Redox regulation in the lens

Progress in Retinal and Eye Research

Volumn 22, Issue 5, 2003, Pages 657-682

  Lou, Marjorie F ^a,b,c  

^a UNIVERSITY OF NEBRASKA LINCOLN   (United States)

^b UNIVERSITY OF NEBRASKA MEDICAL CENTER   (United States)

^c East Campus Loop ^*  (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CYSTEINE; DEHYDROASCORBIC ACID REDUCTASE; DISULFIDE; ENZYME; GAMMA GLUTAMYLCYSTEINE; GLUTATHIONE PEROXIDASE; GLUTATHIONE REDUCTASE; HYDROGEN PEROXIDE; LENS PROTEIN; OXIDIZING AGENT; PROTEIN DISULFIDE ISOMERASE; REACTIVE OXYGEN METABOLITE; RECOMBINANT ENZYME; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE PHOSPHATE; STRUCTURAL PROTEIN; THIOL DERIVATIVE; THIOREDOXIN;

AGING; BIOSYNTHESIS; CATALYSIS; CATARACT; CATARACTOGENESIS; CELL CULTURE; CELL REGENERATION; CLONING; CYTOSOL; ENZYME ACTIVE SITE; ENZYME ACTIVITY; EPITHELIUM CELL; EYE; GENE EXPRESSION; GLYCOLYSIS; HOMEOSTASIS; HUMAN; LENS; MICROORGANISM; MITOCHONDRION; MODEL; MOLECULAR WEIGHT; NONHUMAN; OXIDATION; OXIDATION REDUCTION POTENTIAL; OXIDATION REDUCTION REACTION; OXIDATIVE STRESS; PLANT TISSUE; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN ANALYSIS; PROTEIN CROSS LINKING; PROTEIN DETERMINATION; PROTEIN FUNCTION; PROTEIN LOCALIZATION; PURIFICATION; REGENERATION; REGULATORY MECHANISM; REVIEW; SENILE CATARACT; SOLUBILITY; UPREGULATION;

EID: 0042198801     PISSN: 13509462     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1350-9462(03)00050-8     Document Type: Review

References (123)

1. Anderson E.I., Spector A. The state of sulfhydryl groups in normal and cataractous human lens proteins. I. Nuclear region. Exp. Eye Res. 26:1978;407-417.
2. Andley U.P., Liang J.J.-N., Lou M.F. Biochemical Mechanisms of age-related cataract. Albert D.M., Jakobiec F.A. Principle, Practices in Ophthalmology. 2000;1428-1449 Sanuders, Philadelphia.
3. Arner E.s., Holmgren A. Physiological functions of thioredoxin and thioredoxin reductase. Eur. J. Biochem. 267:2000;6102-6109.
4. Askelof P., Axelsson K., Eriksson S., Mannervik B. Mechanism of action of enzymes catalyzing thiol-disulfide interchange. Thioltransferase rather than transhydrogenases. FEBS Lett. 38:1974;263-267.
5. Augusteyn R.C. Protein modification in cataract. possible oxidative mechanisms Duncan G. Mechanisms of Cataract Formation in the Human Lens. 1981;72-115 Academic Press, New York.
6. Awasthi S., Srivastava S.K., Piper J.T., Singhal s.s., Chauby M., Awasthi Y.C. Curcumin protects against 4-hydroxy-2-trans-nonenal-induced cataract formation in rat lenses. Am. J. Clin. Nutr. 64:1996;761-766.
7. Bando M., Obazawa H. Regional and subcellular distribution of ascorbate free radical reductase activity in the human lens. Tokai J. Exp. Clin. Med. 16:1991;217-222.
8. Bandyopatdhyay S., Starke D.W., Mieyal J.J., Gronostajski R.M. Thioltransferase (Glutaredoxin) reactivates the DNA-binding activity of oxidation-inactivated nuclear factor-1. J. Biol. Chem. 273:1998;392-397.
