Spatial activities and induction of glutamate-cysteine ligase (GCL) in the postimplantation rat embryo and visceral yolk sac

Toxicological Sciences

Volumn 81, Issue 2, 2004, Pages 371-378

  Hansen, Jason M ^a   Lee, Eunyong ^b   Harris, Craig ^b  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

^b UNIVERSITY OF MICHIGAN   (United States)

Author keywords

glutamylcysteine; Glutamate cysteine ligase; Glutathione; Rat conceptus; Rat embryo; Visceral yolk sac

Indexed keywords

BUTYLCRESOL; CYSTEINE; DIAMIDE; GAMMA GLUTAMYLCYSTEINE; GLUTAMATE CYSTEINE LIGASE; GLUTAMIC ACID; GLUTATHIONE; MALEIC ACID DIETHYL ESTER; PROSTAGLANDIN A2;

ANIMAL TISSUE; ARTICLE; CATALYSIS; CONTROLLED STUDY; DENSITOMETRY; EMBRYO; EMBRYONAL TISSUE; ENZYME ACTIVITY; ENZYME INDUCTION; ENZYME KINETICS; ENZYME SUBUNIT; EXPOSURE; FEMALE; FLUORESCENCE ANALYSIS; GESTATION PERIOD; GLUTATHIONE METABOLISM; IMMUNOBLOTTING; IN VITRO STUDY; LINEAR SYSTEM; NIDATION; NONHUMAN; PROTEIN CONTENT; PROTEIN EXPRESSION; QUANTITATIVE ANALYSIS; RAT; REVERSE TRANSCRIPTION POLYMERASE CHAIN REACTION; TIME; TISSUE HOMOGENATE; YOLK SAC;

ANIMALS; BLASTOCYST; CHROMATOGRAPHY, HIGH PRESSURE LIQUID; DIPEPTIDES; DNA PRIMERS; ENZYME INDUCTION; FEMALE; GLUTAMATE-CYSTEINE LIGASE; GLUTATHIONE; IMMUNOBLOTTING; OXIDATIVE STRESS; PREGNANCY; RATS; RATS, SPRAGUE-DAWLEY; REVERSE TRANSCRIPTASE POLYMERASE CHAIN REACTION; RNA, MESSENGER; YOLK SAC;

EID: 5744247195     PISSN: 10966080     EISSN: None     Source Type: Journal    
DOI: 10.1093/toxsci/kfh154     Document Type: Article

References (40)

