Measurement of Extracellular (Exofacial) Versus Intracellular Protein Thiols

Methods in Enzymology

Volumn 474, Issue , 2010, Pages 149-164

  Skalska, Jolanta ^a   Bernstein, Steven ^a   Brookes, Paul ^a  

^a UNIVERSITY OF ROCHESTER MEDICAL CENTER   (United States)

Author keywords

Cysteine; Exofacial; Mitochondria; Redox; Thiol

Indexed keywords

GLUTATHIONE; PROTEIN; THIOL DERIVATIVE;

ANIMAL; ARTICLE; CELL CULTURE; CHEMISTRY; CYTOSOL; ENZYMOLOGY; EXTRACELLULAR SPACE; HUMAN; MITOCHONDRION; OXIDATION REDUCTION REACTION;

ANIMALS; CELLS, CULTURED; CYTOSOL; EXTRACELLULAR SPACE; GLUTATHIONE; HUMANS; MITOCHONDRIA; OXIDATION-REDUCTION; PROTEINS; SULFHYDRYL COMPOUNDS;

MLCS; MLOWN;

EID: 79958051897     PISSN: 00766879     EISSN: 15577988     Source Type: Book Series    
DOI: 10.1016/S0076-6879(10)74009-X     Document Type: Chapter

References (43)

