NADH photo-oxidation is enhanced by a partially purified λ-crystallin fraction from rabbit lens

Molecular Vision

Volumn 13, Issue , 2007, Pages 1722-1729

  Bando, Masayasu ^a   Oka, Mikako ^b   Kawai, Kenji ^a   Obazawa, Hajime ^c   Takehana, Makoto ^b  

^a TOKAI UNIVERSITY SCHOOL OF MEDICINE   (Japan)

^b KEIO UNIVERSITY   (Japan)

^c Eye Res Inst of Cataract Found   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; ASCORBIC ACID; OXYGEN; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE; SUPEROXIDE; SUPEROXIDE DISMUTASE; XANTHINE; XANTHINE OXIDASE;

ANIMAL CELL; ANIMAL TISSUE; ANTIOXIDANT ACTIVITY; ARTICLE; COLUMN CHROMATOGRAPHY; CONCENTRATION (PARAMETERS); CONTROLLED STUDY; FILTER; GEL FILTRATION; LENS EPITHELIUM; NONHUMAN; OXYGEN TENSION; PHOTOOXIDATION; PHOTOSENSITIZATION; PRIORITY JOURNAL; PROTEIN BINDING; PROTEIN PURIFICATION; RABBIT; RADIATION ABSORPTION; ULTRAVIOLET RADIATION; VERTEBRATE;

ANIMALS; CRYSTALLINS; LENS, CRYSTALLINE; NAD; OXIDATION-REDUCTION; RABBITS; SUPEROXIDES; ULTRAVIOLET RAYS; XANTHINE; XANTHINE OXIDASE;

EID: 34748893564     PISSN: None     EISSN: 10900535     Source Type: Journal    
DOI: None     Document Type: Article

References (50)

