Glutathione reductase in human lens epithelium: FAD-induced in vitro activation

References

• Reddy V. N., Giblin F. J. Metabolism and function of glutathione in the lens. “Human Cataract Formation”, Ciba Foundation Symposium 106. Pitman, London 1984; 65–87
   Google Scholar
• Cheng H-M, Chylack L. T., Jr. Lens metabolism. “The Ocular Lens, Structure, Function and Pathology”, H. Maisel. Marcel Dekker, New York 1985; 223–264
   Google Scholar
• Karkela A., Miettinen P. On the changes in the activity of glutathione reductase on the maturation of senile cataract. Acta. Ophthalmologica 1961; 39: 411–415
   Web of Science ®Google Scholar
• Friedburg D., Manthey K. F. Glutathione and NADP linked enzymes in human senile cataract. Exp. Eye Res 1973; 15: 173–177
   PubMed Web of Science ®Google Scholar
• Srivastava S. K., Villacorte D., Arya D. V. 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
• 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
• Rao G. N., Sadasivudu B., Cotlier E. Studies on glutathione S-transferase, glutathione peroxidase and glutathione reductase in human normal and cataractous lens. Ophthalmic Res 1983; 15: 173–179
   PubMed Web of Science ®Google Scholar
• Ohrloff C., Hockwin O., Olson R., Dickman S. Glutathione peroxidase, glutathione reductase and superoxide dismutase in the aging lens. Curr. Eye Res 1984; 3: 109–115
   PubMed Web of Science ®Google Scholar
• Harding J. J., Crabbe J. C. The lens: Development, proteins, metabolism and cataract. “The Eye”, Vol. IB, H. Davson. Academic Press, Orlando 1984; 352–353
   Google Scholar
• Horwitz J., Neuhaus R., Dockstader J. Analysis of microdissected cataractous human lenses. Invest. Ophthalmol. Vis. Sci 1980; 21: 616–619
   Web of Science ®Google Scholar
• Horwitz J., Hansen J. S., Cheung C-C., Ding L-L., Straatsma B. R., Lightfoot D. O., Takemoto L. J. Presence of low molecular weight polypeptides in human brunescent cataracts. Biochem. Biophys. Res. Comm 1983; 223: 65–71
   Google Scholar
• Takemoto L. J., Hansen J. S., Horwitz J. Biochemical analysis of microdissected sections from the normal and cataractous human lens. Curr. Eye Res 1983; 2: 443–450
   Web of Science ®Google Scholar
• Straatsma B. R., Horwitz J., Takemoto L. J., Lightfoot D. O., Ding L-L. Clinicobiochemical correlations in aging-related human cataract. Am. J. Ophthalmol 1984; 97: 457–469
   PubMed Web of Science ®Google Scholar
• McFall-Ngai M. J., Ding L-L., Takemoto L. J., Horwitz J. Spatial and temporal mapping of the age-related changes in human lens crystallins. Exp. Eye Res 1985; 41: 745–758
   PubMed Web of Science ®Google Scholar
• Dovrat A., Straatsma B. R., Revilla P., Lightfoot D. O., Horwitz J. Analysis of five key enzymes in freshly excised human lens epithelium. Invest. Ophthalmol. Vis. Sci 1987; 28: 384, (Suppl.)
   PubMedGoogle Scholar
• Bradford M. M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem 1976; 72: 248–254
   PubMed Web of Science ®Google Scholar
• Chylack L. T., Bettelheim F. A., Tung W. H. Studies on human cataracts I. Evaluation of techniques of human cataract preservation after extraction. Invest. Ophthalmol. Vis. Sci 1981; 20: 327–333
   PubMed Web of Science ®Google Scholar
• Paterson C. A., Delamere N. A., Mawhorter L., Cuizon J. V. Na, K-ATPase in simulated eye bank and cryoextracted rabbit lenses, and human eye bank lenses and cataracts. Invest. Ophthalmol. Vis. Sci 1983; 24: 1534–1538
   PubMed Web of Science ®Google Scholar
• Glatzle D., Korner W. F., Christeller S., Wiss O. Method for the detection of a biochemical riboflavin deficiency stimulation of NADPH-dependent glutathione reductase from human erythrocytes by FAD in vitro. In vestigations on the Vitamin B2 status in healthy people and geriatric patients. Internal.”. J. Vit. Res 1970; 40: 166–183
   Google Scholar
• Williams C. H., Jr. “The Enzymes”, 3rd ed, Vol. 13, P. O. Boyer. Academic Press, New York 1976; 89–172
   Google Scholar
• Thieme R., Pai E. F., Schirmer R. H., Schulz G. E. Three-dimensional structure of glutathione-reductase at 2A resolution. J. Mol. Biol 1981; 152: 763–782
