The effects of modulation of γ-glutamyl transpeptidase activity in HepG2 cells on thiol homeostasis and caspase-3-activity

Biochimica et Biophysica Acta - Molecular Cell Research

Volumn 1773, Issue 2, 2007, Pages 201-208

  Iciek, Małgorzata ^a   Chwatko, Grazyna ^b   Rokita, Hanna ^c   Bald, Edward ^b   Włodek, Lidia ^a  

^a JAGIELLONIAN UNIVERSITY MEDICAL COLLEGE   (Poland)

^b UNIVERSITY OF LODZ   (Poland)

^c JAGIELLONIAN UNIVERSITY   (Poland)

Author keywords

glutamyl transpeptidase; Caspase 3; Cysteine; Cysteinylglycine; Glutathione; Protein S thiolation

Indexed keywords

CASPASE 3; CYSTEINE; CYSTEINYLGLYCINE; GAMMA GLUTAMYLTRANSFERASE; GLUTATHIONE; HYDROGEN PEROXIDE; REACTIVE OXYGEN METABOLITE; THIOL DERIVATIVE;

ARTICLE; CELL STRAIN HEPG2; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME INHIBITION; ENZYME KINETICS; ENZYME MODIFICATION; ENZYME REGULATION; HOMEOSTASIS; HUMAN; HUMAN CELL; INCUBATION TIME; OXIDATION REDUCTION REACTION; PRIORITY JOURNAL;

CASPASE 3; CATALYSIS; CELL DEATH; CELL LINE, TUMOR; CYSTEINE; DIPEPTIDES; DISULFIDES; ENZYME ACTIVATION; ENZYME INHIBITORS; GAMMA-GLUTAMYLTRANSFERASE; GLUTATHIONE; HOMEOSTASIS; HUMANS; HYDROGEN PEROXIDE; OXIDATION-REDUCTION; SULFHYDRYL COMPOUNDS;

EID: 33846302061     PISSN: 01674889     EISSN: None     Source Type: Journal    
DOI: 10.1016/j.bbamcr.2006.10.013     Document Type: Article

References (25)

1. Biswas S., Chida A.S., and Rahman I. Redox modifications of protein-thiols: emerging roles in cell signaling. Biochem. Pharmacol. 71 (2006) 551-564
2. Dröge W. Free radicals in the physiological control of cell function. Physiol. Rev. 82 (2002) 47-92
3. Pompella A., Visvikis A., Paolicchi A., De Tata V., and Casini A.F. The changing faces of glutathione, a cellular protagonist. Biochem. Pharmacol. 66 (2003) 1499-1503
4. Klatt P., and Lamas S. Regulation of protein function by S-glutathiolation in response to oxidative and nitrosative stress. Eur. J. Biochem. 267 (2000) 4928-4944
5. Eaton P., and Shatlock M.J. Protein S-thiolation: emphasis on cell signaling and gene expression. Antioxid. Redox Signal. 7 (2005) 839-840
6. Ghezzi P. Oxidoreduction of protein thiols in redox regulation. Biochem. Soc. Trans. 33 (2005) 1378-1381
7. Ghezzi P. Regulation of protein function by glutathionylation. Free Radical Res. 39 (2005) 573-580
8. Thomas J.A., Poland B., and Honzatko R. Protein sulfhydryls and their role in the antioxidant function of protein s-thiolation. Arch. Biochem. Biophys. 319 (1995) 1-9
9. 2 production and S-thiolation. Free Radic. Biol. Med. 27 (1999) 623-635
10. Dominici S., Paolicchi A., Lorenzini E., Maellaro E., Comporti M., Pieri L., Minotti G., and Pompella A. γ-Glutamyltransferase-dependent prooxidant reaction: a factor in multiple processes. Biofactors 17 (2003) 187-199
11. Dominici S., Paolicchi A., Corti A., Maellaro E., and Pompella A. Prooxidant reactions promoted by soluble and cell-bound γ-glutamyltransferase activity. Methods Enzymol 401 (2005) 484-501
12. 2 production. Biochim. Biophys. Acta 1621 (2003) 76-83
13. Meister A. Selective modification of glutathione metabolism. Science 220 (1983) 472-477
14. Bald E., and Głowacki R. 2-chloro-1 methylquinolinium tetrafluoroborate as an effective and thiol specific UV-tagging reagent for liquid chromatography. J. Liq. Chromatogr. Relat. Technol. 24 (2001) 1323-1339
15. Bald E., Chwatko G., Głowacki R., and Kusmierek K. Analysis of plasma thiols by high-performance liquid chromatography with ultraviolet detection. J. Chromatogr., A 1032 (2004) 109-115
16. Fratelli M., Gianazza E., and Ghezzi P. Redox proteomics: identification and functional role of glutathionylated proteins. Expert Rev. Proteomics 1 (2004) 365-376
17. Mohr S., Zech B., Lapetina E.G., and Brune B. Inhibition of caspase 3 by S-nitrosation and oxidation caused by nitric oxide. Biochem. Biophys. Res. Commun. 238 (1997) 387-391
18. Corti A., Paolicchi A., Franzini M., Dominici S., Casini A.F., and Pompella A. The S-thiolation activity of membrane-γ-glutamyltransferase: formation of cysteinyl-glycine mixed disulfides with cellular proteins in the cell microenvironment. Antioxid. Redox Signal. 7 (2005) 911-918
19. Hultberg M., and Hultberg B. Glutathione turnover in human cell lines in the presence of agents with glutathione influencing potential with and without acivicin inhibition of gamma-glutamyltranspeptidase. Biochim. Biophys. Acta. 1726 (2005) 42-47
20. Hanigan M.H., and Ricketts W.A. Extracellular glutathione is a source of cysteine for cells that express gamma-glutamyltranspeptidase. Biochemistry 32 (1993) 6302-6306
21. Hanigan M.H., Frierson H.F., Swanson P.E., and de Young B.R. Altered expression of gamma-glutamyltranspeptidase in human tumors. Hum. Pathol. 30 (1999) 300-305
22. Hanigan M.H. Gamma-glutamyl transpeptidase, a glutathionase: the expression and function in carcinogenesis. Chem.-Biol Interact. 111-112 (1998) 333-342
23. Del Bello B., Paolicchi A., Comporti M., Pompella A., and Maellaro E. Hydrogen peroxide produced during gamma-glutamyl transpeptidase activity is involved in prevention of apoptosis and maintenance of proliferation in U937 cells. FASEB J. 13 (1999) 69-79
24. Polytarchou C., Hatziapostolou M., and Papadimitriou E. Hydrogen peroxide stimulates proliferation and migration of human prostate cancer cells through activation of activator protein-1 and up-regulation of the heparin affin regulatory peptide gene. J. Biol. Chem. 280 (2005) 40428-40435
25. Cooper C.E., Patel R.P., Brookes P.S., and Darley-Usmar V.M. Nanotransducers in cellular redox signaling: modification of thiols by reactive oxygen and nitrogen species. Trends Biochem. Sci. 27 (2002) 489-492