Redox Clamp Model for Study of Extracellular Thiols and Disulfides in Redox Signaling

Methods in Enzymology

Volumn 474, Issue , 2010, Pages 165-179

  Go, Young Mi ^a   Jones, Dean P ^a  

^a EMORY UNIVERSITY SCHOOL OF MEDICINE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

DISULFIDE; THIOL DERIVATIVE;

ANIMAL; ARTICLE; BIOLOGICAL MODEL; CELL CULTURE; CHEMISTRY; EXTRACELLULAR SPACE; HUMAN; OXIDATION REDUCTION REACTION; SIGNAL TRANSDUCTION; TUMOR CELL LINE;

ANIMALS; CELL LINE, TUMOR; CELLS, CULTURED; DISULFIDES; EXTRACELLULAR SPACE; HUMANS; MODELS, BIOLOGICAL; OXIDATION-REDUCTION; SIGNAL TRANSDUCTION; SULFHYDRYL COMPOUNDS;

MLCS; MLOWN;

EID: 77957297487     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)74010-6     Document Type: Chapter

References (25)

1. Anderson, C.L., Iyer, S.S., Ziegler, T.R., et al. Control of extracellular cysteine/cystine redox state by HT-29 cells is independent of cellular glutathione. Am. J. Physiol. Regul. Integr. Comp. Physiol. 293 (2007), R1069–R1075.
2. Dahm, L.J., Jones, D.P., Rat jejunum controls luminal thiol-disulfide redox. J. Nutr. 130 (2000), 2739–2745.
3. Essex, D.W., Li, M., Redox control of platelet aggregation. Biochemistry 42 (2003), 129–136.
4. Gilbert, H.F., Molecular and cellular aspects of thiol-disulfide exchange. Adv. Enzymol. Relat. Areas Mol. Biol. 63 (1990), 69–172.
5. Go, Y.M., Jones, D.P., Intracellular proatherogenic events and cell adhesion modulated by extracellular thiol/disulfide redox state. Circulation 111 (2005), 2973–2980.
6. Go, Y.M., Jones, D.P., Redox compartmentalization in eukaryotic cells. Biochim. Biophys. Acta 1780 (2008), 1273–1290.
7. Go, Y.M., Park, H., Koval, M., et al. A key role for mitochondria in endothelial signaling by plasma cysteine/cystine redox potential. Free Radic. Biol. Med. 48 (2009), 275–283.
8. Go, Y.M., Craige, S.E., Orr, M., et al. Gene and protein responses of human monocytes to extracellular cysteine redox potential. Toxicol. Sci. 112 (2009), 354–362.
9. Go, Y.M., Pohl, J., Jones, D.P., Quantification of redox conditions in the nucleus. Methods Mol. Biol. 464 (2009), 303–317.
10. Hansen, J.M., Watson, W.H., Jones, D.P., Compartmentation of Nrf-2 redox control: Regulation of cytoplasmic activation by glutathione and DNA binding by thioredoxin-1. Toxicol. Sci. 82 (2004), 308–317.
11. Hwang, C., Sinskey, A.J., The role of oxidation-reduction potential in monitoring growth of cultured mammalian cells. Spier, R.E., Griffiths, J.B., Meignier, B., (eds.) Production of biologicals from animal cells in culture, 991, 1991, Halley Court, Oxford, 548–567.
12. Imhoff, B.R., Hansen, J.M., Extracellular redox status regulates Nrf2 activation through mitochondrial reactive oxygen species. Biochem. J. 424 (2009), 491–500.
13. Iyer, S.S., Accardi, C.J., Ziegler, T.R., et al. Cysteine redox potential determines pro-inflammatory IL-1beta levels. PloS One, 4, 2009, e5017.
14. Jiang, S., Moriarty-Craige, S.E., Orr, M., et al. Oxidant-induced apoptosis in human retinal pigment epithelial cells: Dependence on extracellular redox state. Invest. Ophthalmol. Vis. Sci. 46 (2005), 1054–1061.
15. Jiang, S., Moriarty-Craige, S.E., Li, C., et al. Associations of plasma-soluble fas ligand with aging and age-related macular degeneration. Invest. Ophthalmol. Vis. Sci. 49 (2008), 1345–1349.
16. Jonas, C.R., Ziegler, T.R., Gu, L.H., et al. Extracellular thiol/disulfide redox state affects proliferation rate in a human colon carcinoma (Caco2) cell line. Free Radic. Biol. Med. 33 (2002), 1499–1506.
17. Jonas, C.R., Gu, L.H., Nkabyo, Y.S., et al. Glutamine and KGF each regulate extracellular thiol/disulfide redox and enhance proliferation in Caco-2 cells. Am. J. Physiol. Regul. Integr. Comp. Physiol. 285 (2003), R1421–R1429.
18. Jones, D.P., Liang, Y., Measuring the poise of thiol/disulfide couples in vivo. Free Radic. Biol. Med. 47 (2009), 1329–1338.
19. Jones, D.P., Carlson, J.L., Mody, V.C., et al. Redox state of glutathione in human plasma. Free Radic. Biol. Med. 28 (2000), 625–635.
20. Jones, D.P., Go, Y.-M., Anderson, C.L., et al. Cysteine/cystine couple is a newly recognized node in the circuitry for biologic redox signaling and control. FASEB J. 18 (2004), 1246–1248.
21. Moriarty-Craige, S.E., Adkison, J., Lynn, M., et al. Antioxidant supplements prevent oxidation of cysteine/cystine redox in patients with age-related macular degeneration. Am. J. Ophthalmol. 140 (2005), 1020–1026.
22. Nkabyo, Y.S., Ziegler, T.R., Gu, L.H., et al. Glutathione and thioredoxin redox during differentiation in human colon epithelial (Caco-2) cells. Am. J. Physiol. Gastrointest. Liver Physiol. 283 (2002), G1352–G1359.
23. Nkabyo, Y.S., Go, Y.M., Ziegler, T.R., et al. Extracellular cysteine/cystine redox regulates the p44/p42 MAPK pathway by metalloproteinase-dependent epidermal growth factor receptor signaling. Am. J. Physiol. Gastrointest. Liver Physiol. 289 (2005), G70–G78.
24. Ramirez, A., Ramadan, B., Ritzenthaler, J.D., et al. Extracellular cysteine/cystine redox potential controls lung fibroblast proliferation and matrix expression through upregulation of transforming growth factor-beta. Am. J. Physiol. 293:4 (2007), L972–L981.
25. Reed, D.J., Beatty, P., Sies, H., Wendel, A., (eds.) Functions of Glutathione in Liver and Kidney, 1978, Springer-Verlag, Berlin, 13–21.