UV-B-induced secondary conformational changes in lens α-crystallin

Journal of Photochemistry and Photobiology B: Biology

Volumn 49, Issue 1, 1999, Pages 29-34

  Lin, Shan Yang ^a   Ho, Chia Jen ^a   Li, Mei Jane ^a  

^a TAIPEI VETERANS GENERAL HOSPITAL   (Taiwan)

Author keywords

Lens crystallin; Reflectance FT IR; Secondary conformation; Turbidity; UV B

Indexed keywords

ALPHA CRYSTALLIN; LENS PROTEIN;

ALPHA HELIX; AQUEOUS SOLUTION; ARTICLE; BETA CHAIN; CONFORMATIONAL TRANSITION; FOURIER TRANSFORMATION; INFRARED SPECTROSCOPY; KINETICS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN SECONDARY STRUCTURE; TURBIDITY; ULTRAVIOLET B RADIATION; ULTRAVIOLET SPECTROPHOTOMETRY;

ANIMALS; CATTLE; CRYSTALLINS; KINETICS; LENS, CRYSTALLINE; NEPHELOMETRY AND TURBIDIMETRY; PROTEIN STRUCTURE, SECONDARY; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; ULTRAVIOLET RAYS;

EID: 0033103067     PISSN: 10111344     EISSN: None     Source Type: Journal    
DOI: 10.1016/S1011-1344(99)00010-X     Document Type: Article

References (42)

