Table of Contents Author Guidelines Submit a Manuscript
Journal of Oncology
Volume 2010, Article ID 373491, 7 pages
http://dx.doi.org/10.1155/2010/373491
Research Article

Troglitazone Reduces Glyoxalase I Protein Expression in Glioma and Potentiates the Effects of Chemotherapeutic Agents

1Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-1414, USA
2Cancer Diagnosis Program, Division of Cancer Treatment and Diagnosis, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-1414, USA

Received 9 July 2009; Revised 25 January 2010; Accepted 10 February 2010

Academic Editor: Bruce Baguley

Copyright © 2010 Jeffrey Helgager 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. A. D. Norden and P. Y. Wen, “Glioma therapy in adults,” Neurologist, vol. 12, no. 6, pp. 279–292, 2006. View at Publisher · View at Google Scholar · View at Scopus
  2. J. G. Cairncross, K. Ueki, M. C. Zlatescu et al., “Specific genetic predictors of chemotherapeutic response and survival in patients with anaplastic oligodendrogliomas,” Journal of the National Cancer Institute, vol. 90, no. 19, pp. 1473–1479, 1998. View at Google Scholar · View at Scopus
  3. H. Okamoto, J. Li, S. Gläsker et al., “Proteomic comparison of oligodendrogliomas with and without 1pLOH,” Cancer Biology and Therapy, vol. 6, no. 3, pp. 391–396, 2007. View at Google Scholar · View at Scopus
  4. P. J. Thornalley, “Protecting the genome: defence against nucleotide glycation and emerging role of glyoxalase I overexpression in multidrug resistance in cancer chemotherapy,” Biochemical Society Transactions, vol. 31, part 6, pp. 1372–1377, 2003. View at Google Scholar · View at Scopus
  5. P. J. Thornalley, “Pharmacology of methylglyoxal: formation, modification of proteins and nucleic acids, and enzymatic detoxification—a role in pathogenesis and antiproliferative chemotherapy,” General Pharmacology, vol. 27, no. 4, pp. 565–573, 1996. View at Publisher · View at Google Scholar · View at Scopus
  6. S. Ranganathan, E. S. Walsh, and K. D. Tew, “Glyoxalase I in detoxification: studies using a glyoxalase I transfectant cell line,” Biochemical Journal, vol. 309, part 1, pp. 127–131, 1995. View at Google Scholar
  7. S.-I. Sato, Y. Kwon, S. Kamisuki et al., “Polyproline-rod approach to isolating protein targets of bioactive small molecules: isolation of a new target of indomethacin,” Journal of the American Chemical Society, vol. 129, no. 4, pp. 873–880, 2007. View at Publisher · View at Google Scholar · View at Scopus
  8. J.-R. Weng, C.-Y. Chen, J. J. Pinzone, M. D. Ringel, and C.-S. Chen, “Beyond peroxisome proliferator-activated receptor γ signaling: the multi-facets of the antitumor effect of thiazolidinediones,” Endocrine-Related Cancer, vol. 13, no. 2, pp. 401–413, 2006. View at Publisher · View at Google Scholar · View at Scopus
  9. L. Wu, E. Eftekharpour, G. F. Davies, W. J. Roesler, and B. H. J. Juurlink, “Troglitazone selectively inhibits glyoxalase I gene expression,” Diabetologia, vol. 44, no. 11, pp. 2004–2012, 2001. View at Publisher · View at Google Scholar · View at Scopus
  10. G. F. Davies, W. J. Roesler, B. H. J. Juurlink, and T. A. A. Harkness, “Troglitazone overcomes doxorubicin-resistance in resistant K562 leukemia cells,” Leukemia and Lymphoma, vol. 46, no. 8, pp. 1199–1206, 2005. View at Publisher · View at Google Scholar · View at Scopus
