title: Troglitazone reduces glyoxalase I protein expression in glioma and potentiates the effects of chemotherapeutic agents.
abstract: Despite resistance of most gliomas to chemotherapy, approximately 2/3 of oligodendrogliomas show sensitivity to such agents. This sensitivity has been associated with deletions on chromosome 1p alone or in combination with 19q. Higher expression of the enzyme glyoxalase I has been found in oligodendrogliomas with chromosome 1p intact compared to those with a deletion. Higher expression of this enzyme is also associated with tumor chemoresistance in other cancers. The present study tested whether the drug troglitazone would make a glioma cell line more sensitive to chemotherapeutic agents. This drug was chosen because it has been shown to decrease glyoxalase I enzyme activity in cells. Treatment with troglitazone decreased expression of glyoxalase I, and potentiated cell death when used in combination with chemotherapeutic agents. This decrease in glyoxalase I protein may be one mechanism by which this potentiation occurs, and troglitazone may be a candidate for use in glioma therapy.
authors.affiliation: Surgical Neurology Branch, National Institute of Neurological Disorders and Stroke, National Cancer Institute, National Institutes of Health, Bethesda, MD 20892-1414, USA.
authors.forename: Jeffrey
authors.initials: J
authors.lastname: Helgager
authors.forename: Jie
authors.initials: J
authors.lastname: Li
authors.forename: Irina A
authors.initials: IA
authors.lastname: Lubensky
authors.forename: Russell
authors.initials: R
authors.lastname: Lonser
authors.forename: Zhengping
authors.initials: Z
authors.lastname: Zhuang
references.citation: Leuk Lymphoma. 2005 Aug;46(8):1199-206
references.pmid: 16085563
references.citation: Cancer Biol Ther. 2007 Mar;6(3):391-6
references.pmid: 17264672
references.citation: Diabetologia. 2001 Nov;44(11):2004-12
references.pmid: 11719831
references.citation: J Am Chem Soc. 2007 Jan 31;129(4):873-80
references.pmid: 17243824
references.citation: Cancer Res. 1978 Feb;38(2):257-60
references.pmid: 620400
references.citation: J Natl Cancer Inst. 1998 Oct 7;90(19):1473-9
references.pmid: 9776413
references.citation: Br J Cancer. 2004 Oct 18;91(8):1561-5
references.pmid: 15467764
references.citation: Cancer. 2001 Oct 1;92(7):1936-42
references.pmid: 11745268
references.citation: Parasitology. 1993;107 Suppl:S177-86
references.pmid: 8115182
references.citation: Neurologist. 2006 Nov;12(6):279-92
references.pmid: 17122724
references.citation: Diabetes. 2000 May;49(5):759-67
references.pmid: 10905484
references.citation: Clin Cancer Res. 2001 Aug;7(8):2513-8
references.pmid: 11489834
references.citation: Cancer Res. 1982 Mar;42(3):1008-14
references.pmid: 7059967
references.citation: Cancer Genet Cytogenet. 2005 Jul 1;160(1):1-14
references.pmid: 15949564
references.citation: Cancer Res. 2001 May 15;61(10):4024-9
references.pmid: 11358821
references.citation: Endocr Relat Cancer. 2006 Jun;13(2):401-13
references.pmid: 16728570
references.citation: Am J Hosp Pharm. 1981 Apr;38(4):483-6
references.pmid: 6945043
references.citation: Anticancer Res. 1994 Sep-Oct;14(5A):2047-52
references.pmid: 7847848
references.citation: Biochem Soc Trans. 2003 Dec;31(Pt 6):1372-7
references.pmid: 14641066
references.citation: Gen Pharmacol. 1996 Jun;27(4):565-73
references.pmid: 8853285
references.citation: J Natl Cancer Inst. 1992 Apr 1;84(7):515-9
references.pmid: 1312177
references.citation: Biochem J. 1995 Jul 1;309 ( Pt 1):127-31
references.pmid: 7619046