Efecto del tratamiento con oxaliplatino sobre los niveles de tiorredoxina y de la molécula ido (indolamina 2,3 dioxigenasa) en lineas celulares de cáncer colorrectal.

  1. Mónica Cavia 1
  2. Susana Gonzalez-Mateo 1
  3. Carlos García Giron 1
  4. Pilar Muñiz 2
  1. 1 Unidad de Investigación del Hospital General Yagüe. Complejo Asistencial Universitario de Burgos.
  2. 2 Departamento de Bioquímica y Biología Molecular. Universidad de Burgos. Burgos
Journal:
Revista Electrónica de Biomedicina

ISSN: 1697-090X

Year of publication: 2012

Issue: 1

Pages: 37-40

Type: Article

More publications in: Revista Electrónica de Biomedicina

Abstract

Increases in indoleamine-2-3-dyoxigenase activity and changes in redox state have been reported in cancer. However, their relationship with chemoterapy remains unknown. The aim of the present study was to evaluate the oxaliplatin treatment in colorectal cancer cell lines (Caco-2 and SW480) on the immunosuppressive molecule IDO and its relationship with the Trx/TrxR system. Results of this study was a higher IDO enzyme activity in Caco-2 cells than in SW480 cells associated with lower levels of the thioredoxin.

Bibliographic References

  • Cavia M, Muñiz P, DeSantiago R, Herreros-Villanueva M., García-Giron C., López AS, Coma MJ, Changes in the levels of thioredoxin and indoleamine-2,3-dioxygenase activity in plasma patients with colorectal cancer treated with chemotherapy. Biochem Cell Biol 2012; 90: 1-7.
  • Uyttenhove C. Evidence for a tumoral immune resistance mechanism based on tryptophan degradation by indoleamine 2,3- dioxygenase. Nat Med 2003; 9: 1269-1274.
  • Valko M, Leibfritz D, Moncol J, Cronin MT, Mazur M, Telser J. Free radicals and antioxidants in normal physiological functions and human disease. Int J Biochem Cell Biol. 2007;39:44-84.
  • Oliva MR, Ripoll F, Muñiz P, Iradi A, Trullenque R, Valls V, Drehmer E, Sáez GT. Genetic alterations and oxidative metabolism in sporadic colorectal tumors from a Spanish community. Mol Carcinog. 1997;18:232-243.
  • Biaglow JE, Miller RA. The thioredoxin reductase/thioredoxin system: novel redox targets for cancer therapy. Cancer Biol Ther. 2005;4:6-13.
  • Fujino G, Noguchi T, Takeda K, Ichijo H. Thioredoxin and protein kinases in redox signaling. Semin Cancer Biol. 2006;16:427- 435.
  • Lu J, Chew EH, Holmgren A. Targeting thioredoxin reductase is a basis for cancer therapy by arsenic trioxide. Proc Natl Acad Sci U S A. 2007;104:12288-12293.
  • Munn DH. Indoleamine 2,3-dioxygenase, tumor-induced tolerance and counter-regulation. Curr Opin Immunol 2006; 18:220- 225
  • Alegre E, López AS, González A. Tryptophan metabolites interfere with the Ehrlich reaction used for the measurement of kynurenine. Analitical Biochemistry 2005;339:188-9
  • Soderberg A, Sahaf B, Rosen A. Thioredoxin reductase, a redox-active selenoproein, is secreted by normal and neoplastic cells: presence in human plasma. Cancer Res 2000; 60: 2281-2289.
  • Holmgren A, Björnstedt M. Thioredoxin and thioredoxin reductase. Methods Enzymol 1995; 252: 191-208.