Revival of Glutathione Reductase in Human Cataractous and Clear Lens Extracts by Thioredoxin and Thioredoxin Reductase, in Conjunction with α -Crystallin or Thioltransferase

REFERENCES

• Harding J J. Affinity chromatography in the purification of glutathione reductase. J Chromatogr. 1973; 77: 191–199
   PubMed Web of Science ®Google Scholar
• Harding J J. Cataract: Biochemistry, Epidemiology and Pharmacology. Chapman and Hall, London 1991
   Google Scholar
• Rogers K M, Augusteyn R C. Glutathione reductase in normal and cataractous human lenses. Exp Eye Res. 1978; 27: 719–721
   PubMed Web of Science ®Google Scholar
• Srivastava S K, Villacorte D, Arya D V. Letter: Distribution of glutathione reductase in lens epithelium, cortex and nucleus in various species and in human cataractous lenses. Exp Eye Res. 1973; 16: 519–521
   PubMed Web of Science ®Google Scholar
• Rao G N, Sadasivudu B, Cotlier E. Studies on glutathione S-transferase, glutathione peroxidase and glutathione reductase in human normal and cataractous lenses. Ophthalmic Res. 1983; 15: 173–179
   PubMed Web of Science ®Google Scholar
• Zhang W Z, Augusteyn R C. Ageing of glutathione reductase in the lens. Exp Eye Res. 1994; 59: 91–95
   PubMed Web of Science ®Google Scholar
• Andley U P, Liang JJ-N, Lou M F. Biochemical mechanisms of age-related cataract. Principle and Practices in Ophthalmology, D M Albert, F A Jakobiec. Saunders, Philadelphia 2000; 1428–1449
   Google Scholar
• Lou M F, Dickerson J E, Jr. Protein-thiol mixed disulfides in human lens. Exp Eye Res 1992; 55: 889–896
   PubMed Web of Science ®Google Scholar
• Harding J J. Can drugs or micronutrients prevent cataract?. Drugs Aging 2001; 18: 473–486
   PubMed Web of Science ®Google Scholar
• Lou M F. Redox regulation in the lens. Prog Retin Eye Res. 2003; 22: 657–682
   PubMed Web of Science ®Google Scholar
• Holmgren A. Thioredoxin and glutaredoxin system. J Biol Chem. 1989; 264: 13963–13966
   PubMed Web of Science ®Google Scholar
• Qiao F, Xing K, Lou M F. Modulation of lens glycolytic pathway by thioltransferase. Exp Eye Res. 2000; 70: 745–753
   PubMed Web of Science ®Google Scholar
• Yegorova S, Liu A, Lou M F. Human lens thioredoxin: molecular cloning and functional characterization. Invest Ophthalmol Vis Sci. 2003; 44: 3263–3271
   PubMed Web of Science ®Google Scholar
• Xing K Y, Lou M F. Effect of H2O2 on human lens epithelial cells and the possible mechanism for oxidative damage repair by thioltransferase. Exp Eye Res 2002; 74: 113–122
   PubMed Web of Science ®Google Scholar
• Horwitz J. Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci USA. 1992; 89: 10449–10453
   PubMed Web of Science ®Google Scholar
• Derham B K, Harding J J. Alpha-crystallin as a molecular chaperone. Prog Retin Eye Res. 1999; 18: 463–509
   PubMed Web of Science ®Google Scholar
• Horwitz J. Alpha-crystallin. Exp Eye Res. 2003; 76: 145–154
   PubMed Web of Science ®Google Scholar
• Ganea E, Harding J J. alpha-crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase. Biochem J. 2000; 345: 467–472
   PubMed Web of Science ®Google Scholar
• Kumar M S, Reddy P Y, Sreedhar B, Reddy G B. AlphaB-crystallin assisted reactivation of glucose-6-phosphate dehydrogenase upon refolding. Biochem J. 2005; 391: 335–341
   PubMed Web of Science ®Google Scholar
• Yan H, Harding J J. The molecular chaperone, alpha-crystallin, protects against loss of antigenicity and activity of esterase caused by sugars, sugar phosphate and a steroid. Biol Chem. 2003; 384: 1185–1194
   PubMed Web of Science ®Google Scholar
• Blakytny R, Harding J J. Bovine and human alpha-crystallins as molecular chaperones: prevention of the inactivation of glutathione reductase by fructation. Exp Eye Res. 1997; 64: 1051–1058
