy,” American Journal of Nephrology, vol. 14, no. 4–6, pp. 423–425, 1994. View at Google Scholar
  15. F. Visioli and C. Galli, “Biological properties of olive oil phytochemicals,” Critical Reviews in Food Science and Nutrition, vol. 42, no. 3, pp. 209–221, 2002. View at Publisher · View at Google Scholar
  16. A. Guinda, “Use of solid residue from the olive industry,” Grasas y Aceites, vol. 57, no. 1, pp. 107–115, 2006. View at Google Scholar
  17. E. Altiok, D. Baycin, O. Bayraktar, and S. Ulku, “Isolation of polyphenols from the extracts of olive leaves (Olea europaea L.) by adsorption on silk fibroin,” Separation and Purification Technology, vol. 62, no. 2, pp. 342–348, 2008. View at Publisher · View at Google Scholar
  18. P. T. Albi, A. Guinda, and A. Lanzon, “Procedimiento de obtencion y determinacion de acidos terpenicos de la hoja del olivo (Olea europaea),” Grasas y Aceites, vol. 52, no. 5, pp. 275–278, 2001. View at Google Scholar
  19. A. Guinda, A. Lanzon, J. J. Rios, and T. Albi, “Aislamiento y cuantification de los componentes hoja del olivo. Extracto de hexano,” Grasas Y Aceites, vol. 53, pp. 240–245, 2002. View at Google Scholar
  20. L. Ok-Hwan, L. Hee-Bong, L. Junsoo et al., “Chemical properties of olive and bay leaves,” Journal of the Korean Society of Food Science and Nutrition, vol. 34, no. 4, pp. 503–508, 2005. View at Google Scholar
  21. G. Corona, M. Deiana, A. Incani, D. Vauzour, M. Assunta Dessì, and J. P. E. Spencer, “Inhibition of p38/CREB phosphorylation and COX-2 expression by olive oil polyphenols underlies their anti-proliferative effects,” Biochemical and Biophysical Research Communications, vol. 362, no. 3, pp. 606–611, 2007. View at Publisher · View at Google Scholar · View at PubMed
  22. R. Japon-Lujan and M. D. Luque de Castro, “Superheated liquid extraction of oleuropein and related biophenols from olive leaves,” Journal of Chromatography A, vol. 1136, no. 2, pp. 185–191, 2006. View at Publisher · View at Google Scholar · View at PubMed
  23. L. Tao, S. Yang, MI. Xie, P. M. Kramer, and M. A. Pereira, “Effect of trichloroethylene and its metabolites, dichloroacetic acid and trichloroacetic acid, on the methylation and expression of c-Jun and c-Myc protooncogenes in mouse liver: prevention by methionine,” Toxicological Sciences, vol. 54, no. 2, pp. 399–407, 2000. View at Google Scholar
  24. M. Y. Hung, T. Y. C. Fu, P. H. Shih, C. P. Lee, and G. C. Yen, “Du-Zhong (Eucommia ulmoides Oliv.) leaves inhibits CCl4-induced hepatic damage in rats,” Food and Chemical Toxicology, vol. 44, no. 8, pp. 1424–1431, 2006. View at Publisher · View at Google Scholar · View at PubMed
  25. S. Kumar, J. G. Sharma, and R. Chakrabarti, “Quantitative estimation of proteolytic enzyme and ultrastructural study of anterior part of intestine of Indian major carp (Catla catla) larvae during ontogenesis,” Current Science, vol. 79, no. 7, pp. 1007–1011, 2000. View at Google Scholar
  26. O. H. Lowry, N. J. Rosebrough, A. L. Farr, and R. J. Randall, “Protein measurement with the Folin phenol reagent,” Journal of Biological Chemistry, vol. 193, pp. 265–275, 1951. View at Google Scholar
  27. M. L. Anson, “The estimation of pepsin, trypsin, papain and cathepsin with hemoglobin,” The Journal of General Physiology, vol. 22, pp. 79–89, 1938. View at Google Scholar
  28. O. Folin and V. Ciocalteu, “On tyrosine and tryptophane determinations in proteins,” Journal of Biological Chemistry, vol. 73, pp. 627–650, 1927. View at Google Scholar
  29. M. M. Acharya and S. S. Katyare, “An improved micromethod for tyrosine estimation,” Zeitschrift fur Naturforschung. Section C., vol. 59, no. 11-12, pp. 897–900, 2004. View at Google Scholar