1. Abate, C., Patel, L., and Rauscher, F. J. 3rd (1990). Curran T. Redox regulation of fos and jun DNA-binding activity in vitro. Science 249(4973), 1157-1161.
2. Beckman, D. A., Pubarelli, J. E., Jensen, M., Koszalka, T. R., Brent, R. L., and Lloyd, J. B. (1990). Sources of amino acids for protein synthesis during early organogenesis in the rat. I. Relative concentrations of free amino acids and proteins. Placenta 11, 109-121.
3. Berberian, R. M., Eurich, G. E., Rios, G. A., and Harris, C. (1996). Formation of glutathione adducts and 2-aminofluorene from 2-nitrosofluorene in post-implantation rat conceptuses in vitro. Reprod. Toxicol. 10, 273-284.
4. Choe, H., Hansen, J. M., and Harris, C. (2001). Spatial and temporal ontogenies of glutathione peroxidase and glutathione disulfide reductase during development of the prenatal rat. J. Biochem. Mol. Toxicol. 15, 197-206.
5. Cotgreave, I. A., and Gerdes, R. G. (1998). Recent trends in glutathione biochemistry - glutathione-protein interactions: A molecular link between oxidative stress and cell proliferation. Biochem. Biophys Res. Commun. 242, 1-9.
6. Diaz, D., Krejsa, C. M., and Kavanagh, T. J. (2002). Expression of glutamate-cysteine ligase during mouse development. Mol. Reprod. Dev. 62, 83-91.
7. Erickson, A. M., Nevarea, Z., Gipp, J. J., and Mulcahy, R. T. (2002). Identification of a variant antioxidant response element in the promoter of the human glutamate-cysteine ligase modifier subunit gene. Revision of the ARE consensus sequence. J. Biol. Chem. 277, 30730-30737.
8. Fenton, S. S., and Fahey, R. C. (1986). Analysis of biological thiols: Determination of thiol components of disulfides and thioesters. Anal. Biochem. 154, 34-42.
9. Gardiner, C. S., and Reed, D. J. (1995). Synthesis of glutathione in the pre-implantation mouse embryo. Arch. Biochem. Biophys. 318, 30-36.
10. Hagen, T. W., and Jones, D. P. (1987). Transepithelial transport of glutathione in vascularly perfused small intestine of rat. Am. J. Physiol. 252, G607-G613.
11. Hansen, J. M., Carney, E. W., and Harris, C. (1999). Differential alteration by thalidomide of the glutathione content of rat vs. rabbit conceptuses in vitro. Reprod. Toxicol. 13, 547-554.
12. Harris, C. (1993). Glutathione biosynthesis in the postimplantation rat conceptus in vitro. Toxicol. Appl. Pharmacol. 120, 247-256.
13. Harris, C., Hiranruengchok, R., Lee, E., Berberian, R. M., and Eurich, G. E. (1995). Glutathione status in chemical embryotoxicity: Synthesis, turnover and adduct formation. Toxicol. in vitro 9, 623-631.
14. Harris, C., Stark, K. L., and Juchau, M. R. (1988). Glutathione status and the incidence of neural tube defects elicited by direct acting teratogens in vitro. Teratology 37, 577-590.
15. Hiranruengchok, R., and Harris, C. (1993) Glutathione oxidation and embryo-toxicity elicited by diamide in the developing rat conceptus in vitro. Toxicol. Appl. Pharmacol. 120, 62-71.
16. Hiranruengchok, R., and Harris, C. (1995a). Diamide-induced alterations of intracellular thiol status and the regulation of glucose metabolism in the developing rat conceptus in vitro. Teratology 52, 205-214.
17. Hiranruengchok, R., and Harris, C. (1995b). Formation of protein-glutathione mixed disulfides in the developing rat conceptus following diamide treatment in vitro. Teratology 52, 196-204.
18. Jones, T. W., Thor, H., and Orrenius, S. (1986). Cellular defense mechanisms against toxic substances. Arch. Toxicol. Suppl. 9, 259-271.
19. Kaplowitz, N., Aw, T. Y., and Ookhtens, M. (1985). The regulation of hepatic GSH. Annu. Rev. Pharmacol. Toxicol. 25, 714-744.
20. Kosower, N. S., and Kosower, E. M. (1978). The glutathione status of cells. Int. Rev. Cytol. 54, 109-160.
21. Lash, L. H., and Jones, D. P. (1983). Transport of glutathione by renal basal-lateral membrane vesicles. Biochem. Biophys. Res. Comm. 112, 55-60.
22. Lee, E., and Harris, C. (1995). Differential chemical modulation of glutathione and cysteine status in rat embryo and visceral yolk sac in vitro: Microinjection and addition to the culture medium. In Vitro Toxicol. 8, 129-138.
23. Meister, A. (1974). Glutathione synthesis. In The Enzymes (P. D. Boyer, Ed.), pp. 671-697. Academic Press, New York.
24. Meister, A. (1984). New aspects of glutathione biochemistry and transport: Selective alteration of glutathione metaboism. Fed. Proc. 43, 3031-3042.
25. Meister, A., and Anderson, M. E. (1983). Glutathione. Ann. Rev. Biochem. 52, 711-760.
26. Orlowski, M., and Meister, A. (1971). Isolation of highly purified γ-glutamyl-cysteine synthetase from rat kidney. Biochemistry 10, 372-380.
27. Ozolins, R. S., and Hales, B. F. (1997) Oxidative stress regulates the expression and activity of transcription factor activator protein-1 in rat conceptus. J. Pharmacol. Exp. Ther. 280, 1085-1093.
28. Ozolins, R. S., and Hales, B. F. (1999a). Post-translational regulation of AP-1 transcription factor DNA-binding activity in the rat conceptus. Mol. Pharmacol. 56, 537-544.
29. Ozolins, R. S., and Hales, B. F. (1999b). Tissue-specific regulation of glutathione homeostasis and the activator protein-1 (AP-1) response in the rat conceptus. Biochem. Pharmacol. 57, 1165-1175.
30. Ozolins, T. R, Harrouk, W., Doerksen, T., Trasler, J. M., and Hales, B. F. (2002). Buthionine sulfoximine embryotoxicity is associated with prolonged AP-1 activation. Teratology 66, 192-200.
31. Richman, P., and Meister, A. (1975). Regulation of γ-glutamyl-cysteine synthetase by nonallosteric feedback inhibition by glutathione. J. Biol. Chem. 250, 1422-1426.
32. Schafer, F. Q., and Buettner, G. R. (2001). Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Rad. Biol. Med. 30, 1191-1212.
33. Seelig, G. F., and Meister, A. (1985a). Glutathione biosynthesis; γ-glutamyl-cysteine synthetase from rat kidney. Methods Enzymol. 113, 379-390.
34. Seelig, G. F., and Meister, A. (1985b). γ-Glutamylcysteine synthetase from erythrocytes. Methods Enzymol. 113, 390-392.
35. Slott, V. L., and Hales, B. F. (1987). Protection of rat embryos in culture against the embryotoxicity of acrolein using exogenous glutathione. Biochem. Pharmacol. 36, 2187-2194.
36. Snoke, J. E., and Bloch, K. (1954). The biosynthesis of glutathione. In Glutathione - a symposium (S. Colowick, A. Lazarow, E. Racker, D. R. Schwarz, E. Stadtman, and H. Waelsch, Eds.), pp. 129-41. Academic Press, New York.
37. Solis, W. A., Dalton, T. P., Dieter, M. Z., Freshwater, S., Harrer, J. M., He, L., Shertzer, H. G., and Nebert, D. W. (2002). Glutamate-cysteine ligase modifier subunit: Mouse Gclm gene structure and regulation by agents that cause oxidative stress. Biochem. Pharmacol. 63, 1739-1754.
38. Stark, K. L., Harris, C., and Juchau, M. R. (1987). Embryotoxicity elicited by inhibition of γ-glutamyltransferase by acivicin and transferase antibodies in cultured rat embryos. Toxicol. Appl. Pharmacol. 89, 88-96.
39. Thompson, S. A., White, C. C., Krejsa, C. M., Eaton, D. L., and Kavanagh, T. J. (2000). Modulation of glutathione and glutamate-L-cysteine ligase by methyl-mercury during mouse development. Toxicol. Sci. 57, 141-146.
40. Tsuchiya, K., Mulcahy, R. T., Reid, L. L., Disteche, C. M., and Kavanagh, T. J. (1995). Mapping of the glutamate-cysteine ligase catalytic subunit gene (GLCLC) to human chromosome 6p12 and mouse chromosome 9D-E and of the regulatory subunit gene (GLCLR) to human chromosome 1p21-p22 and mouse chromosome 3H1-3. Genomics 30, 630-632.