Cysteinyl-glycine in the control of glutathione homeostasis in bovine lenses

Molecular Vision

Volumn 16, Issue , 2010, Pages 1025-1033

  de Donatis, Gian Marco ^a,b   Moschini, Roberta ^a   Cappiello, Mario ^a   del Corso, Antonella ^a   Mura, Umberto ^a  

^a UNIVERSITY OF PISA   (Italy)

^b NATIONAL CANCER INSTITUTE   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; CYSTEINYLGLYCINE; GAMMA GLUTAMYLCYSTEINE; GAMMA GLUTAMYLTRANSFERASE; GLUTAMATE CYSTEINE LIGASE; GLUTATHIONE; GLUTATHIONE SYNTHASE; SERINE BORATE; THIOL;

ANIMAL TISSUE; ARTICLE; CALF (BOVINE); CONTROLLED STUDY; ENZYME INHIBITION; ENZYME LOCALIZATION; EX VIVO STUDY; GLUTATHIONE METABOLISM; LENS; LENS EPITHELIUM; METABOLIC REGULATION; NONHUMAN; PRIORITY JOURNAL; PROTEIN DEGRADATION; PROTEIN TRANSPORT; SIGNAL TRANSDUCTION; TISSUE CULTURE; TISSUE LEVEL; ZONE ELECTROPHORESIS;

ANIMALS; BORATES; CATTLE; CYSTEINE; DIPEPTIDES; GAMMA-GLUTAMYLTRANSFERASE; GLUTATHIONE; HOMEOSTASIS; LENS, CRYSTALLINE; OSMOLAR CONCENTRATION; SERINE; TISSUE CULTURE TECHNIQUES; TISSUE DISTRIBUTION; UP-REGULATION;

EID: 77955633215     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

References (45)