1. Kinsey VE. Spectral transmission of the eye to ultraviolet radiations. Arch Ophthalmol 1948; 39:508-13.
2. Boettner EA, Wolter JR. Transmission of the ocular media. Invest Ophthalmol 1962; 1:776-83.
3. van Heyningen R. The glucoside of 3-hydroxykynurenine and other fluorescent compounds in the human lens. In: The human lens - in relation to cataract. New York: Elsevier; 1973. p. 151-71.
4. Ham WT Jr, Mueller HA, Sliney DH. Retinal sensitivity to damage from short wavelength light. Nature 1976; 260:153-5.
5. Ham WT Jr, Mueller HA, Ruffolo JJ Jr, Guerry D 3rd, Guerry RK. Action spectrum for retinal injury from near-ultraviolet radiation in the aphakic monkey. Am J Ophthalmol 1982; 93:299-306.
6. Dillon J, Zheng L, Merriam JC, Gaillard ER. The optical properties of the anterior segment of the eye: implications for cortical cataract. Exp Eye Res 1999; 68:785-95.
7. Zigman, S, Vaughan T. Near-ultraviolet light effects on the lenses and retinas of mice. Invest Ophthalmol 1974; 13:462-5.
8. East EJ, Chang RC, Yu NT, Kuck JF Jr. Raman spectroscopic measurement of total sulfhydryl in intact lens as affected by aging and ultraviolet irradiation. Deuterium exchange as a probe for aceessible sulfhydryl in living tissue. J Biol Chem 1978; 253:1436-41.
9. Barron BC, Yu NT, Kuck JF Jr. Raman spectroscopic evaluation of aging and long-wave UV exposure in the guinea pig lens: a possible model for human aging. Exp Eye Res 1988; 46:249-58.
10. Bando M, Obazawa H. Ascorbate free radical reductase and ascorbate redox cycle in the human lens. Jpn J Ophthalmol 1988; 32:176-86.
11. Reddy VN, Giblin FJ. Metabolism and function of glutathione in the lens. Ciba Found Symp 1984; 106:65-87.
12. Zigler JS Jr, Rao PV. Enzyme/crystallins and extremely high pyridine nucleotide levels in the eye lens. FASEB J 1991; 5:223-5.
13. Rao PV, Zigler JS Jr. Extremely high levels of NADPH in guinea pig lens: correlation with zeta-crystallin concentration. Biochem Biophys Res Commun 1990; 167:1221-8.
14. Rao CM, Zigler JS Jr. Levels of reduced pyridine nucleotides and lens photodamage. Photochem Photobiol 1992; 56:523-8.
15. Cunningham ML, Johnson JS, Giovanazzi SM, Peak MJ. Photosensitized production of superoxide anion by monochromatic (290-405 nm) ultraviolet irradiation of NADH and NADPH coenzymes. Photochem Photobiol 1985; 42:125-8.
16. Cunningham ML, Krinsky NI, Giovanazzi SM, Peak MJ. Superoxide anion is generated from cellular metabolites by solar radiation and its components. J Free Radic Biol Med 1985; 1:381-5.
17. Matsukura S, Bando M, Obazawa H, Oka M, Takehana M. Ascorbate free radical reductase activity in vertebrate lenses of certain species. Jpn J Ophthalmol 2001; 45:233-9.
18. Mulders JW, Hendriks W, Blankesteijn WM, Bloemendal H, de Jong WW. Lambda-crystallin, a major rabbit lens protein, is related to hydroxyacyl-coenzyme A dehydrogenases. J Biol Chem 1988; 263:15462-6.
19. Ishikura S, Usami N, Araki M, Hara A. Structural and functional characterization of rabbit and human L-gulonate 3-dehydrogenase. J Biochem (Tokyo) 2005; 137:303-14.
20. Suzuki T, Bando M, Oka M, Tsukamoto H, Akatsuka I, Kawai K, Obazawa H, Kobayashi S, Takehana M. Iambda-crystallin related to dehydroascorbate reductase in the rabbit lens. Jpn J Ophthalmol 2003; 47:437-43.
21. Bando M, Oka M, Kawai K, Obazawa H, Kobayashi S, Takehana M. NADH binding properties of rabbit lens lambda-crystallin. Mol Vis 2006; 12:692-7.
22. Crapo JD, McCord JM, Fridovich I. Preparation and assay of superoxide dismutases. Methods Enzymol 1978; 53:382-93.
23. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klenk DC. Measurement of protein using bicinchoninic acid. Anal Biochem 1985; 150:76-85. Erratum in: Anal Biochem 1987; 163:279.
24. Nishikimi M. Oxidation of ascorbic acid with superoxide anion generated by the xanthine-xanthine oxidase system. Biochem Biophys Res Commun 1975; 63:463-8.
25. Chan PC, Bielski BH. Enzyme-catalyzed free radical reactions with nicotinamide adenine nucleotides. II. Lactate dehydrogenase-catalyzed oxidation of reduced nicotinamide adenine dinucleotide by superoxide radicals generated by xanthine oxidase. J Biol Chem 1974; 249:1317-9.
26. Bielski BH, Chan PC. Re-evaluation of the kinetics of lactate dehydrogenase-catalyzed chain oxidation of nicotinamide adenine dinucleotide by superoxide radicals in the presence of ethylenediaminetetraacetate. J Biol Chem 1976; 251:3841-4.