   PubMed Web of Science ®Google Scholar
• Rachdan D, Lou M F, Harding J J. Revival of inactive glyceraldehyde 3-phosphate dehydrogenase in human cataract lenses by reduction. Exp Eye Res. 2004; 79: 105–109
   PubMed Web of Science ®Google Scholar
• Rachdan D, Lou M F, Harding J J. Glutathione reductase from human cataract lenses can be revived by reducing agents and by a molecular chaperone, α -crystallin. Curr Eye Res. 2005; 30: 919–925
   PubMed Web of Science ®Google Scholar
• Yan H, Lou M F, Fernando M R, Harding J J. Thioredoxin, thioredoxin reductase, and α -crystallin revive inactivated glyceraldehyde 3-phosphate dehydrogenase in human aged and cataract lens extracts. Mol Vis. 2006; 12: 1153–1159
   PubMed Web of Science ®Google Scholar
• Pirie A. Color and solubility of the proteins of human cataracts. Invest Ophthalmol. 1968; 7: 634–650
   PubMedGoogle Scholar
• Qiao F, Xing K, Liu A, Ehlers N, Raghavachari N, Lou M F. Human lens thioltransferase: cloning, purification, and function. Invest Ophthalmol Vis Sci. 2001; 42: 743–751
   PubMed Web of Science ®Google Scholar
• Slingsby C, Bateman O A. Rapid separation of bovine beta-crystallin subunits beta B1, beta B2, beta B3, beta A3 and beta A4. Exp Eye Res. 1990; 51: 21–26
   PubMed Web of Science ®Google Scholar
• Bergmeyer H U. Methods of Enzymatic Analysis. Academic Press, New York 1963; 1064
   Google Scholar
• Harding J J. Free and protein-bound glutathione in normal and cataractous human lenses. Biochem J. 1970; 117: 957–960
   PubMed Web of Science ®Google Scholar
• 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 1999; 68: 547–552
   PubMed Web of Science ®Google Scholar
• Bhuyan K C, Reddy P G, Bhuyan D K. Thioredoxin genes in lens: regulation by oxidative stress. Methods Enzymol 2002; 347: 421–435
   PubMed Web of Science ®Google Scholar
• Padgaonkar V A, Leverenz V R, Dang L, Chen S C, Pelliccia S, Giblin F J. Thioredoxin reductase may be essential for the normal growth of hyperbaric oxygen-treated human lens epithelial cells. Exp Eye Res. 2004; 79: 847–857
   PubMed Web of Science ®Google Scholar
• Spector A, Kleiman N J, Huang R R, Wang R R. Repair of H2O2-induced DNA damage in bovine lens epithelial cell cultures. Exp Eye Res. 1989; 49: 685–698
   PubMed Web of Science ®Google Scholar
• Christensen 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. 2000; 275: 26556–26565
   PubMed Web of Science ®Google Scholar
• Xing K Y, Lou M F. The possible physiological function of thioltransferase in cells. FASEB J. 2003; 17: 2088–2090
   PubMed Web of Science ®Google Scholar
• Horwitz J, Dovrat A, Straatsma B R, Revilla P J, Lightfoot D O. Glutathione reductase in human lens epithelium: FAD-induced in vitro activation. Curr Eye Res. 1987; 6: 1249–1256
   PubMed Web of Science ®Google Scholar
• Lou M F, Xing K Y. Effect of age on TTase and TRx/TR systems in the human lens. Invest Ophthalmol Vis Sci., Abstract. 2006 ARVO CD ROM Post boarder number 3520
   Google Scholar
• Lahm D, Lee L K, Bettelheim F A. Age dependence of freezable and nonfreezable water content of normal human lenses. Invest Ophthalmol Vis Sci. 1985; 26: 1162–1165
   PubMed Web of Science ®Google Scholar
• Sweeney M H, Truscott R J. An impediment to glutathione diffusion in older normal human lenses: a possible precondition for nuclear cataract. Exp Eye Res. 1998; 67: 587–595
   PubMed Web of Science ®Google Scholar
• Raghavachari N, Lou M F. Evidences for the presence of thioltransferase in the lens. Exp Eye Res. 1996; 63: 433–441
   PubMed Web of Science ®Google Scholar