1. Addanki, S., Cahill, F.D., Sotos, J.F., Intramitochondrial pH and intra-extramitochondrial pH gradient of beef heart mitochondria in various functional states. Nature 214 (1967), 400–402.
2. Aesif, S.W., Anathy, V., Havermans, M., Guala, A.S., Ckless, K., Taatjes, D.J., Janssen-Heininger, Y.M., In situ analysis of protein S-glutathionylation in lung tissue using glutaredoxin-1-catalyzed cysteine derivatization. Am. J. Pathol. 175 (2009), 36–45.
3. Banjac, A., Perisic, T., Sato, H., Seiler, A., Bannai, S., Weiss, N., Kolle, P., Tschoep, K., Issels, R.D., Daniel, P.T., Conrad, M., Bornkamm, G.W., The cystine/cysteine cycle: A redox cycle regulating susceptibility versus resistance to cell death. Oncogene 27 (2008), 1618–1628.
4. Beech, D.J., Sukumar, P., Channel regulation by extracellular redox protein. Channels (Austin) 1 (2007), 400–403.
5. Brookes, P.S., Yoon, Y., Robotham, J.L., Anders, M.W., Sheu, S.S., Calcium, ATP, and ROS: A mitochondrial love-hate triangle. Am. J. Physiol. Cell. Physiol. 287 (2004), C817–C833.
6. Burgess, R.R., Deutscher, M.P., Methods in enzymology. Preface. Methods Enzymol. 463 (2009), xxv–xxxvi.
7. Burwell, L.S., Brookes, P.S., Mitochondria as a target for the cardioprotective effects of nitric oxide in ischemia-reperfusion injury. Antioxid. Redox Signal. 10 (2008), 579–599.
8. Ceccarelli, J., Delfino, L., Zappia, E., Castellani, P., Borghi, M., Ferrini, S., Tosetti, F., Rubartelli, A., The redox state of the lung cancer microenvironment depends on the levels of thioredoxin expressed by tumor cells and affects tumor progression and response to prooxidants. Int. J. Cancer 123 (2008), 1770–1778.
9. Chaiswing, L., Bourdeau-Heller, J.M., Zhong, W., Oberley, T.D., Characterization of redox state of two human prostate carcinoma cell lines with different degrees of aggressiveness. Free Radic. Biol. Med. 43 (2007), 202–215.
10. Chaiswing, L., Zhong, W., Cullen, J.J., Oberley, L.W., Oberley, T.D., Extracellular redox state regulates features associated with prostate cancer cell invasion. Cancer Res. 68 (2008), 5820–5826.
11. Circu, M.L., Rodriguez, C., Maloney, R., Moyer, M.P., Aw, T.Y., Contribution of mitochondrial GSH transport to matrix GSH status and colonic epithelial cell apoptosis. Free Radic. Biol. Med. 44 (2008), 768–778.
12. Cox, D.A., Matlib, M.A., A role for the mitochondrial Na(+)-Ca2+ exchanger in the regulation of oxidative phosphorylation in isolated heart mitochondria. J. Biol. Chem. 268 (1993), 938–947.
13. Falk, M.H., Hultner, L., Milner, A., Gregory, C.D., Bornkamm, G.W., Irradiated fibroblasts protect Burkitt lymphoma cells from apoptosis by a mechanism independent of bcl-2. Int. J. Cancer 55 (1993), 485–491.
14. Fang, J., Lu, J., Holmgren, A., Thioredoxin reductase is irreversibly modified by curcumin: A novel molecular mechanism for its anticancer activity. J. Biol. Chem. 280 (2005), 25284–25290.
15. Gelderman, K.A., Hultqvist, M., Holmberg, J., Olofsson, P., Holmdahl, R., T cell surface redox levels determine T cell reactivity and arthritis susceptibility. Proc. Natl. Acad. Sci. USA 103 (2006), 12831–12836.
16. Hedley, D.W., Nicklee, T., Moreno-Merlo, F., Pintilie, M., Fyles, A., Milosevic, M., Hill, R.P., Relations between non-protein sulfydryl levels in the nucleus and cytoplasm, tumor oxygenation, and clinical outcome of patients with uterine cervical carcinoma. Int. J. Radiat. Oncol. Biol. Phys. 61 (2005), 137–144.
17. Hurd, T.R., James, A.M., Lilley, K.S., Murphy, M.P., Chapter 19 Measuring redox changes to mitochondrial protein thiols with redox difference gel electrophoresis (redox-DIGE). Methods Enzymol. 456 (2009), 343–361.
18. Janssen-Heininger, Y.M., Mossman, B.T., Heintz, N.H., Forman, H.J., Kalyanaraman, B., Finkel, T., Stamler, J.S., Rhee, S.G., van der Vliet, A., Redox-based regulation of signal transduction: Principles, pitfalls, and promises. Free Radic. Biol. Med. 45 (2008), 1–17.
19. Kimura, Y., Goto, Y.I., Kimura, H., Hydrogen sulfide increases glutathione production and suppresses oxidative stress in mitochondria. Antioxid. Redox Signal 12 (2010), 1–13.
20. Laragione, T., Bonetto, V., Casoni, F., Massignan, T., Bianchi, G., Gianazza, E., Ghezzi, P., Redox regulation of surface protein thiols: Identification of integrin alpha-4 as a molecular target by using redox proteomics. Proc. Natl. Acad. Sci. USA 100 (2003), 14737–14741.
21. Lilley, K.S., Friedman, D.B., All about DIGE: quantification technology for differential-display 2D-gel proteomics. Expert Rev. Proteomics 1 (2004), 401–409.