9. Barrett W.C., DeGnore J.P., Keng Y.-F., Zhang S.-Y., Yim M.B., Chock P.B. Roles of superoxide radical anion in signal transduction mediated by reversible regulation of protein-tyrosine phosphatase 1B. J. Biol. Chem. 274:1999;34543-34546.
10. Benedek G.B. Theory of transparency of the eye. Appl. Optics. 10:1971;459-473.
11. Benedek G.B., Pande J., Thurston G.M., Clark J.I. Theoretical and experimental basis for the inhibition of cataract. Prog. Retin. Eye Res. 18:1999;391-402.
12. 2 level in emory mouse cataract. Invest. Ophthalmol. Vis. Sci. 37(Suppl.):1996;S559.
13. Bhuyan K.C., Reddy B.P., Bhuyan D.K. Thioredoxin genes in lens. regulation by oxidative stress Meth. Enzymol. 374:2002;421-435.
14. Blundell T., Lindley P., Miller L., Moss D., Slingsby C., Tickle I., Turnell B., Wistow G. The molecular structure and stability of the eye lens. X-ray analysis of gamma-crystallin II Nature. 289:1981;771-777.
15. Brigelius R. Mixed disulfides. biological functions and increase in oxidative stress Sies H. Oxidative Stress. 1985;243-272 Academic Press, New York.
16. Casagrande S., Bonetto V., Fratelli M., Gianazza E., Eberini I., Massignan T., Salmona M., Chang G., Holmgren A., Ghezzi P. Glutathionylation of human thioredoxin. a possible crosstalk between the glutathione and thioredoxin systems Proc. Natl. Acad. Sci. 99:2002;9745-9749.
17. Chai Y.C., Ashraf S.S., Rokutan K., Johnston R.B., Thomas J.A. S-thiolation of individual human neutrophil proteins including actin by stimulation of the respiratory burst. evidence against a role for glutathione disulfide Arch. Biochem. Biophys. 310:1994;273-281.
18. Cotgreave, A., Gerdes, R.G., 1998. Recent trends in glutathione biochemistry-glutathione-protein interactions: a molecular link between oxidative stress and cell proliferation? Biochem. Biophys. Res. Comm. 242, 1-9.
19. Crestensen C.A., Starke D.W., Mieyal J.J. Acute cadmium exposure inactivates thioltransferase (glutaredoxin), inhibits intracellular reduction of protein-glutathionyl-mixed disulfides, and initiates apoptosis. J. Biol. Chem. 275:2000;26556-26565.
20. 2 exposure on rat lens morphology and biochemistry. Exp. Eye Res. 57:1993;157-167.
21. Daily D., Vlamis-Gardikas A., Offen D., Mittelman L., Melamed E., Holmgren A., Barzilai A. Glutaredoxin protects cerebellar granule neurons from dopamine-induced apoptosis by dual activation of the Ras-phosphoinositide-3-kinase and Jun N-terminal kinase pathways. J. Biol. Chem. 276:2001;21618-21626.
22. Dal Monte M., Cecconi I., Buono F., Vilardo D.G., Mura U. Thioltransferase activity of bovine lens glutathione-S-transferase. Biochem. J. 334:1998;57-62.
23. Delaye M., Tardieu A. Short-range order of crystallin proteins accounts for eye lens transparency. Nature (London). 302:1983;415-417.
24. Dickerson J.E., Lou M.F. A new mixed disulfide species in human cataractous and aged lenses. Biochim. Biophys. Acta. 1157:1993;141-146.
25. Dickerson J.E. Jr., Lou M.F. Free cysteine in normal human lenses. Exp. Eye Res. 65:1997;451-454.
26. Dische Z., Zil H. Studies on the oxidation of cysteine to cystine in the lens proteins during cataract formation. Am. J. Ophthalmol. 34:1951;104-113.
27. Engelberg D., Klein C., Martinetto H., Struhl K., Karin M. The UV response involving the Ras signaling pathway and AP-1 transcription factors is conserved between yeast and mammals. Cell. 77:1994;381-390.