27. Cban PC, Bielski BH. Glyceraldehyde-3-phosphate dehydrogenase-catalyzed chain oxidation of reduced nicotinamide adenine dinucleotide by perhydroxyl radicals. J Biol Chem 1980; 255:874-6.
28. Bhuyan KC, Bhuyan DK. Superoxide dismutase of the eye: relative functions of superoxide dismutase and catalase in protecting the ocular lens from oxidative damage. Biochim Biophys Acta 1978; 542:28-38.
29. Varma SD, Chand D, Sharma YR, Kuck JF Jr, Richards RD. Oxidative stress on lens and cataract formation: role of light and oxygen. Curr Eye Res 1984; 3:35-57.
30. Varma SD, Ets TK, Richards RD. Protection against superoxide radicals in rat lens. Ophthalmic Res 1977; 9:421-31.
31. Sawada. Y, Yamazaki I. One-electron transfer reactions in bio-chemical systems. 8. Kinetic study of superoxide dismutase. Biochim Biophys Acta 1973; 327:257-65.
32. Petrat F, Bramey T, Kirsch M, De Groot H. Initiation of a superoxide-dependent chain oxidation of lactate dehydrogenase-bound NADH by oxidants of low and high reactivity. Free Radic Res 2005; 39:1043-57.
33. Eaton JW. Is the lens canned? Free Radic Biol Med 1991; 11:207-13.
34. Wistow GJ. Molecular biology and evolution of crystallins: gene recruitment and multifunctional proteins in the eye lens. Austin (TX): RG Landes; 1995.
35. Wistow GJ, Mulders JW, de Jong WW. The enzyme lactate dehydrogenase as a structural protein in avian and crocodilian lenses. Nature 1987; 326:622-4.
36. Jimenez-Asensio J, Gonzalez P, Zigler JS Jr, Garland DL. Glyceraldehyde 3-phosphate dehydrogenase is an enzyme-crystallin in diurnal geckos of the genus Phelsuma. Biochem Biophys Res Commun 1995; 209:796-802.
37. Graham C, Hodin J, Wistow G. A retinaldehyde dehydrogenase as a structural protein in a mammalian eye lens. Gene recruitment of eta-crystallin. J Biol Chem 1996; 271:15623-8.
38. Rao PV, Krishna CM, Zigler JS Jr. Identification and characterization of the enzymatic activity of zeta-crystallin from guinea pig lens. A novel NADPH:quinone oxidoreductase. J Biol Chem 1992; 267:96-102.
39. Hyndman D, Bauman DR, Heredia VV, Penning TM. The aldoketo reductase superfamily homepage. Chem Biol Interact 2003; 143-144:621-31.
40. Burczynski ME, Sridhar GR, Palackal NT, Penning TM. The reactive oxygen species - and Michael acceptor-inducible human aldo-keto reductase AKR1C1 reduces the alpha,beta-unsaturated aldehyde 4-hydroxy-2-nonenal to 1,4-dihydroxy-2-nonene. J Biol Chem 2001; 276:2890-7.
41. Srivastava S, Spite M, Trent JO, West MB, Ahmed Y, Bhatnagar A. Aldose reductase-catalyzed reduction of aldehyde phospholipids. J Biol Chem 2004; 279:53395-406.
42. Friedburg D. Enzyme activity patterns in clear human lenses and in different types of human senile cataract. In: The human lens- in relation to cataract. New York: Elsevier; 1973. p. 117-33.
43. King G, Holmes R. Human corneal and lens aldehyde dehydrogenases. Purification and properties of human lens ALDH1 and differential expression as major soluble proteins in human lens (ALDH1) and cornea (ALDH3). Adv Exp Med Biol 1997; 414:19-27.
44. King G, Holmes R. Human ocular aldehyde dehydrogenase isozymes: distribution and properties as major soluble proteins in cornea and lens. J Exp Zool 1998; 282:12-7.
45. King G, Hirst L, Holmes R. Human corneal and lens aldehyde dehydrogenases. Localization and function(s) of ocular ALDH1 and ALDH3 isozymes. Adv Exp Med Biol 1999; 463:189-98.
46. Choudhary S, Xiao T, Vergara LA, Srivastava S, Nees D, Piatigorsky J, Ansari NH. Role of aldehyde dehydrogenase isozymes in the defense of rat lens and human lens epithelial cells against oxidative stress. Invest Ophthalmol Vis Sci 2005: 46:259-67.
47. Wood AM, Truscott RJ. UV filters in human lenses: tryptophan catabolism. Exp Eye Res 1993; 56:317-25.
48. Bova LM, Sweeney MH, Jamie JF, Truscott RJ. Major changes in human ocular UV protection with age. Invest Ophthalmol Vis Sci 2001; 42:200-5.
49. Thiagarajan G, Shirao E, Ando K, Inoue A, Balasubramanian D. Role of xanthurenic acid 8-O-beta-D-glucoside, a novel fluorophore that accumulates in the brunescent human eye lens. Photochem Photobiol 2002; 76:368-72.
50. Inoue A, Sasaki D, Satoh K. Minimization of photooxidative insult to calf lens protein irradiated with near UV-light in the presence of pigmented glucosides derived from human lens protein. Exp Eye Res 2004; 79:833-7.