A method for measuring disulfide reduction by cultured mammalian cells: Relative contributions of glutathione-dependent and glutathione-independent mechanisms

Analytical Biochemistry

Volumn 281, Issue 1, 2000, Pages 77-86

  Biaglow, John E ^a   Donahue, Jerry ^a   Tuttle, Steve ^a   Held, Kathryn ^b   Chrestensen, Carol ^c   Mieyal, John ^c  

^a UNIVERSITY OF PENNSYLVANIA   (United States)

^b HARVARD UNIVERSITY   (United States)

^c CASE WESTERN RESERVE UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

A549 lung carcinoma; Chinese hamster ovary cells with and without the enzyme G6PD; DU145 prostate carcinoma; Glucose; MCF7 mammary carcinoma; Rodent cells

Indexed keywords

BIOLOGICAL ORGANS; CELL CULTURE; ENZYMES; GLUCOSE; MAMMALS; PEPTIDES; SULFUR COMPOUNDS; TUMORS; UROLOGY;

CHINESE HAMSTER OVARY CELLS; DISULFIDE REDUCTION; GLUCOSE 6 PHOSPHATES; GLUTATHIONE DISULFIDE; LUNG CARCINOMA; MAMMARY CARCINOMA; PROSTATE CARCINOMA; RELATIVE CONTRIBUTION;

CELLS;

ALPHA LIPOATE; ARSENIC TRIOXIDE; ARSENOSOBENZENE; CARMUSTINE; CYSTAMINE; DISULFIDE; DITHIOTHREITOL; GLUTATHIONE PEROXIDASE; HYDROXYETHYL DISULFIDE; OXIDOREDUCTASE; UNCLASSIFIED DRUG;

ANALYTIC METHOD; ANIMAL CELL; ARTICLE; CHEMICAL REACTION KINETICS; CONTROLLED STUDY; DISULFIDE BOND; ENZYME INHIBITION; GLUCOSE 6 PHOSPHATE DEHYDROGENASE DEFICIENCY; GLUTATHIONE METABOLISM; HUMAN; HUMAN CELL; NONHUMAN; PRIORITY JOURNAL; QUANTITATIVE DIAGNOSIS; RAT; REDUCTION;

ANIMALIA; CRICETINAE; CRICETULUS GRISEUS; MAMMALIA; RODENTIA;

EID: 0034658104     PISSN: 00032697     EISSN: None     Source Type: Journal    
DOI: 10.1006/abio.2000.4533     Document Type: Article

References (46)