28. Fahey R.C., Newton G.L. Determination of low-molecular-weight thiols using monobromobimane fluorescent labeling and high-performance liquid chromatography. Meth. Enzymol. 143:1987;85-96.
29. Fernando, M.R., Lou, M.F., 2002. Thioltransferase can catalyze dehydroascorbate reduction in human lens epithelial cells [abstract]. Annual Meeting Abstract and Program Planner accessed at www.arvo.org. Association for Research in Vision and Ophthalmology. Abstract 2364.
30. Fernando M.R., Nanri H., Yoshitake S., Nagata-Kuno K., Minakami S. Thioredoxin regenerates proteins inactivated by oxidative stress in endothelial cells. Eur. J. Biochem. 209:1992;917-922.
31. Fernando, M.R., Gladyshev, V.N., Lou, M.F., 2003. The presence of mitochondrial thioltransferase (Grx2) and its protective and regenerative roles of ascorbic acid in human lens epithelial cells [abstract]. Annual Meeting Abstract and Program Planner accessed at www.arvo.org. Association for Research in Vision and Ophthalmology. Abstract 325.
32. Finkel T., Holbrook N.J. Oxidants, oxidative stress and the biology of ageing. Nature. 408:2000;239-247.
33. Gan Z.R., Wells W. The primary structure of pig liver thioltransferase. J. Biol. Chem. 262:1987;6699-6703.
34. Garland D. Role of site-specific, metal-catalyzed oxidation in lens aging and cataract. a hypothesis Exp. Eye Res. 50:1990;677-682.
35. Giblin F.J. Glutathione. a vital lens antioxidant Ocular Pharmacology and Therapeutics. 16:2000;121-135.
36. Giblin F.J., Padgaonkar V.A., Leverenz V.R., Lin L.R., Lou M.F., Unakar N.J., Dang L., Dickerson J.E. Jr., Reddy V.N. Nuclear light scattering, disulfide formation and membrane damage in lenses of older guinea pigs treated with hyperbaric oxygen. Exp. Eye Res. 60:1995;219-235.
37. Giblin F.J., Leverenz V.R., Padgaonkar V.A., Unakar N.J., Dang L., Lin L.-R., Lou M.F., Reddy V.N., Borchman D., Dillon J.P. UVA light in vivo reaches the nucleus of the guinea pig lens and produces deleterious, oxidative effects. Exp. Eye Res. 75:2002;445-458.
38. Gladyshav V., Sun C.A., Liu A.-M., Lou M.F. Identification and characterization of a new mammalian mitochondrial glutaredoxin (thioltransferase). J. Biol. Chem. 276:2001;30374-30380.
39. Gravina S.A., Mieyal J.J. Thioltransferase is a specific glutathionyl mixed disulfide oxidoreductase. Biochemistry. 32:1993;3368-3676.
40. Hanson S.R.A., Chen A.A., Smith J.B., Lou M.F. Modification of γB-crystallins from a hydrogen peroxide treated bovine lens. J. Biol. Chem. 274:1997;4735-4742.
41. Hanson S.R.A., Hasan A., Smith D.L., Smith J.B. The major in vivo modifications of the human water-insoluble lens crystallins are disulfide bonds, deamidation, methionine oxidation, and backbone cleavage. Exp. Eye Res. 71:2000;195-207.
42. Harding J.J. Free and protein-bound glutathione in normal and cataractous human lenses. Biochem. J. 117:1970;957-960.
43. Harding, J.J., Crabbe, M.J., 1984. The lens: development, proteins, metabolism and cataract. In: Davson, H. (Ed.), The Eye, Vol. 1B. Academic Press, Orlando, pp. 207-492.
44. Hirota K., Matsui M., Iwata S., Nishiyama A., Mori K., Yodoi J. Ap-1 transcriptional activity is regulated by a direct association between thioredoxin and Ref-1. Proc Natl. Acad. Sci. USA. 94(8):1997;3633-3638.
45. Holmgren A. Hydrogen donor system for Escherichia coli ribonucleoside-diphosphate reductase dependent upon glutathione. Proc. Natl. Acad. Sci. USA. 73:1976;2275-2279.