  30. A. J. Barret and M. F. Heath, “Lysosomal enzymes,” in Lysosome: Laboratory Handbook, J. T. Dingle, Ed., pp. 124–126, North Holland, Amsterdam, The Netherlands, 1977. View at Google Scholar
  31. M. A. Nerurkar, J. G. Satav, and S. S. Katyare, “Insulin-dependent changes in lysosomal cathepsin D activity in rat liver, kidney, brain and heart,” Diabetologia, vol. 31, no. 2, pp. 119–122, 1988. View at Google Scholar
  32. M. A. Khandkar, D. V. Parmar, M. Das, and S. S. Katyare, “Is activation of lysosomal enzymes responsible for paracetamol-induced hepatotoxicity and nephrotoxicity?” Journal of Pharmacy and Pharmacology, vol. 48, no. 4, pp. 437–440, 1996. View at Google Scholar
  33. M. M. Acharya, S. H. Khamesra, and S. S. Katyare, “Effect of repeated intraperitoneal exposure to picrotoxin on rat liver lysosomal function,” Indian Journal of Experimental Biology, vol. 42, no. 8, pp. 808–811, 2004. View at Google Scholar
  34. D. B. Duncan, “Multiple range and multiple F tests,” Biometrics, vol. 11, pp. 1–42, 1955. View at Google Scholar
  35. F. Marzo, E. Urdaneta, and S. Santidrian, “Liver proteolytic activity in tannic-fed birds,” Poultry Science, vol. 81, pp. 92–94, 2002. View at Google Scholar
  36. B. Werle, C. Kraft, T. T. Lah et al., “Cathepsin B in infiltrated lymph nodes is of prognostic significance for patients with nonsmall cell lung carcinoma,” Cancer, vol. 89, no. 11, pp. 2282–2291, 2000. View at Google Scholar
  37. D. Flores-Reséndiz, E. Castellanos-Juárez, and L. Benítez-Bribiesca, “Proteases in cancer progression,” Gaceta Medica de Mexico, vol. 145, no. 2, pp. 131–142, 2009. View at Google Scholar
  38. T. Lah, M. Čerček, A. Blejec et al., “Cathepsin B, a prognostic indicator in lymph node-negative breast carcinoma patients: comparison with cathepsin D, cathepsin L, and other clinical indicators,” Clinical Cancer Research, vol. 6, no. 2, pp. 578–584, 2000. View at Google Scholar
  39. N. M. Abdel-Hamid, “Premalignant variations in extracellular matrix composition in chemically induced hepatocellular carcinoma in rats,” The Journal of Membrane Biology, vol. 230, no. 3, pp. 155–162, 2009. View at Google Scholar
  40. N. M. Abdel-Hamid and M. A. Morsy, “Novel biochemical pathways for 5-fluorouracil in managing experimental hepatocellular carcinoma in rats,” Journal of Membrane Biology, vol. 234, no. 1, pp. 29–34, 2010. View at Publisher · View at Google Scholar · View at PubMed
  41. M. Yamashita and S. Konagaya, “Participation of cathepsin L into extensive softening of the muscle of chum salmon in spawning migration,” Comparative Biochemistry and Physiology, vol. 95, no. 1, pp. 149–152, 1990. View at Google Scholar
  42. J. P. Braun, A. Rico, and P. Bernard, “Changes in the distribution of gamma-glutamyl transferase in the organs of the mouse as a function of developmentEvolution de la distrubtion de la gamma-glutamyl transférase dans les organes de la Souris en fonction du développement,” Comptes Rendus Hebdomadaires des Seances de l"Academie des Sciences. Serie D, vol. 286, no. 20, pp. 1483–1485, 1978. View at Google Scholar
  43. H. M. Beere and J. A. Hickman, “Differentiation: a suitable strategy for cancer chemotherapy?” Anti-Cancer Drug Design, vol. 8, no. 4, pp. 299–322, 1993. View at Google Scholar
  44. L. Abaza, T. P. N. Talorete, P. Yamada, Y. Kurita, M. Zarrouk, and H. Isoda, “Induction of growth inhibition and differentiation of Human Leukemia HL-60 cells by a Tunisian Gerboui olive leaf extract,” Bioscience, Biotechnology and Biochemistry, vol. 71, no. 5, pp. 1306–1312, 2007. View at Publisher · View at Google Scholar