1. Gravina S. A., Mieyal J. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry. 32:1993;3368-3376.
2. Starke D. W., Chen Y. C., Bapna C. P., Lesnefsky E. J., Mieyal J. J. Sensitivity of protein sulfhydryl repair enzymes to oxidative stress. Free Radic. Biol. Med. 23:1997;373-384.
3. Mieyal J. J., Gravina S. A., Mieyal P. A., Srinivaan U., Stark D. W. Glutathionyl specificity of thioltransferase: mechanistic and physiological implications. Packer L., Cardenas E. Biothols in Health and Disease. 1995;14-372 Dekker, New York.
4. Srinivasan U., Mieyal P. A., Mieyal J. J. pH profiles indicative of rate limiting nucleophilic displacement in thioltransferase (glutaredoxin) catalysis. Biochemistry. 16:1997;3199-3205.
5. Yang Y., Jao S. C., Nanduri S., Starke D. W., Mieyal J. J., Qin J. Reactivity of the human thioltransferase C7S, C25S, C78S, C82S mutant and NMR solution structure of its glutathionyl mixed disulfide intermediate reflect catalytic specificity. Biochemistry. 37:1998;17145-11756.
6. Powis G., Briehl M., Oblong J. Redox signaling and the control of cell growth and death. Pharmacol. Ther. 68:1995;149-173.
7. Powis G., Gasdaska J. R., Baker A. Redox signaling and the control of cell growth and death. 1997;Academic Press, New York. p. 329-359.
8. Tuttle S. E., Biaglow J. E. Sensitivity to chemical oxidants and radiation in CHO lines deficient in oxidative pentose cycle activity. Int. J. Radiat. Oncol. Biol. Phys. 22:1992;671-675.
9. Biaglow J. B., Tuttle S., Evans S. MIBG inhibits respiration: Potential for radio and hyperthermic sensitization. Int. J. Radiat. Biol. Phys. 42:1998;871-876.
10. Voet D., Voet J. G. Biochemistry. 1995;Wiley, New York. p. 617-623.
11. Constantinescu A., Pick U., Handelman G. J., Haramaki N., Han D., Podda M., Tritschler H. J., Packer L. Reduction and transport of lipoate by human erythrocytes. Biochem. Pharmacol. 50:1995;253-261.
12. Bustamante J., Lodge J. K. M., Marcoccl L., Tritschler H. J., Packer L., Rihn B. H. α-Lipoate in liver metabolism and disease. Free Radic. Biol. Med. 24:1998;1023-1039.
13. Packer L., Roy S., Sem C. K. α-Lipoate: A metabolic antioxidant and potential redox modulator of transcription. Adv. Pharmacol. 38:1997;79-101.
14. Arner E. S. J., Nordberg J., Holmgren A. Effect of reduction of lipoamide and lipoic acid by mammalian thioredoxin reductase, thioredoxin. Biochem. Biophys. Res. Commun. 225:1996;268-274.
15. Wells W. W., Peng X., Yang Y., Rocue P. A. Mammalian thiotransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265:1990;15361-15364.
16. Han D., Handelman G., Marcocci L., Sen K. S., Sashwati R., Hiortusu H., Tritscher H. J., Flohe L., Packer L. Lipoic acid increases de novo synthesis of cellular glutathione by improving cystine utilization. Biofactors. 6:1997;321-338.
17. Mantusogo S., Yan L. J., Tritscher H. J., Packer L. Elucidation of antioxidant activity of α-lipoic acid toward hydroxyl radical. Biochem. Biophys. Res. Commun. 208:1995;161-167.
18. Kahler W., Kuklinski B., Ruhlman C., Plotz C. Diabetes mellitus - A free radical-associated disease: Effects of adjuvant supplementation of antioxidants. Griwes F. A., Wessel K. H. The Role of Antioxidants in Diabetes Mellitus: Oxygen Radicals and Antioxidants in Diabetes. 1980;33-53 Thieme, Stuttgart.
19. Sen C. K. Redox signaling and the emerging therapeutic potential of thiol antioxidants. Biochem. Pharmacol. 55:1998;1747-1758.
20. Delmonte M., Cerconi I., Buono F., Vilardo P. G., Del Corsd A., Mura U. Thioltransferase activity of bovine lens glutathione S-transferase. Biochem. J. 334:1998;57-62.
21. Anderson M. E. Glutathione and glutathione delivery systems. Antioxidants in Disease Mechanisms and Therapy. 1997;Academic Press, New York. p. 61-74.
22. Jocelyn P. C. Biochemistry of the SH Group. 1972;Academic Press, New York. p. 324-325.
23. Held K., Biaglow J. E. Mechanisms for the oxygen radical mediated toxicity of various thiol containing compounds in cultured mammalian cells. Radiat. Res. 139:1994;5-23.