46. Holmgren A. Thioredoxin. Annu. Rev. Biochem. 54:1985;237-271.
47. Holmgren A. Thioredoxin and glutaredoxin systems. J. Biol. Chem. 264:1989;13963-13966.
48. Inoue M. Dynamic aspect of protein mixed diusulfide formation. Dolphin D., Poulson R., Avramovic O. Glutathione: Chemical, Biochemical and Medical Aspects. 1989;613-644 Wiley, New York.
49. Jahngen-Hodge J., Cry D., Laxman E., Taylor A. Ubiquitin and ubiquitin conjugates in human lens. Exp. Eye Res. 55:1992;897-902.
50. Jayaraman L., Murthy K.G., Zhu C., Curran T., Xanthoudakis S., Prives C. Identification of redox/repair protein Ref-1 as a potent activator of p53. Genes Dev. 11(5):1997;558-570.
51. Jedziniak J.A., Kinoshita J.H., Yates E.M., Benedek G.B. The concentration and localization of heavy molecular weight aggregates in aging normal and cataractous human lenses. Exp. Eye Res. 20:1975;367-369.
52. Karin M., Liu Z.G., Zandi E. AP-1 function and regulation. Curr. Opin. Cell Biol. 9(2):1997;240-246.
53. Kono M., Chakrabarti B. Changes in the conformation stability of gamma-crystallins upon glutathione reaction. Biochemistry. 29:1990;464-470.
54. Krysan K., Lou M.F. Human thioltransferase (TTase) gene is controlled by AP-1 and mediated through redox signaling. Invest. Opthalmol. Vis. Sci. 43:2002;1876-1883.
55. Kuck J.F. Late onset hereditary cataract of the emory mouse. A model for human senile cataract. Exp. Eye Res. 50:1990;659-664.
56. Latta K., Augusteyn R.C. The purification and properties of human lens glutathione reductase. Exp. Eye Res. 39:1984;343-354.
57. Lau K.-H.W., Thomas J.A. Specific mixed disulfide formation with purified bovine cardiac glycogen synthase I and glutathione. J. Biol. Chem. 258:1983;2321-2326.
58. 2 and N-acetyl-L-cysteine regulate expression of c-jun and c-fos in lens systems. Exp. Eye Res. 59:1994;179-190.
59. Liang J.N., Pelletier M.R. Destabilization of lens protein conformation by glutathione mixed disulfide. Exp. Eye Res. 47:1988;17-25.
60. Lii C.-K., Chai Y.-C., Zhao W., Thomas J.A., Hendrich S. S-thiolation and irreversible oxidation of sufhydryls on carbonic anhydrase III during oxidative stress. a method for studying protein modification inintact cells and tissues Arch. Biochem. Biophys. 308:1994;231-239.
61. Lou, M.F., 1985. Quantitation of protein mixed disulfides in the lens. US-CCRG abstract 1985; Honolulu, HI.
62. Lou M.F. Protein-thiol mixed disulfides and thioltransferase in the lens - a review. Green K., Edelhauser H.F., Hackett R.B., Hull D.S., Potter D.E., Tripathi R.C. Advances in Ocular Toxicology. 1997;27-46 Plenum, New York.
63. Lou M.F. Thiol regulation in the lens. J. Ocular Pharmacol. Therapeutics. 16:2000;137-148.
64. Lou, M.F., unpublished results.
65. Lou M.F., Dickerson E.J. Jr. Human lens protein-thiol mixed disulfides. Exp. Eye Res. 55:1992;889-896.
66. Lou, M.F., Zigler, J.S., Jr., 1986. The effect of photooxidation of protein mixed disulfide in Lens. Proc. ICER IV, 87.
67. Lou M.F., Mckellar R., Chyan O. Quantitation of lens protein mixed disulfides by ion-exchange chromatography. Exp. Eye Res. 42:1986;607-616.
