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Original Article

Effect of UVB radiation on corneal aldehyde dehydrogenase

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Pages 685-690 | Received 25 Nov 1995, Accepted 27 Feb 1996, Published online: 02 Jul 2009

References

  • Boettner E. A., Wolters J. R. Transmission of the ocular media. Invest. Ophthalmol. 1962; 1: 776–783
  • Kinsey V. E. Spectral transmission of the eye to ultraviolet radiation. Arch. Ophthalmol. 1948; 39: 508–513
  • Kurzel R. B, Wolbarsht M. L., Yamanishi B. S. Ultraviolet radiation effects on the eye. Photochem. Photo-biol. Rev. 1977; 2: 133–167
  • Cogan D. G., Kinsey V. E. Action spectrum of keratitis produced by ultraviolet radiation. Arch. Ophthalmol. 1946; 35: 670–677
  • Pitts D. G, Cullen A. P., Hacker P. D. Ocular effects of ultraviolet radiation from 295 to 365 nm. Invest. Ophthalmol. Visual Sci. 1977; 16: 932–939
  • Grossweiner L. I. Photochemistry of proteins: a review. Curr. Eye Res. 1984; 3: 137–144
  • Esterbauer H., Zollner H., Lang J. Metabolism of the lipid peroxidation product 4-hydroxynonenal by isolated hepatocytes and by liver cytosolic fractions. Bio-chem. J. 1985; 228: 363–373
  • Gondhowiardjo T. D, van-Haeringen N. J., Kijlstra A. Molecular weight forms of corneal aldehyde dehydrogenase. Curr. Eye Res. 1992; 11: 377–381
  • Abedinia M., Pain T., Algar E. M., Holmes R. S. Bovine corneal aldehyde dehydrogenase: the major soluble corneal protein with a possible dual protective role for the eye. Exp. Eye Res. 1990; 51: 419–426
  • Gondhowiaedjo T. D., van Haeringen N. J. Corneal aldehyde dehydrogenase, glutathione reductase and glutathione S-transferase in pathological corneas. Cornea 1993; 12: 310–314
  • Gondhowiardjo T. D., van Haeringen N. J, Hoekzema R., Pels L., Kijlstra A. Detection of aldehyde dehydrogenase in human corneal extracts. Curr. Eye Res. 1991; 11: 1001–1007
  • Lindahl R., Petersen D. R. Lipid aldehyde oxidation as a physiological role for class 3 aldehyde dehydro-genases. Biochem. Pharmacol. 1991; 41: 1583–1587
  • Cooper D. L, Baptist E. W, Enghild J. I, Isola N. R., Klintworth G. K. Bovine corneal protein 54K (BCP 54) is a homologue of the tumour-associated aldehyde dehydrogenase (class 3) rat aldehyde dehydrogenase (RATALD). Gene 1991; 98: 201–207
  • Rabaey M., Segers J. Changes in the polypep-tide composition of the bovine corneal epithelium during development. Vlth Congress of the European Society of Ophthalmology, P. D. Trevor-Roper. Academic Press, London 1981
  • Konishi Y., Mimura Y. Kinetic properties of the bovine corneal aldehyde dehydrogenase (BCP 54). Exp. Eye Res. 1992; 55: 569–578
  • Lindahl R. Aldehyde dehydrogenase in 2-acetamido-fluorene-induced rat hepatomas. Biochem. J. 1977; 164: 119–123
  • Lerman S. Radiant Energy and the Eye. Macmillan, New York 1980; 122–125
  • Perczel A., Park K., Fasman G. D. The convex constraint analysis method of protein secondary structure estimation. Anal. Biochem. 1992; 203: 83–93
  • Walrant P., Santus R. N-formylkynurenine, a Trp photooxidation product as a photodynamic sensitizer. Photochem. Photobiol. 1974; 20: 411–417
  • Guptasarma P., Balasubramanian D., Matsugo S., Saito I. Hydroxyl radical mediated damage to proteins, with special reference to the crystallins. Biochemistry 1992; 31: 4296–4303
  • Hott J. L., Borkman R. F. Analysis of photo-oxidized amino acids in tryptic peptides of calf lens gamma-II crystallin. Photochem. Photobiol. 1992; 56: 257–263
  • McDermott M., Chiesa R., Roberts J. E., Dillon J. Photooxidation of specific residues in alpha-crystallin polypeptides. Biochemistry 1991; 30: 8653–8660
  • Dillon J., Garner M. H, Roy D., Spector A. The photolysis of lens proteins: Molecular changes. Exp. Eye Res. 1982; 34: 651–658
  • Cardamone M., Puri N. K. Spectrofluorometric assessment of the surface hydrophobicity of proteins. Biochem. J. 1992; 282: 589–593
  • Davies K. J.A. Protein damage and degradation by oxygen radicals. J. Biol Chem. 1987; 262: 9895–9901
  • Mandal K., Kono M., Bose S. K, Thomson J., Chakrabarthi B. Structure and stability of Γ-crystal-lins-IV. Aggregation and structural destabilization in photosensitized reactions. Photochem. Photobiol. 1988; 47: 583–591
  • Horwitz J. α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA 1992; 89: 10449–10453
  • Wang K., Spector A. The chaperone activity of bovine α-crystallin. J. Biol. Chem. 1994; 269: 13601–13608
  • Raman B., Ramakrishna T., Mohan Rao C h. Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 1995; 365: 133–136

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