1. Finkel T, Holbrook NJ. Oxidant, oxidative stress and the biology of ageing. Nature 2000; 408:239-47.
2. Beal MF. Aging, energy and oxidative stress in neurodegenerative disease. Ann Neurol 1995; 38:357-66.
3. Hammond CL, Lee TK, Ballatori N. Novel roles for glutathione in gene expression, cell death, and membrane transport of organic solutes. J Hepatol 2001; 34:946-54.
4. Meister A, Anderson ME. Glutathione. Annu Rev Biochem 1983; 52:711-60.
5. Del Corso A, Vilardo PG, Cappiello M, Cecconi I, Dal Monte M, Barsacchi D, Mura U. Physiological thiols as promoters of glutathione oxidation and modifying agents in protein Sthiolation. Arch Biochem Biophys 2002; 397:392-8.
6. Del Corso A, Cappiello M, Mura U. Thiol dependent oxidation of enzymes: the last chance against oxidative stress. Int J Biochem 1994; 26:745-50.
7. Mura U, Cappiello M, Vilardo PG, Cecconi I, Dal Monte M, Del Corso A. Signalling potential and protein modifying ability of physiological thiols. Biofactors 2003; 17:279-85.
8. Gallogly MM, Mieyal JJ. Mechanisms of reversible protein glutathionylation in redox signaling and oxidative stress. Curr Opin Pharmacol 2007; 7:381-91.
9. Mieyal JJ, Gallogly MM, Qanungo S, Sabens EA, Shelton MD. Molecular mechanisms and clinical implications of reversible protein S-glutathionylation. Antioxid Redox Signal 2008; 10:1941-88.
10. Shelton MD, Mieyal JJ. Regulation by reversible Sglutathionylation: molecular targets implicated in inflammatory diseases. Mol Cells 2008; 25:332-46.
11. Dalle-Donne I, Milzani A, Gagliano N, Colombo R, Giustarini D, Rossi R. Molecular mechanisms and potential clinical significance of S-glutathionylation. Antioxid Redox Signal 2008; 10:445-73.
12. Rahman I, Biswas SK, Jimenez LA, Torres M, Forman HJ. Glutathione, stress responses, and redox signaling in lung inflammation. Antioxid Redox Signal 2005; 7:42-59.
13. Franco R, Cidlowski JA. Apoptosis and glutathione: beyond an antioxidant. Cell Death Differ 2009; 16:1303-14.
14. Martin HL, Teismann P. Glutathione-a review on its role and significance in Parkinson's disease. FASEB J 2009; 23:3263-72.
15. Yuan L, Kaplowitz N. Glutathione in liver diseases and hepatotoxicity. Mol Aspects Med 2009; 30:29-41.
16. Spector A. Oxidative stress-induced cataract: mechanism of action. FASEB J 1995; 9:1173-82.
17. Meister A, Tate SS. Glutathione and related gamma-glutamyl compounds: biosynthesis and utilization. Annu Rev Biochem 1976; 45:559-604.
18. Wang W, Ballatori N. Endogenous glutathione conjugates: occurrence and biological functions. Pharmacol Rev 1998; 50:335-56.
19. Franco R, Schoneveld OJ, Pappa A, Panayiotidis MI. The central role of glutathione in the pathophysiology of human diseases. Arch Physiol Biochem 2007; 113:234-58.
20. Ballatori N, Krance SM, Notenboom S, Shi S, Tieu K, Hammond CL. Glutathione dysregulation and the etiology and progression of human diseases. Biol Chem 2009; 390:191-214.
21. Gukasyan HJ, Lee VH, Kim KJ, Kannan R. Net glutathione secretion across primary cultured rabbit conjunctival epithelial cell layers. Invest Ophthalmol Vis Sci 2002; 43:1154-61.
22. Gukasyan HJ, Kim KJ, Lee VH, Kannan R. Glutathione and its transporters in ocular surface defense. Ocul Surf 2007; 5:269-79.
23. Riley MV, Meyer RF, Yates EM. Glutathione in the aqueous humor of human and other species. Invest Ophthalmol Vis Sci 1980; 19:94-6.
24. Lieberman MW, Wiseman AL, Shi ZZ, Carter BZ, Barrios R, Ou CN, Chévez-Barrios P, Wang Y, Habib GM, Goodman JC, Huang SL, Lebovitz RM, Matzuk MM. Growth retardation and cysteine deficiency in gamma-glutamyl transpeptidase-deficient mouse. Proc Natl Acad Sci USA 1996; 93:7923-6.
25. Kumar TR, Wiseman AL, Kala G, Kala SV, Matzuk MM, Lieberman MW. Reproductive defects in gamma-glutamyl transpeptidase-deficient mouse. Endocrinology 2000; 141:4270-7.
26. Meister A, Tate SS, Griffith OW. Gamma-glutamyl transpeptidase. Methods Enzymol 1981; 77:237-53.
27. Frey IM, Rubio-Aliaga I, Siewert A, Sailer D, Drobyshev A, Beckers J, De Angelis MH, Aubert J, Bar Hen A, Fiehn O, Heichinger HM, Daniel H. Profiling at mRNA, protein, and metabolite levels reveals alterations in renal aminoacid handling and glutathione metabolism in kidney tissue of Pept2-/-mice. Physiol Genomics 2007; 28:301-10.
28. Kozak EM, Tate SS. Glutathione-degrading enzymes of microvillus membranes. J Biol Chem 1982; 257:6322-7.
29. Cappiello M, Lazzarotti A, Buono F, Scaloni A, D'Ambrosio C, Amodeo P, Méndez BL, Pelosi P, Del Corso A, Mura U. New role for leucyl aminopeptidase in glutathione turnover. Biochem J 2004; 378:35-44.
30. Enoiu M, Aberkane H, Salazar JF, Leroy P, Groffen J, Siest G, Wellman M. Evidence for the pro-oxidant effect of gammaglutamyltranspeptidase-related enzyme. Free Radic Biol Med 2000; 29:825-33.
31. Dominici S, Valentini M, Maellaro E, Del Bello B, Paolicchi A, Lorenzini E, Tongiani R, Comporti M, Pompella A. Redox modulation of cell surface protein thiols in U937 lymphoma cells: the role of gamma-glutamyl transpeptidase-dependent H2O2 production and S-thiolation. Free Radic Biol Med 1999; 27:623-35.
32. Del Bello B, Paolicchi A, Comporti M, Pompella A, Maellaro E. Hydrogen peroxide produced during gamma-glutamyl transpeptidase activity is involved in prevention of apoptosis and maintainance of proliferation in U937 cells. FASEB J 1999; 13:69-79.
33. Graber R, Losa GA. Apoptosis in human lymphoblastoid cells induced by acivicin, a specific gamma-glutamyltransferase inhibitor. Int J Cancer 1995; 62:443-8.
34. Cappiello M, Del Corso A, Camici M, Mura U. Thiol and disulfide determination by free zone capillary electrophoresis. J Biochem Biophys Methods 1993; 26:335-41.
35. Rathbun WB, Betlach MV. Estimation of enzymatically produced orthophosphate in the presence of cysteine and adenosine triphosphate. Anal Biochem 1969; 28:436-45.
36. Del Corso A, Cappiello M, Buono F, Moschini R, Paolicchi A, Mura U. Colorimetric coupled enzyme assay for gammaglutamyltransferase activity using glutathione as substrate. J Biochem Biophys Methods 2006; 67:123-30.
37. Gaitonde MK. A spectrophotometric method for the direct determination of cysteine in the presence of other naturally occurring amino acids. Biochem J 1967; 104:627-33.
38. Bradford MM. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal Biochem 1976; 72:248-54.
39. Tate SS, Meister A. Serine-borate complex as a transition-state inhibitor of gamma-glutamyl transpeptidase. Proc Natl Acad Sci USA 1978; 75:4806-9.
40. Washtien W, Abeles RH. Mechanism of inactivation of gammacystathionase by the acetylenic substrate analogue propargylglycine. Biochemistry 1977; 16:2485-91.
41. Griffith OW. Mechanism of action, metabolism and toxicity of buthionine sulfoximine and its higher homologs, potent inhibitors of glutathione synthesis. J Biol Chem 1982; 257:13704-12.
42. Rich DH, Moon BJ, Harbeson S. Inhibition of aminopeptidases by amastatin and bestatin derivatives. Effect of inhibitor structure on slow-binding processes. J Med Chem 1984; 27:417-22.
43. Burley SK, David PR, Lipscomb WN. Leucine aminopeptidase: Bestatin inhibition and a model for enzyme-catalyzed peptide hydrolysis. Proc Natl Acad Sci USA 1991; 88:6916-20.
44. Ueda Y, Duncan MK, David LL. Lens proteomics: the accumulation of crystallin modification in the mouse lens with age. Invest Ophthalmol Vis Sci 2002; 43:205-15.
45. Sharma KK, Santhoshkumar P. Lens aging: effects of crystallins. Biochim Biophys Acta 2009; 1790:1095-108.