68. Lou M.F., Huang Q.L., Zigler S.J. Jr. Effect of opacification on human lens protein thio/disulfide and solubility. Curr. Eye Res. 8:1989;883-890.
69. Lou M.F., Dickerson J.E. Jr., Garadi R. The role of protein thiol mixed disulfides in cataratogenesis. Exp. Eye Res. 50:1990;819-826.
70. Lou M.F., Wang G.-M., Wu F., Raghavachari N., Reddan J.R. Thioltransferase is present in the lens epithelial cells as a highly oxidative stress-resistant enzyme. Exp. Eye Res. 66:1998;477-485.
71. Lou M.F., Dickerson J.E. Jr., Wolfe J.K., Tung W., Chylack L. Jr. Correlation of protein-thiol mixed disulfide level with the opacity and brunescence in human lens. Exp. Eye Res. 68:1999;547-552.
72. Lund A.L., Smith J.B., Smith D.L. Modifications of the water-insoluble human lens alpha-crystallins. Exp. Eye Res. 63:1996;661-672.
73. Lundberg M., Johansson C., Chandra J., Enoksson M., Jacobsson G., Ljung J., Johansson M., Holmgren A. Cloning and expression of a novel human glutaredoxin (Grx2) with mitochondrial and nuclear isoforms. J. Biol. Chem. 276:2001;26269-26275.
74. Mallis R.J., Poland B.W., Chatterjee T.K., Fisher R.A., Darmawan S., Honzatko R.B., Thomas J.A. Crystal structure of S-glutathiolated carbonic anhydrase III. FEBS Lett. 482:2000;237-241.
75. Mannervik B., Alin P., Guthenberg C., Jensson H., Tahir M.K., Warholm M., Jornvall H. Identification of three classes of cytosolic glutathione transferase common to several mammalian species. Proc. Natl. Acad. Sci. USA. 82:1985;7202-7206.
76. Martensson J., Steinherz R., Jain A., Meister A. Glutathione ester prevents buthionine sulfoximine-induced cataracts and lens epithelial cell damage. Proc. Natl. Acad. Sci. USA. 86:1989;8727-8771.
77. Martensson J., Han J., Griffith O.w., Meister A. Glutathione ester delays the onset of scurvy in ascorbate-deficient guinea pigs. Proc. Natl. Acad. Sci. USA. 90:1993;317-321.
78. Mieyal J.J., Srinivasan U., Starke D.W., Gravina S.A., Mieyal P.A. Glutathionyl specificity of thioltransferases. mechanistic and physiological implications Packer L., Cadenas E. Biothiols in Health and Disease. 1995;305-372 Marcel Dekker Inc, New York.
79. Nagaraj R.H., Sell D.R., Prabhakaram M., Ortwerth B.J., Monnier V.M. High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. Proc. Natl. Acad. Sci. USA. 88:1991;10257-10261.
80. Ortwerth B.J., Olesen P.R. Ascorbic acid-induced crosslinking of lens proteins. evidence supporting a maillard reaction Biochim. Biophys. Acta. 956:1988;10-22.
81. Padilla C.A., Spyrou G., Holmgren A. High-level expression of fully active human glutaredoxin (thioltransferase) in E. Coli and characterization of Cys 7 to Ser mutant protein. FEBS Letters. 378:1996;69-73.
82. Pande J., Berland C., Broide M., Ogun O., Melhuish J., Benedek G. Suppression of phase separation in solutions of bovine gamma IV-crystallin by polar modification of the sulfur-containing amino acids. Proc. Natl. Acad. Sci. USA. 88:1991;4916-4920.
83. Park J.B., Levine M. The human glutaredoxin gene. determination of its organization, transcription start point, and promoter analysis Gene. 197(1-2):1997;189-193.
84. Powis G., Montfort W.R. Properties and biological activities of thioredoxins. Ann. Rev. Pharmacol. Toxicol. 41:2001;261-295.
85. Qiao F.-Y., Xing K.-Y., Lou M.F. Modulation of glucose metabolism by thioltransferase in the lens. Exp. Eye Res. 70:2000;745-754.