  11. J. S. Kovach, P. A. Svingen, and D. J. Schaid, “Levamisole potentiation of fluorouracil antiproliferative activity mimicked by orthovanadate, an inhibitor of tyrosine phosphatase,” Journal of the National Cancer Institute, vol. 84, no. 7, pp. 515–519, 1992. View at Google Scholar · View at Scopus
  12. H. Sakamoto, T. Mashima, S. Sato, Y. Hashimoto, T. Yamori, and T. Tsuruo, “Selective activation of apoptosis program by S-p-bromobenzylglutathione cyclopentyl diester in glyoxalase I-overexpressing human lung cancer cells,” Clinical Cancer Research, vol. 7, no. 8, pp. 2513–2518, 2001. View at Google Scholar · View at Scopus
  13. W. J. Dills Jr., “Nutritional and physiological consequences of tumour glycolysis,” Parasitology, vol. 107, supplement, pp. S177–S186, 1993. View at Google Scholar
  14. M. E. Law, K. L. Templeton, G. Kitange et al., “Molecular cytogenetic analysis of chromosomes 1 and 19 in glioma cell lines,” Cancer Genetics and Cytogenetics, vol. 160, no. 1, pp. 1–14, 2005. View at Publisher · View at Google Scholar · View at Scopus
  15. Y. Fukui, S.-I. Masui, S. Osada, K. Umesono, and K. Motojima, “A new thiazolidinedione, NC-2100, which is a weak PPAR-γ activator, exhibits potent antidiabetic effects and induces uncoupling protein 1 in white adipose tissue of KKAy obese mice,” Diabetes, vol. 49, no. 5, pp. 759–767, 2000. View at Google Scholar · View at Scopus
  16. R. J. Weinkam and D. F. Deen, “Quantitative dose-response relations for the cytotoxic activity of chloroethylnitrosoureas in cell culture,” Cancer Research, vol. 42, no. 3, pp. 1008–1014, 1982. View at Google Scholar · View at Scopus
  17. G. K. Poochikian, J. C. Cradock, and K. P. Flora, “Stability of anthracycline antitumor agents in four infusion fluids,” American Journal of Hospital Pharmacy, vol. 38, no. 4, pp. 483–486, 1981. View at Google Scholar · View at Scopus
  18. K. Fabel, J. Dietrich, P. Hau et al., “Long-term stabilization in patients with malignant glioma after treatment with liposomal doxorubicin,” Cancer, vol. 92, no. 7, pp. 1936–1942, 2001. View at Publisher · View at Google Scholar · View at Scopus
  19. J. McHowat, L. M. Swift, A. Arutunyan, and N. Sarvazyan, “Clinical concentrations of doxorubicin inhibit activity of myocardial membrane-associated, calcium-independent phospholipase A(2),” Cancer Research, vol. 61, no. 10, pp. 4024–4029, 2001. View at Google Scholar
  20. P. S. Schein, J. M. Bull, D. Doukas, and D. Hoth, “Sensitivity of human and murine hematopoietic precursor cells to 2-[3-(2-chloroethyl)-3-nitrosoureido]-D-glucopyranose and 1,3-bis(2-chloroethyl)-1-nitrosourea,” Cancer Research, vol. 38, no. 2, pp. 257–260, 1978. View at Google Scholar · View at Scopus
  21. Y.-C. Shen, C. Hsu, J.-Y. Chen, and A.-L. Cheng, “Lack of efficacy of troglitazone at clinically achievable concentrations, with or without 9-cis retinoic acid or cytotoxic agents, for hepatocellular carcinoma cell lines,” British Journal of Cancer, vol. 91, no. 8, pp. 1561–1565, 2004. View at Publisher · View at Google Scholar · View at Scopus
  22. N. S. Paranka and R. T. Dorr, “Effect of doxorubicin on glutathione and glutathione-dependent enzymes in cultured rat heart cells,” Anticancer Research, vol. 14, no. 5A, pp. 2047–2052, 1994. View at Google Scholar · View at Scopus