1. [1] J. Horwitz, The function of alpha-crystallin, Invest. Ophthal. Vis. Sci. 34 (1993) 10-22.
2. [2] P.J.T.A. Groenen, K.B. Merck, W.W. de Jong, H. Bloemendal, Structure and modifications of the junior chaperone α-crystallin: from lens transparency to molecular pathology, Eur. J. Biochem. 225 (1994) 1-19.
3. [3] J. Harding (Ed.), Cataract: Biochemistry, Epidemiology and pharmacology, Chapman and Hall, London, 1991, pp. 1-82.
4. [4] B. Raman, T. Ramakrishna, C.M. Rao, Temperature dependent chaperone-like activity of alpha-crystallin, FEBS Lett. 365 (1995) 133-136.
5. [5] J. Bours, Calf lens α-crystallin, a molecular chaperone, builds stable complexes with βs-and γ-crystallins, Ophthalmic Res. 28 (suppl. 1) (1996) 23-31.
6. [6] K.J. Dilley, A. Pirie, Changes in the proteins of the human lens nucleus in cataract, Exp. Eye Res. 19 (1974) 59-72.
7. [7] A. Spector, T. Freund, L.K. Li, R.C. Augusteyn, Age-dependent changes in the structure of alpha crystallin, Invest. Ophthal. Vis. Sci. 13 (1971) 677-686.
8. [8] J.N. Liang, S.K. Bose, B. Chakrabarti, Age-related changes in protein formation in bovine lens crystallins, Exp. Eye Res. 40 (1985) 461-469.
9. [9] U.P. Adley, P. Sutherland, J.N. Liang, B. Chakrabarti, Changes in tertiary structure of calf-lens α-crystallin by near UV irradiation: role of hydrogen peroxide, Photochem. Photobiol. 40 (1984) 343-349.
10. [10] U.P. Andley, S.F. Chapman, Conformational changes of bovine lens crystallins in a photodynamic system, Photochem. Photobiol. 44 (1985) 67-74.
11. [11] U.P. Andley, Spectroscopic studies on the riboflavin-sensitized conformational changes of calf lens α-crystallin, Exp. Eye Res. 46 (1988) 531-544.
12. [12] R.F. Borkman, G. Knight, B. Obi, The molecular chaperone α-crystallin inhibits UV-induced protein aggregation, Exp. Eye Res. 62 (1996) 141-148.
13. [13] D.H. Sliney, Physical factors in cataractogenesis: ambient ultraviolet radiation and temperature, Invest. Ophthal. Vis. Sci. 27 (1986) 781-790.
14. [14] U.P. Andley, Photodamage to the eye, Photochem. Photobiol. 46 (1987) 1057-1066.
15. [15] H.R. Taylor, S.K. West, F.S. Rosenthal, B. Munoz, H.S. Newland, H. Abbey, E.A. Emmett, Effect of ultraviolet radiation on cataract formation, New Engl. J. Med. 319 (1988) 1429-1433.
16. [16] U.P. Andley, B.A. Clark, Generation of oxidants in the near-UV photo-oxidation of human lens α-crystallin, Invest. Ophthal. Vis. Sci. 30 (1989) 706-713.
17. [17] M. McDermott, R. Chiesa, J.E. Roberts, J. Dillon, Photoxidation of specific residues in α-crystallin polypeptides, Biochemistry 30 (1991) 8653-8660.
18. [18] D.Y. Li, R.F. Borkman, R.H. Wang, J. Dillon, Mechanisms of photochemically produced turbidity in lens protein solutions, Exp. Eye Res. 51 (1990) 663-669.
19. L-and γ-crystallin solutions, Photochem. Photobiol. 57 (1993) 312-317.
20. [20] R.F. Borkman, J. Mclaughlin, The molecular chaperone function of α-crystallin is impaired by UV photolysis, Photochem. Photobiol. 62 (1995) 1046-1051.
21. [21] J.A. Schauerte, A. Gafni, Photodegradation of tryptophan residues and attenuations of molecular chaperone activity in α-crystallin are correlated, Biochem Biophys, Res. Commun. 212 (1995) 900-905.
22. [22] S.Y. Lin, S.M. Lee, C.L. Cheng, R.C. Liang, Effect of diabetic duration on the seondary structures of human lens capsules in diabetic cataracts, Biochem. Biophys. Res. Commun. 216 (1995) 183-189.
23. [23] S.M. Lee, S.Y. Lin, C.L. Cheng, R.C. Liang, Possible changes in secondary structures and composition of human lens capsules in hereditary congenital cataract, Graef. Arch. Clin. Exper. Ophthal. 234 (1996) 342-348.
24. [24] S.M. Lee, S.Y. Lin, C.L. Cheng, R.C. Liang, Progressive changes in secondary conformation and composition of the senile cataractous human lens capsules, Acta Ophthal. Scan. 74 (1996) 542-546.
25. [25] S.M. Lee, S.Y. Lin, M.J. Li, R.C. Liang, Possible mechanism of exacerbating cataract formation in cataractous human lens capsules induced by systemic hypertension or glaucoma, Ophthalmic Res. 29 (1997) 83-90.
26. [26] S.Y. Lin, R.C. Liang, The effect of ultraviolet B irradiation on the isolated porcine stratum corneum: colorimetric and ATR/FT-IR spectroscopic investigations, Biomed. Res. 15 (1994) 9-15.
27. [27] S.Y. Lin, K.J. Duan, T.C. Lin, Skin lipid-ordering effect of pyrrolidone-carboxylate sodium after topical treatment with penetration enhancers, Biomed. Mater. Engineer. 5 (1995) 9-20.
28. [28] S.Y. Lin, K.J. Duan, T.C. Lin, Simultaneous determination of the protein conversion process in porcine stratum corneum after pretreatment with skin enhancers by a combined microscopic FT-IR/DSC system, Spectrochim. Acta (A) 52 (1996) 1671-1678.
29. [29] S.Y. Lin, K.J. Duan, T.C. Lin, Microscopic FT-IR/DSC combined system used to investigate the thermotropic behavior of lipidin porcine stratum corneum after pretreatment with skin penetration enhancers, Skin Res. Technol. 2 (1996) 186-191.
30. [30] S.Y. Lin, C.M. Liao, G.H. Hsiue, Thermal-dependent anhydride formation of eudragit L-100 films determined by reflectance FTIR/DSC microspectroscopy, Polymer 36 (1995) 3239-3241.
31. [31] L.S. Lee, C.W. Chi, H.C. Liu, C.L. Cheng, M.J. Li, S.Y. Lin, Assessment of protein conformation in human benign and malignant astrocytomas by reflectance FT-IR microspectroscopy, Oncol. Res. 10 (1998) 23-27.
32. [32] D.C. Lee, D. Chapman, Analysis of peptide and protein structures using Fourier transform infrared spectroscopy, Meth. Mol. Biol. 22 (1994) 183-202.
33. [33] H. Susi, D.M. Byler, Protein structure by Fourier transform infrared spectroscopy: second derivative spectra, Biochem. Biophys. Res. Commun. 115 (1983) 391-397.
34. [34] E.A. Cooper, K. Knutson, Fourier transform infrared spectroscopy investigations of protein structure, in: J.N. Herron, W. Jiskoot, D.J.A. Crommelin (Eds.), Physical Methods to Characterize Pharmaceutical Proteins, Plenum, New York, 1995, pp. 101-143.
35. [35] J.D. Goosey, J.S. Zigler, J.H. Kinoshita, Cross-linking of lens crystallins in a photodynamic system: a process mediating by singlet oxygen, Science 208 (1980) 1278-1290.
36. [36] J. Dillon, R.H. Wang, S.J. Atherton, Photochemical and photophysical studies on human lens constitutents, Photochem. Photobiol. 52 (1990) 849-854.
37. [37] S.H. Rao, C.M. Rao, D. Balasubramanian, The conformational status of a protein influences the aerobic photolysis of its tryptophan residues: melittin, β-lactoglobulin and the crystallins, Photochem. Photobiol. 51 (1990) 357-362.
38. [38] W.K. Surewicz, P.R. Olesen, On the thermal stability of α-crystallin: a new insight from infrared spectroscopy. Biochemistry 34 (1995) 9655-9660.
39. [39] T.M. Przybycien, J.E. Bailey, Structure-relationships in the inorganic salt-induced precipitation of alpha-chymotrypsin, Biochim. Biophys. Acta 995 (1989) 231-245.
40. [40] Y. Kim, C.A. Rose, Y. Liu, Y. Ozaki, G. Datta, A.T. Tu, FT-IR and near infrared FT-Raman studies of the secondary structure of insulinotropin in the solid state: α-helix to β-sheet conversion induced by phenol and/or high shear force, J. Pharm. Sci. 83 (1994) 1175-1180.
41. [41] U.P. Andley, B.A. Clark, Photoreaction of human lens monomeric crystallins, Biochim. Biophys. Acta 7 (1988) 571-579.
42. [42] R.F. Borkman, A. Douhal, K. Yoshihara, Picosecond fluorescence decay in photolyzed lens protein alpha-crystallin, Biochemistry 32 (1993) 4787-4792.