86. Qiao F.-Y., Xing K.-Y., Liu A., Raghavarchari N., Ehlers N., Lou M.F. Recombinant human lens thioltransferase. purification, characterization and function Invest. Opthalmol. Vis. Sci. 42:2001;743-751.
87. Raghavachari N., Lou M.F. Evidences for the presence of thioltransferase in the lens. Exp. Eye Res. 63:1996;433-441.
88. Raghavachari N., Qiao F.-Y., Lou M.F. Does glutathione S-transferases dethiolate lens protein-thiol mixed disulfide? - a comparative study with thioltransferase. Exp. Eye Res. 68:1999;715-724.
89. Raghavachari N., Kryzan K., Xing K.-Y., Lou M.F. Regulation of thioltransferase expression in human lens epithelial cells. Invest. Ophthalmol. Vis. Sci. 42:2001;1002-1008.
90. Rao V., John F., Gonzalez P., Leto T., Zigler J.S. Jr. The biochemical and molecular evidence for an active Rac ATPase/NADPH oxidase system in the ocular lens. Invest. Ophthalmol. Vis. Sci. 40:1999;S169.
91. Rathbun W.B. Lenticular glutathione synthesis. rate-limiting factors in its regulation and decline Curr. Eye Res. 3:1984;101-108.
92. Rathbun, W.B., 1989. Glutathione in ocular tissues. In: Dolphin, D., Poulson, R., Avramovic, O. (Eds.), Glutathione: Coenzymes and Cofactors, Vol. 3. Wiley, New York, p. 467.
93. Reddy V.N. Glutathione and its function in the lens - an overview. Exp. Eye Res. 50:1990;771-778.
94. Reddy V.N., Han R.F. Protein-bound glutathione in mammalian lenses and in galactose cataract. Doc. Ophthalmol. Proc. Ser. 8:1976;153.
95. Reddy V.N., Kinsey V.E. Studies on the crystalline lens IX quantitative analysis of free amino acids and related compounds. Invest. Ophthalmol. 1:1962;635-641.
96. Reddy P.G., Bhuyan D.K., Bhuyan K.C. Lens-specific regulation of the thioredoxin-1 gene, but not thioredoxin-2 upon in vivo photochemical oxidative stress in the Emory mouse. Biochem. Biophys. Res. Comm. 265:1999;345-349.
97. Sasaki H., Giblin F.J., Winkler B.s., Chakrapani B., Leverenz V., Chen S.C. A protective role for glutathione-dependent reduction of dehydroascorbic acid in lens epithelium. Invest. Ophthalmol. Vis. Sci. 36:1995;1804-1817.
98. Spector A. The search for a solution to senile cataracts. proctor lecture Invest. Ophthalmol. Vis. Sci. 25:1984;130-146.
99. Spector A. Oxidative stress-induced cataract. mechanism of action FASEB J. 9:1995;1173-1182.
100. Spector A., Roy D. Disulfide-linked high molecular weight protein associated with human cataract. Proc. Natl. Acad. Sci. USA. 75:1978;3244-3248.
101. 2 upon thioredoxin-enriched lens epithelial cells. J. Biol. Chem. 263:1988;4984-4990.
102. Srivastava S.K., Beutler E. Cleavage of lens proteins-GSH mixed disulphide by glutathione reductase. Exp. Eye Res. 17:1973;33-42.
103. Takemoto L. Increase in the intramolecular disulfide bonding of alpha-crystallin during aging of the human lens. Exp. Eye Res. 63:1996;585-590.
104. Terada T., Oshida T., Nishimura M., Maeda H., Hara T., Hosomi S., Mizoguchi T., Nishihara T. Study on human erythrocyte thioltransferase. comparative characterization with bovine enzyme and its physiological role under oxidative stress J. Biochem. 111:1992;688-692.
105. Tomarev S.I., Zinovieva R.D. Squid major lens polypeptides are homologous to glutathione S-transferase subunit. Nature. 336:1988;86-88.
