Assessment of endoplasmic reticulum glutathione redox status is confounded by extensive ex vivo oxidation

Antioxidants and Redox Signaling

Volumn 10, Issue 5, 2008, Pages 963-972

  Dixon, Brian M ^a   Heath, Shi Hua D ^a   Kim, Robert ^b   Suh, Jung H ^b   Hagen, Tory M ^a  

^a OREGON STATE UNIVERSITY   (United States)

^b CHILDREN S HOSPITAL OAKLAND RESEARCH INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE; GLUTATHIONE DISULFIDE; IODOACETIC ACID; OXIDOREDUCTASE;

ANIMAL CELL; ANIMAL TISSUE; ARTICLE; CONTROLLED STUDY; ENDOPLASMIC RETICULUM; ENZYME ACTIVITY; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; LIVER MICROSOME; NONHUMAN; OXIDATION; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL; PROTEIN ANALYSIS; RAT; WESTERN BLOTTING;

ANIMALS; ENDOPLASMIC RETICULUM; ENZYME INHIBITORS; GLUTATHIONE; GLUTATHIONE DISULFIDE; IODOACETIC ACID; MICROSOMES, LIVER; OXIDATION-REDUCTION; RATS; RATS, INBRED F344;

RATTUS;

EID: 39749200944     PISSN: 15230864     EISSN: None     Source Type: Journal    
DOI: 10.1089/ars.2007.1869     Document Type: Article

References (44)

