Protocols for the Detection of S-Glutathionylated and S-Nitrosylated Proteins In Situ

Methods in Enzymology

Volumn 474, Issue , 2010, Pages 289-296

  Aesif, Scott W ^a   Janssen Heininger, Yvonne M W ^a   Reynaert, Niki L ^b  

^a UNIVERSITY OF VERMONT COLLEGE OF MEDICINE   (United States)

^b MAASTRICHT UNIVERSITY   (Netherlands)

Author keywords

[No Author keywords available]

Indexed keywords

GLUTATHIONE; S NITROSOGLUTATHIONE; S NITROSOTHIOL;

ANIMAL; ARTICLE; CHEMISTRY; CYTOLOGY; HISTOLOGY; LUNG;

ANIMALS; GLUTATHIONE; HISTOCYTOLOGICAL PREPARATION TECHNIQUES; LUNG; S-NITROSOGLUTATHIONE; S-NITROSOTHIOLS;

MLCS; MLOWN;

EID: 79251483598     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)74017-9     Document Type: Chapter

References (28)

1. Aesif, S.W., et al. In situ analysis of protein S-glutathionylation in lung tissue using glutaredoxin-1-catalyzed cysteine derivatization. Am. J. Pathol. 175 (2009), 36–45.
2. Anathy, V., et al. Redox amplification of apoptosis by caspase-dependent cleavage of glutaredoxin 1 and S-glutathionylation of Fas. J. Cell Biol. 184 (2009), 241–252.
3. Benhar, M., et al. Protein denitrosylation: Enzymatic mechanisms and cellular functions. Nat. Rev. Mol. Cell Biol. 10 (2009), 721–732.
4. Chrestensen, C.A., et al. Acute cadmium exposure inactivates thioltransferase (Glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. J. Biol. Chem. 275 (2000), 26556–26565.
5. Ckless, K., et al. In situ detection and visualization of S-nitrosylated proteins following chemical derivatization: Identification of Ran GTPase as a target for S-nitrosylation. Nitric Oxide 11 (2004), 216–227.
6. Dalle-Donne, I., et al. S-glutathionylation in protein redox regulation. Free Radic. Biol. Med. 43 (2007), 883–898.
7. Dalle-Donne, I., et al. Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid. Redox Signal. 10 (2008), 445–473.
8. Forrester, M.T., et al. Detection of protein S-nitrosylation with the biotin-switch technique. Free Radic. Biol. Med. 46 (2009), 119–126.
9. Gallogly, M.M., Mieyal, J.J., Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr. Opin. Pharmacol. 7 (2007), 381–391.
10. Ghezzi, P., Regulation of protein function by glutathionylation. Free Radic. Res. 39 (2005), 573–580.
11. Giles, G.I., et al. Evaluation of sulfur, selenium and tellurium catalysts with antioxidant potential. Org. Biomol. Chem. 1 (2003), 4317–4322.
12. Gow, A.J., et al. Basal and stimulated protein S-nitrosylation in multiple cell types and tissues. J. Biol. Chem. 277 (2002), 9637–9640.
13. Hess, D.T., et al. Protein S-nitrosylation: Purview and parameters. Nat. Rev. Mol. Cell Biol. 6 (2005), 150–166.
14. Holmgren, A., Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. USA 73 (1976), 2275–2279.
15. Holmgren, A., et al. Thiroedoxin from Escherichia coli. Radioimmunological and enzymatic determinations in wild type cells and mutants defective in phage T7 DNA replication. J. Biol. Chem. 253 (1978), 430–436.
16. Holmgren, A., et al. Thiol redox control via thioredoxin and glutaredoxin systems. Biochem. Soc. Trans. 33 (2005), 1375–1377.
17. Jacob, C., et al. Sulfur and selenium: the role of oxidation state in protein structure and function. Angew. Chem. Int. Ed. Engl. 42 (2003), 4742–4758.
18. Jaffrey, S.R., Snyder, S.H., The biotin switch method for the detection of S-nitrosylated proteins. Sci. STKE, 2001, 2001, pl1.
19. Janssen-Heininger, Y.M., et al. Redox-based regulation of signal transduction: Principles, pitfalls, and promises. Free Radic. Biol. Med. 45 (2008), 1–17.
20. Ji, Y., et al. S-nitrosylation and S-glutathiolation of protein sulfhydryls by S-nitroso glutathione. Arch. Biochem. Biophys. 362 (1999), 67–78.
21. Kim, S.O., et al. OxyR: A molecular code for redox-related signaling. Cell 109 (2002), 383–396.
22. Mallis, R.J., Thomas, J.A., Effect of S-nitrosothiols on cellular glutathione and reactive protein sulfhydryls. Arch. Biochem. Biophys. 383 (2000), 60–69.
23. Meng, T.C., et al. Reversible oxidation and inactivation of protein tyrosine phosphatases in vivo. Mol. Cell 9 (2002), 387–399.
24. Pineda-Molina, E., et al. Glutathionylation of the p50 subunit of NF-kappaB: A mechanism for redox-induced inhibition of DNA binding. Biochemistry 40 (2001), 14134–14142.
25. Reynaert, N.L., et al. In situ detection of S-glutathionylated proteins following glutaredoxin-1 catalyzed cysteine derivatization. Biochim. Biophys. Acta 1760 (2006), 380–387.
26. Shelton, M.D., et al. Glutaredoxin: Role in reversible protein S-glutathionylation and regulation of redox signal transduction and protein translocation. Antioxid. Redox Signal. 7 (2005), 348–366.
27. Stamler, J.S., et al. Nitrosylation. The prototypic redox-based signaling mechanism. Cell 106 (2001), 675–683.
28. Takashima, Y., et al. Differential expression of glutaredoxin and thioredoxin during monocytic differentiation. Immunol. Lett. 68 (1999), 397–401.