106. Toone W.M., Kuge S., Samuels M., Morgan B.A., Toda T., Jones N. Regulation of the fission yeast transcription factor Pap 1 by oxidative stress. requirement for the nuclear export factor Crm 1 (Exportin) and the stress-activated MAP kinase Sty1/Spc1 Gene Dev. 12:1998;1453-1463.
107. Truscott R.J.W., Augusteyn R.C. The state of sulphydryl groups in normal and cataractous human lenses. Exp. Eye Res. 25:1977;139-148.
108. Veltman J., Lou M.F. Quantitation of free cysteine in the lens. Invest. Ophthalmol. Vis. Sci. 34(Suppl.):1993;758.
109. Wagner B.J., Margolis J.W., Garland D., Roseman J.E. Bovine lens neutral proteinase preferentially hydrolyses oxidatively modified glutamine synthetase. Exp. Eye Res. 43:1986;1141-1143.
110. 3-up-regulated protein-1 is a stress-responsive gene that regulates cardiomyocyte viability through interaction with thioredoxin. J. Biol. Chem. 277:2002;26496-26500.
111. Wells W.W., Xu D.P. Dehydroascorbate reduction. J. Bioenerg. Biomemb. 26:1994;369-377.
112. Wells W.W., Xu D.P., Yang Y., Rocque P.A. Mammalian thioltransferase (glutaredoxin) and protein disulfide isomerase have dehydroascorbate reductase activity. J. Biol. Chem. 265:1990;15361-15364.
113. Willis A., Schleich T. 13C NMR spectroscopic measurement of glutathione synthesis and antioxidant metabolism in the intact ocular lens. Biochem. Biophys. Res. Commun. 186:1992;931-935.
114. Winkler B.S., Orselli S.M., Rex T.S. The redox couple between glutathione and ascorbic acid. a chemical and physiological perspective Free Rad. Biol. Med. 17:1994;333-349.
115. Wu F., Raghavachari N., Wang G.-M., Lou M.F. Distribution of thioltransferase in ocular tissues. Invest. Ophthalmol. Vis. Sci. 39:1998;476-480.
116. Xing K.-Y., Lou M.F. Oxidative stress of human lens epithelial cells (B3). Exp. Eye Res. 74:2002;113-122.
117. Xing, K.-Y., Lou, M.F., 2003. The possible physiological function of thioltransferase in the cells [abstract]. Annual Meeting Abstract and Program Planner accessed at www.arvo.org. Association for Research in Vision and Ophthalmology. Abstract 323.
118. Xu G.T., Zigler J.S. Jr., Lou M.F. The possible mechanism of naphthalene cataract in rat and its prevention by an aldose reductase inhibitor (AL01576). Exp. Eye Res. 54:1992;63-72.
119. Yegorova, S., Liu, A., M.F. Lou., 2002. Human lens thioredoxin: cloning, overexpression, characterization and H2O2-upregulation [abstract]. Annual Meeting Abstract and Program Planner accessed at www.arvo.org. Association for Research in Vision and Ophthalmology. Abstract 2365.
120. Yoshitake S., Nanri H., Fernando M.R., Minikami S. Possible differences in the regenerative roles played by thioltransferase and thioredoxin for oxidatively damaged proteins. J. Biochem. 116:1994;42-46.
121. Yu L.H., Bhuyan D.K., Lou M.F., Dickerson J.E. Jr., Bhuyan K.C. Redox-active thiols of rabbit lens as altered by diquat in vivo. Invest. Ophthal. Vis. Sci. 32(Suppl.):1991;749.
122. Zhang, W., Lou, M., 2003. The presence of an endogenous superoxide anion-generating system in the cells [abstract]. Annual Meeting Abstract and Program Planner accessed at www.arvo.org. Association for Research in Vision and Ophthalmology. Abstract 316.
123. Zigman S., Paxhia T., McDaniel T., Lou M.F., Yu N.T. Effect of chronic near-ultraviolet radiation on the gray squirrel lens in vivo. Invest. Ophthalmol. Vis. Sci. 32:1991;1723-1732.