   PubMed Web of Science ®Google Scholar
• Pai E. F., Schulz G. E. The catalytic mechanism of glutathione reductase as derived from X-ray diffraction analyses of reaction intermediates. J. Biol. Chem 1983; 258: 1752–1757
   PubMed Web of Science ®Google Scholar
• Beutler E. Glutathione reductase: Stimulation in normal subjects by riboflavin supplementation. Science 1969; 165: 613–615
   PubMed Web of Science ®Google Scholar
• Ono S., Hirano H. FAD-induced in vitro activation of glutathione reductase in the lens of B2 deficient rats. Curr. Eye Res 1984; 3: 663–665
   PubMed Web of Science ®Google Scholar
• Skalka H. W., Prchal J. T. Riboflavin deficiency and cataract formation. Metabol. Ped. Ophthalmol 1981; 5: 17–20
   PubMedGoogle Scholar
• Skalka H. W., Prchal J. T. Cataracts and riboflavin deficiency. Am. J. Clin. Nutrit 1981; 34: 861–863
   PubMed Web of Science ®Google Scholar
• van Veelen A. W.C., Rijksen G., Vlug A. M.C., Staal G. E.J. Correlation between cataract and glutathione metabolism. Clinica Chimica Acta 1983; 131: 123–128
   PubMed Web of Science ®Google Scholar
• Jacques P. P., Hartz S. C., Chylack L. T., Jr., McGandy R. B., Sadowski J. A. Nutritional status in persons with and without senile cataract: Blood vitamin and mineral levels. J. Clin. Nutrit 1987, in press
   Google Scholar
• Jusco W. J., Levy G. Absorption, protein binding, and elimination of riboflavin. “Riboflavin”, R. S. Rivlin. Plenum Press, New York 1975; 100–146
   Google Scholar
• McCormick D. B. Metabolism of riboflavin. “Riboflavin”, R. S. Rivlin. Plenum Press, New York 1975; 153–189
   Google Scholar
• Merrill A. H., Froehlich J. A., McCormick D. B. Isolation and identification of alternative riboflavin-binding proteins from human plasma. Biochemical Med 1981; 25: 198–206
   PubMedGoogle Scholar
• Ono S., Hirano H., Sato Y. Formation of flavin adenine dinucleotide and flavin mononucleotide by lens homogenate. Exp. Eye Res 1982; 34: 297–301
   PubMed Web of Science ®Google Scholar
• Ono S., Hirano H. Riboflavin metabolism in the single lens of rat. Ophthalmic Res 1983; 15: 140–145
   PubMed Web of Science ®Google Scholar
• Fecondo J., Augusteyn R. Superoxide dismutase, catalase and glutathione peroxidase in the human cataractous lens. Exp. Eye Res 1983; 36: 15–23
   PubMed Web of Science ®Google Scholar
• Kuck J. F.R. Leucine metabolism by same-donor pairs of human lenses from eye bank eyes. Ophthalmic. Res 1982; 14: 450–458
   PubMed Web of Science ®Google Scholar
• Rathbun W. B., Bovis M. G. Activity of gluthathione peroxidase and glutathione reductase in the human lens related to age. Curr. Eye Res 1986; 5: 381–385
   PubMed Web of Science ®Google Scholar
• Yagi K., Ohishi N., Ohkawa H. Biomedical aspects of flavoproteins. “Flavin and Flavoproteins”, V. Massey, C. H. Williams. Elsevier North Holland, Amsterdam 1982; Vol. 21: 402–409
   Google Scholar
• Rivlin R. S., Langdon R. G. Regulation of hepatic FAD levels by thyroid hormone. “Advances in Enzyme Regulation”, G. Weber. Pergamon Press, OxfordEngland 1966; Vol. 4: 44–58
   Google Scholar
• Domjan G., Kokai K. The flavin adenine dinucleotide (FAD) content of the rat's liver in hypothyroid state and in the liver of hypothyroid animals after in vivo thyroxine treatment. Acta Biol. Hung 1966; 16: 237–241
   Google Scholar
• Cimino J. A., Jhangiani S., Schwartz E., Cooperman J. M. Riboflavin metabolism in the hypothyroid human adult. Proc. Soc. Exp. Biol. Med 1987; 184: 151–153
   PubMed Web of Science ®Google Scholar
• Rivlin R. S. Hormonal regulation of riboflavin metabolism. “Riboflavin”, R. S. Rivlin. Plenum Press, New York 1975; 393–420
   Google Scholar
• Reddi A. S. Riboflavin nutritional status and flavoprotein enzymes in streptozotocin-diabetic rats. Biochim. et Biophys. Acta 1986; 882: 71–76
   PubMedGoogle Scholar
• Rivlin R. S., Pinto J., Huang Y-P., Pelliccione N. Regulation of flavin metabolism by thyroid hormones and psychotropic drugs. “Flavin and Flavoproteins”, V. Massay, C. H. Williams. Elsevier North Holland, Amsterdam 1982; Vol. 21: 417–421
   Google Scholar