Alpha-Crystallin Acting As a Molecular Chaperonin Against Photodamage by UV Irradiation

Overview

Journal J Protein Chem

Specialties Biochemistry
Chemistry

Date 1997 May 1

PMID 9188067

Citations 12

Authors

J S Lee

J H Liao

S H Wu

S H Chiou

Affiliations

Soon will be listed here.

Abstract

alpha-Crystallin, a major protein of the eye lens, is known to have chaperone activity in preventing heat-induced aggregation of enzymes and other crystallins. In this study, we investigate the ability of alpha-crystallin to inhibit UV-light-induced aggregation of other lens proteins and the effect of exposure of alpha-crystallin to UV irradiation on its chaperone activity. The chaperone activities of alpha-crystallin preincubated at different temperatures were found to be different and could be correlated with its change in quaternary structure as determined by the fluorescence probe ANS (8-anilo-1-naphthalene sulfonate). alpha-Crystallin can inhibit the aggregation of gamma-crystallin from UV irradiation at room temperature, and the preheated alpha-crystallins provide more protection than the native one. Upon irradiation by UV light, alpha-crystallin gradually lost its ability to protect beta-crystallin against thermal aggregation. The loss of the chaperone efficacy of alpha-crystallin to protect other lens proteins may shed light on human cataract formation induced by long-term exposure to UV irradiation.

Citing Articles

UV light and the ocular lens: a review of exposure models and resulting biomolecular changes.

MacFarlane E, Donaldson P, Grey A Front Ophthalmol (Lausanne). 2024; 4:1414483.

PMID: 39301012 PMC: 11410779. DOI: 10.3389/fopht.2024.1414483.

The mechanism for thermal-enhanced chaperone-like activity of α-crystallin against UV irradiation-induced aggregation of γD-crystallin.

Li H, Yu Y, Ruan M, Jiao F, Chen H, Gao J Biophys J. 2022; 121(12):2233-2250.

PMID: 35619565 PMC: 9279354. DOI: 10.1016/j.bpj.2022.05.032.

UV-B induced fibrillization of crystallin protein mixtures.

Cetinel S, Semenchenko V, Cho J, Ghaffari Sharaf M, Damji K, Unsworth L PLoS One. 2017; 12(5):e0177991.

PMID: 28542382 PMC: 5444657. DOI: 10.1371/journal.pone.0177991.

Differential role of arginine mutations on the structure and functions of α-crystallin.

Panda A, Nandi S, Chakraborty A, Nagaraj R, Biswas A Biochim Biophys Acta. 2015; 1860(1 Pt B):199-210.

PMID: 26080000 PMC: 4914040. DOI: 10.1016/j.bbagen.2015.06.004.

Molecular mechanism of formation of cortical opacity in CRYAAN101D transgenic mice.

Hegde S, Srivastava K, Tiwary E, Srivastava O Invest Ophthalmol Vis Sci. 2014; 55(10):6398-408.

PMID: 25146988 PMC: 4197685. DOI: 10.1167/iovs.14-14623.

References

Chiou S, Chylack Jr L, Tung W, BUNN H . Nonenzymatic glycosylation of bovine lens crystallins. Effect of aging. J Biol Chem. 1981; 256(10):5176-80. View

Das K, Surewicz W . Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 1995; 369(2-3):321-5. DOI: 10.1016/0014-5793(95)00775-5. View

Raman B, Rao C . Chaperone-like activity and quaternary structure of alpha-crystallin. J Biol Chem. 1994; 269(44):27264-8. View

Groenen P, Merck K, de Jong W, Bloemendal H . Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Eur J Biochem. 1994; 225(1):1-19. DOI: 10.1111/j.1432-1033.1994.00001.x. View

Horwitz J . Alpha-crystallin can function as a molecular chaperone. Proc Natl Acad Sci U S A. 1992; 89(21):10449-53. PMC: 50356. DOI: 10.1073/pnas.89.21.10449. View

Hendrick J, Hartl F . Molecular chaperone functions of heat-shock proteins. Annu Rev Biochem. 1993; 62:349-84. DOI: 10.1146/annurev.bi.62.070193.002025. View

Kelley M, David L, Iwasaki N, Wright J, Shearer T . alpha-Crystallin chaperone activity is reduced by calpain II in vitro and in selenite cataract. J Biol Chem. 1993; 268(25):18844-9. View

Chiou S, Azari P . Physicochemical characterization of alpha-crystallins from bovine lenses: hydrodynamic and conformational properties. J Protein Chem. 1989; 8(1):1-17. DOI: 10.1007/BF01025075. View

Goosey J, Zigler Jr J, KINOSHITA J . Cross-linking of lens crystallins in a photodynamic system: a process mediated by singlet oxygen. Science. 1980; 208(4449):1278-80. DOI: 10.1126/science.7375939. View

10.

Schauerte J, Gafni A . Photodegradation of tryptophan residues and attenuation of molecular chaperone activity in alpha-crystallin are correlated. Biochem Biophys Res Commun. 1995; 212(3):900-5. DOI: 10.1006/bbrc.1995.2054. View

11.

Augusteyn R, Ghiggino K, Putilina T . Studies on the location of aromatic amino acids in alpha-crystallin. Biochim Biophys Acta. 1993; 1162(1-2):61-71. DOI: 10.1016/0167-4838(93)90128-e. View

12.

Hott J, Borkman R . Concentration dependence of transmission losses in UV-laser irradiated bovine alpha-, beta H-, beta L- and gamma-crystallin solutions. Photochem Photobiol. 1993; 57(2):312-7. DOI: 10.1111/j.1751-1097.1993.tb02293.x. View

13.

Walker M, Borkman R . Light scattering and photocrosslinking in the calf lens crystallins gamma-II, III and IV. Exp Eye Res. 1989; 48(3):375-83. DOI: 10.1016/s0014-4835(89)80006-5. View

14.

Fujimori E . Crosslinking and blue-fluorescence of photo-oxidized calf-lens alpha-crystallin. Exp Eye Res. 1982; 34(3):381-8. DOI: 10.1016/0014-4835(82)90084-7. View

15.

Dillon J, Spector A . Detection of bityrosine in cataractous human lens protein. Science. 1978; 199(4331):897-9. DOI: 10.1126/science.622574. View

16.

Srivastava O . Age-related increase in concentration and aggregation of degraded polypeptides in human lenses. Exp Eye Res. 1988; 47(4):525-43. DOI: 10.1016/0014-4835(88)90092-9. View

17.

Horwitz J . Proctor Lecture. The function of alpha-crystallin. Invest Ophthalmol Vis Sci. 1993; 34(1):10-22. View

18.

Borkman R, Knight G, Obi B . The molecular chaperone alpha-crystallin inhibits UV-induced protein aggregation. Exp Eye Res. 1996; 62(2):141-8. DOI: 10.1006/exer.1996.0018. View

19.

Kato A, Nakai S . Hydrophobicity determined by a fluorescence probe method and its correlation with surface properties of proteins. Biochim Biophys Acta. 1980; 624(1):13-20. DOI: 10.1016/0005-2795(80)90220-2. View