1. Banhegyi G, Benedetti A, Csala M, and Mandl J. Stress on redox. FEBS Lett 581: 3634-3640, 2007.
2. Bass R, Ruddock LW, Klappa P, and Freedman RB. A major fraction of endoplasmic reticulum-located glutathione is present as mixed disulfides with protein. J Biol Chem 279: 5257-5262, 2004.
3. Burns JA, Butler JC, Moran J, and Whitesides GM. Selective reduction of disulfides by tris(2-carboxythyl)phosphine. J Org Chem 56: 2648-2650, 1991.
4. Carelli S, Ceriotti A, Cabibbo A, Fassina G, Ruvo M, and Sitia R. Cysteine and glutathione secretion in response to protein disulfide bond formation in the ER. Science 277: 1681-1684, 1997.
5. Chakravarthi S and Bulleid NJ. Glutathione is required to regulate the formation of native disulfide bonds within proteins entering the secretory pathway. J Biol Chem 279: 39872-39879, 2004.
6. Chakravarthi S, Jessop CE, and Bulleid NJ. The role of glutathione in disulphide bond formation and endoplasmic-reticulum-generated oxidative stress. EMBO Rep 7: 271-275, 2006.
7. Csala M, Fulceri R, Mandl J, Benedetti A, and Banhegyi G. Glutathione transport in the endo/sarcoplasmic reticulum. Biofactors 17: 27-35, 2003.
8. Duggan PF and Martonosi A. Sarcoplasmic reticulum: The permeability of sarcoplasmic reticulum membranes. J Gen Physiol 56: 147-167, 1970.
9. Ellgaard L. Catalysis of disulphide bond formation in the endoplasmic reticulum. Biochem Soc Trans 32: 663-667, 2004.
10. Fariss MW and Reed DJ. High-performance liquid chromatography of thiols and disulfides: dinitrophenol derivatives. Methods Enzymol 143: 101-109, 1987.
11. Gorlach A, Klappa P, and Kietzmann T. The endoplasmic reticulum: folding, calcium homeostasis, signaling, and redox control. Antioxid Redox Signal 8: 1391-1418, 2006.
12. Hagen TM, Ingersoll RT, Lykkesfeldt J, Liu J, Wehr CM, Vinarsky V, Bartholomew JC, and Ames AB. (R)-alpha-lipoic acid-supplemented old rats have improved mitochondrial function, decreased oxidative damage, and increased metabolic rate. FASEB J 13: 411-418, 1999.
13. Hagen TM, Ingersoll RT, Wehr CM, Lykkesfeldt J, Vinarsky V, Bartholomew JC, Song MH, and Ames BN. Acetyl-L-carnitine fed to old rats partially restores mitochondrial function and ambulatory activity. Proc Natl Acad Sci USA 95: 9562-9566, 1998.
14. Hagen TM, Vinarsky V, Wehr CM, and Ames BN. (R)-alpha-lipoic acid reverses the age-associated increase in susceptibility of hepatocytes to tert-butylhydroperoxide both in vitro and in vivo. Antioxid Redox Signal 2: 473-483, 2000.
15. Hirs CH. Reduction and S- carboxymethylation of proteins. In: Methods in Enzymology, Hirs CH, ed. New York: Academic Press, 1967, pp. 199-203.
16. Holmgren A. Thioredoxin catalyzes the reduction of insulin disulfides by dithiothreitol and dihydrolipoamide. J Biol Chem 254: 9627-9632, 1979.
17. Hwang C, Sinskey AJ, and Lodish HF. Oxidized redox state of glutathione in the endoplasmic reticulum. Science 257: 1496-1502, 1992.
18. Jocelyn PC. Biochemistry of SH Group. New York, Academic Press, 1972, p. 94.
19. Jones DP, Carlson JL, Samiec PS, Sternberg P, Jr., Mody VC, Jr., Reed RL, and Brown LA. Glutathione measurement in human plasma. Evaluation of sample collection, storage and derivatization conditions for analysis of dansyl derivatives by HPLC. Clin Chim Acta 275: 175-184, 1998.
20. Koivu J and Myllyla R. Interchain disulfide bond formation in types I and II procollagen. Evidence for a protein disulfide isomerase catalyzing bond formation. J Biol Chem 262: 6159-6164, 1987.
21. Krueger SK, Yueh MF, Martin SR, Pereira CB, and Williams DE. Characterization of expressed full-length and truncated FMO2 from rhesus monkey. Drug Metab Dispos 29: 693-700, 2001.
22. Liu G and Pessah IN. Molecular interaction between ryanodine receptor and glycoprotein triadin involves redox cycling of functionally important hyperreactive sulfhydryls. J Biol Chem 269: 33028-33034, 1994.
23. Lundstrom-Ljung J and Holmgren A. Glutaredoxin accelerates glutathione-dependent folding of reduced ribonuclease A together with protein disulfide-isomerase. J Biol Chem 270: 7822-7828, 1995.
24. Lyles MM and Gilbert HF. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: dependence of the rate on the composition of the redox buffer. Biochemistry 30: 613-619, 1991.
25. Lyles MM and Gilbert HF. Catalysis of the oxidative folding of ribonuclease A by protein disulfide isomerase: pre-steady-state kinetics and the utilization of the oxidizing equivalents of the isomerase. Biochemistry 30: 619-625, 1991.
26. Marciniak SJ and Ron D. Endoplasmic reticulum stress signaling in disease. Physiol Rev 86: 1133-1149, 2006.
27. Mezghrani A, Fassio A, Benham A, Simmen T, Braakman I, and Sitia R. Manipulation of oxidative protein folding and PDI redox state in mammalian cells. EMBO J 20: 6288-6296, 2001.
28. Molteni SN, Fassio A, Ciriolo MR, Filomeni G, Pasqualetto E, Fagioli C, and Sitia R. Glutathione limits Ero1-dependent oxidation in the endoplasmic reticulum. J Biol Chem 279: 32667-32673, 2004.
29. Narayan M, Welker E, Wedemeyer WJ, and Scheraga HA. Oxidative folding of proteins. Acc Chem Res 33: 805-812, 2000.
30. Nardai G, Korcsmaros T, Papp E, and Csermely P. Reduction of the endoplasmic reticulum accompanies the oxidative damage of diabetes mellitus. Biofactors 17: 259-267, 2003.
31. Nardai G, Stadler K, Papp E, Korcsmaros T, Jakus J, and Csermely P. Diabetic changes in the redox status of the microsomal protein folding machinery. Biochem Biophys Res Commun 334: 787-795, 2005.
32. Petersen JG and Dorrington KJ. An in vitro system for studying the kinetics of interchain disulfide bond formation in immunoglobulin G. J Biol Chem 249: 5633-5641, 1974.
33. Saxena VP and Wetlaufer DB. Formation of three-dimensional structure in proteins. I. Rapid nonenzymic reactivation of reduced lysozyme. Biochemistry 9: 5015-5023, 1970.
34. Schafer FQ and Buettner GR. Redox environment of the cell as viewed through the redox state of the glutathione disulfide/glutathione couple. Free Radic Biol Med 30: 1191-1212, 2001.
35. Schroder M and Kaufman RJ. ER stress and the unfolded protein response. Mutat Res 569: 29-63, 2005.
36. Schwaller M, Wilkinson B, and Gilbert RF. Reduction-reoxidation cycles contribute to catalysis of disulfide isomerization by protein-disulfide isomerase. J Biol Chem 278: 7154-7159, 2003.
37. Share L and Hansrote RW. Permeability of rat liver microsomes to sucrose and carboxypolyglucose in vitro. J Biophys Biochem Cytol 7: 239-242, 1960.
38. Smith AR, Visioli F, and Hagen TM. Vitamin C matters: increased oxidative stress in cultured human aortic endothelial cells without supplemental ascorbic acid. FASEB J 16: 1102-1104, 2002.
39. Suh JH, Heath SH, and Hagen TM. Two subpopulations of mitochondria in the aging rat heart display heterogenous levels of oxidative stress. Free Radic Biol Med 35: 1064-1072, 2003.
40. Sun J, Xu L, Eu JP, Stamler JS, and Meissner G. Classes of thiols that influence the activity of the skeletal muscle calcium release channel. J Biol Chem 276: 15625-15630, 2001.
41. Wetlaufer DB, Branca PA, and Chen GX. The oxidative folding of proteins by disulfide plus thiol does not correlate with redox potential. Protein Eng 1: 141-146, 1987.
42. Xia R, Stangler T, and Abramson JJ. Skeletal muscle ryanodine receptor is a redox sensor with a well defined redox potential that is sensitive to channel modulators. J Biol Chem 275: 36556-36561, 2000.
43. Yoshida H. ER stress and diseases. FEBS J 274: 630-658, 2007.
44. Zable AC, Favero TG, and Abramson JJ. Glutathione modulates ryanodine receptor from skeletal muscle sarcoplasmic reticulum. Evidence for redox regulation of the Ca2+ release mechanism. J Biol Chem 272: 7069-7077, 1997.