24. Biaglow J. E., Held K. Cellular oxygen utilization and hypoxia: Interaction of dithiols with cellular electron transfer systems. Adv. Exp. Med. Biol. 200:1986;591-601.
25. Tietze E. Enzymatic method for quantitative determination of nanogram amounts of total and oxidized glutathione. Methods Enzymol. 27:1969;305-322.
26. Ziegler D. M. Role of reversible oxidation reduction of enzyme thiol-disulfides in metabolic regulation. Annu. Rev. Biochem. 54:1985;305-329.
27. Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 364:1989;13963-13967.
28. Biaglow J. E., Clark E. P., Epp E. R., Morse-Gaudio M., Varnes M. E., Mitchell J. B. Non-protein thiols and the radiation response of A549 human lung carcinoma cells. Int. J. Radiat. Biol. 44:1983;489-495.
29. Frischer H., Ahmad T. Severe generalized glutathione reductase deficiency after antitumor chemotherapy with BICNU [1,3-bis(chloroethyl)-1-nitrosourea]. J. Clin. Invest. 89:1987;1080-1091.
30. Schallreuter K. U., Gleason F. K., Wood J. M. The mechanism of action of the nitrosourea anti-tumor drugs on thioredoxin reductase, glutathione reductase and ribonucleotide reductase. Biochim. Biophys. Acta. 1054:1990;14-22.
31. Baker M. A., Hagner B. Diamide induced shift in protein and glutathione thiol: Disulfide status delays DNA rejoining X-irradiation of human cancer cells. Biochim. Biophys. Acta. 1037:1990;39-47.
32. Bjornstedt M., Kumar S., Holmgren A. Selenite and selenodiglutathione: Reactions with thioredoxin systems. Methods Enzymol. 252:1995;209-219.
33. Miller R. M., Park E. M., Thomas J. A. Reduction (dethiolation) of protein mixed disulfides: Distribution and specificity of dethiolating enzymes and N,N′-bis(2-chloroethyl)-N-nitrosourea inhibition of an NADPH-dependent cardiac dethiolase. Arch. Biochem. Biophys. 15:1991;112-120.
34. Luthman M., Holmgren A. Rat liver thioredoxin and thioredoxin reductase: Purification and characterization. Biochemistry. 26:1982;6628-6633.
35. Park E. M., Thomas J. A. The mechanisms of reduction of protein mixed disulfides (dethiolation) in cardiac tissue. Arch. Biochem. Biophys. 274:1989;47-54.
36. Stewart M. S., Spalholtz J. E., Needle K. H., Pende B. C. Selenium compounds have disparate abilities to impose oxidative stress and induce apoptosis. Free Radic. Biol. Med. 26:1999;42-48.
37. Webb J. L. Enzyme and Metabolic Inhibitors. 1966;Academic Press, New York. p. 602-656.
38. Joshi S., Hughes J. B. Inhibition of coupling factor B activity by cadmium ion, arsenite-2,3-dimercaptopropanol, and phenylarsine oxide, and preferential reactivation by dithiols. J. Biol. Chem. 256:1981;11112-11116.
39. Biaglow J. E., Varnes M. E. Factors influencing the oxidation of cysteamine and other thiols: Implications for hyperthermic sensitization and radiation protection. Radiat. Res. 100:1984;298-312.
40. Kachur A. V., Koch C. J., Biaglow J. E. Mechanism of copper-catalyzed autoxidation of cysteine. Free Radic. Res. 31:1999;23-34.
41. Sato N., Iwata S., Nakamura K., Hori T., Mori K., Yodoi J. Thiol-mediated redox regulation of apoptosis. Possible roles of cellular thiols other than glutathione in T cell apoptosis. J. Immunol. 154:1995;3194-3203.
42. Mitchell J. B., Russo A., Biaglow J. E. Role of glutathione and other endogenous thiols in radiation response. Pharmacol. Ther. 39:1988;269-274.
43. Biaglow J. E., Nygaard O. F. The use of the oxidant diamide for studying the non-mitochondrial reducing capacity of Ehrlich ascites tumor cells. Biochem. Biophys. Res. Commun. 54:1973;874-881.
44. Gitler C., Londner M. Use of p-nitrophenyl disulfide to measure reductive capacity of intact cells. Methods Enzymol. 251:1995;279-286.
45. Biaglow J. E., Varnes M. E. Cellular protection against damage by hydroperoxides: Role of glutathione. Basic Life Sci. 49:1988;567-573.
46. Srinivasan U. Studies on the Properties and Selective Inhibition of Thioltransferase. 1998.