22. Lin, T.K., Hughes, G., Muratovska, A., Blaikie, F.H., Brookes, P.S., Darley-Usmar, V., Smith, R.A., Murphy, M.P., Specific modification of mitochondrial protein thiols in response to oxidative stress: A proteomics approach. J. Biol. Chem. 277 (2002), 17048–17056.
23. Mani, A.R., Ebrahimkhani, M.R., Ippolito, S., Ollosson, R., Moore, K.P., Metalloprotein-dependent decomposition of S-nitrosothiols: Studies on the stabilization and measurement of S-nitrosothiols in tissues. Free Radic. Biol. Med. 40 (2006), 1654–1663.
24. Martinez-Ruiz, A., Lamas, S., Signalling by NO-induced protein S-nitrosylation and S-glutathionylation: Convergences and divergences. Cardiovasc. Res. 75 (2007), 220–228.
25. Moriarty-Craige, S.E., Jones, D.P., Extracellular thiols and thiol/disulfide redox in metabolism. Annu. Rev. Nutr. 24 (2004), 481–509.
26. Murphy, M.P., Targeting lipophilic cations to mitochondria. Biochim. Biophys. Acta 1777 (2008), 1028–1031.
27. Nakamura, H., Masutani, H., Yodoi, J., Extracellular thioredoxin and thioredoxin-binding protein 2 in control of cancer. Semin. Cancer Biol. 16 (2006), 444–451.
28. Olm, E., Fernandes, A.P., Hebert, C., Rundlof, A.K., Larsen, E.H., Danielsson, O., Bjornstedt, M., Extracellular thiol-assisted selenium uptake dependent on the x(c)-cystine transporter explains the cancer-specific cytotoxicity of selenite. Proc. Natl. Acad. Sci. USA 106 (2009), 11400–11405.
29. Ou, W., Silver, J., Role of protein disulfide isomerase and other thiol-reactive proteins in HIV-1 envelope protein-mediated fusion. Virology 350 (2006), 406–417.
30. Rhee, S.G., Bae, Y.S., Lee, S.R., Kwon, J., Hydrogen peroxide: A key messenger that modulates protein phosphorylation through cysteine oxidation. Sci. STKE, 2000, 2000, ⁎⁎p.pe.1.
31. Rossignol, R., Gilkerson, R., Aggeler, R., Yamagata, K., Remington, S.J., Capaldi, R.A., Energy substrate modulates mitochondrial structure and oxidative capacity in cancer cells. Cancer Res. 64 (2004), 985–993.
32. Sahaf, B., Heydari, K., Herzenberg, L.A., Lymphocyte surface thiol levels. Proc. Natl. Acad. Sci. USA 100 (2003), 4001–4005.
33. Sahaf, B., Heydari, K., Herzenberg, L.A., The extracellular microenvironment plays a key role in regulating the redox status of cell surface proteins in HIV-infected subjects. Arch. Biochem. Biophys. 434 (2005), 26–32.
34. Salazar, M., Rojo, A.I., Velasco, D., de Sagarra, R.M., Cuadrado, A., Glycogen synthase kinase-3beta inhibits the xenobiotic and antioxidant cell response by direct phosphorylation and nuclear exclusion of the transcription factor Nrf2. J. Biol. Chem. 281 (2006), 14841–14851.
35. Schwertassek, U., Balmer, Y., Gutscher, M., Weingarten, L., Preuss, M., Engelhard, J., Winkler, M., Dick, T.P., Selective redox regulation of cytokine receptor signaling by extracellular thioredoxin-1. EMBO J. 26 (2007), 3086–3097.
36. Sebastia, J., Cristofol, R., Martin, M., Rodriguez-Farre, E., Sanfeliu, C., Evaluation of fluorescent dyes for measuring intracellular glutathione content in primary cultures of human neurons and neuroblastoma SH-SY5Y. Cytometry A 51 (2003), 16–25.
37. Seyfried, J., Soldner, F., Schulz, J.B., Klockgether, T., Kovar, K.A., Wullner, U., Differential effects of L-buthionine sulfoximine and ethacrynic acid on glutathione levels and mitochondrial function in PC12 cells. Neurosci. Lett. 264 (1999), 1–4.
38. Shan, X., Jones, D.P., Hashmi, M., Anders, M.W., Selective depletion of mitochondrial glutathione concentrations by (R, S)-3-hydroxy-4-pentenoate potentiates oxidative cell death. Chem. Res. Toxicol. 6 (1993), 75–81.
39. Shepherd, D., Garland, P.B., The kinetic properties of citrate synthase from rat liver mitochondria. Biochem. J. 114 (1969), 597–610.
40. Smith, R.A., Adlam, V.J., Blaikie, F.H., Manas, A.R., Porteous, C.M., James, A.M., Ross, M.F., Logan, A., Cocheme, H.M., Trnka, J., Prime, T.A., Abakumova, I., et al. Mitochondria-targeted antioxidants in the treatment of disease. Ann. N. Y. Acad. Sci. 1147 (2008), 105–111.
41. Tassi, S., Carta, S., Vene, R., Delfino, L., Ciriolo, M.R., Rubartelli, A., Pathogen-induced interleukin-1beta processing and secretion is regulated by a biphasic redox response. J. Immunol. 183 (2009), 1456–1462.
42. Unlü, M., Morgan, M.E., Minden, J.S., Difference gel electrophoresis: a single gel method for detecting changes in protein extracts. Electrophoresis 18 (1997), 2071–2077.
43. Yu, Y.P., Yu, G., Tseng, G., Cieply, K., Nelson, J., Defrances, M., Zarnegar, R., Michalopoulos, G., Luo, J.H., Glutathione peroxidase 3, deleted or methylated in prostate cancer, suppresses prostate cancer growth and metastasis. Cancer Res. 67 (2007), 8043–8050.