Eye lens αA- and αB-crystallin: Complex stability versus chaperone- like activity

Biochimica et Biophysica Acta - Protein Structure and Molecular Enzymology

Volumn 1434, Issue 1, 1999, Pages 114-123

  Van Boekel, Martinus A M ^a   De Lange, Frank ^a   De Grip, Willem J ^a   De Jong, Wilfried W ^a  

^a RADBOUD UNIVERSITY NIJMEGEN   (Netherlands)

Author keywords

Cataract; Chaperone; Crystallin; Eye lens; Protein evolution; Small heat shock protein

Indexed keywords

ALPHA CRYSTALLIN; CHAPERONE; CRYSTALLIN; HEAT SHOCK PROTEIN; PROTEIN SUBUNIT; 1-ANILINO-8-NAPHTHALENESULFONATE; 8 ANILINO 1 NAPHTHALENESULFONIC ACID; FLUORESCENT DYE; INSULIN; RECOMBINANT PROTEIN; UREA;

ANALYTIC METHOD; ARTICLE; CATARACT; CATTLE; LENS; NONHUMAN; PRIORITY JOURNAL; PROTEIN AGGREGATION; PROTEIN LOCALIZATION; PROTEIN STABILITY; PROTEIN STRUCTURE; THERMOSTABILITY; ANIMAL; CHEMISTRY; COMPARATIVE STUDY; GEL CHROMATOGRAPHY; INFRARED SPECTROSCOPY; PRECIPITATION; TEMPERATURE;

ANILINO NAPHTHALENESULFONATES; ANIMALS; CATTLE; CHROMATOGRAPHY, GEL; CRYSTALLINS; FLUORESCENT DYES; INSULIN; MOLECULAR CHAPERONES; PRECIPITATION; RECOMBINANT PROTEINS; SPECTROSCOPY, FOURIER TRANSFORM INFRARED; TEMPERATURE; UREA;

EID: 0033554332     PISSN: 01674838     EISSN: None     Source Type: Journal    
DOI: 10.1016/S0167-4838(99)00178-8     Document Type: Article

References (43)

1. P. Farnsworth, K. Singh (Eds.), Special Issue: α-Crystallin, Int. J. Biol. Macromol. 22 (1998) 149-344.
2. Vanhoudt J., Aerts T., Abgar S., Clauwaert J. Quaternary structure of bovine α-crystallin: influence of temperature. Int. J. Biol. Macromol. 22:1998;229-237.
3. van den Oetelaar P.J.M., Clauwaert J., van Laethem M., Hoenders H.J. The influence of isolation conditions on the molecular weight of α-crystallin. J. Biol. Chem. 260:1985;14030-14034.
4. van den Oetelaar P.J.M., van Someren P.F.H.M., Thomson J.A., Siezen R.J., Hoenders H.J. A dynamic quaternary structure of bovine α-crystallin as indicated from intermolecular exchange of subunits. Biochemistry. 29:1990;3488-3493.
5. Haley D.A., Horwitz J., Stewart P.L. The small heat shock protein αB-crystallin has a variable quaternary structure. J. Mol. Biol. 277:1998;27-35.
6. Caspers G.J., Leunissen J.A.M., de Jong W.W. The expanding small heat-shock protein family, and structure predictions of the conserved 'α-crystallin domain'. J. Mol. Evol. 40:1995;238-248.
7. Kim K.K., Kim R., Kim S.-H. Crystal structure of a small heat shock protein. Nature. 394:1998;595-599.
8. Horwitz J. α-Crystallin can act as a molecular chaperone. Proc. Natl. Acad. Sci. USA. 89:1992;10449-10453.
9. Farahbakhsh Z.T., Huang Q.L., Ding L.L., Altenbach C., Steinhoff H.J., Horwitz J., Hubbell W.L. Interaction of α-crystallin with spin-labeled peptides. Biochemistry. 34:1995;509-516.
10. Sun T.-X., Das B.K., Liang J.J.-N. Conformational and functional differences between recombinant human lens αA- and αB-crystallin. J. Biol. Chem. 272:1997;6220-6225.
11. Raman B., Rao C.M. Chaperone-like activity and quaternary structure of α-crystallin. J. Biol. Chem. 269:1994;27264-27268.
12. Wang K., Spector A. α-Crystallin can act as a chaperone under conditions of oxidative stress. Invest. Ophthalmol. Vis. Sci. 36:1995;311-321.
13. Lindner R.A., Kapur A., Carver J.A. The interaction of the molecular chaperone, α-crystallin, with molten globule states of bovine α-lactalbumin. J. Biol. Chem. 272:1997;27722-27729.
14. Rajaraman K., Raman B., Ramakrishna T., Rao C.M. The chaperone-like α-crystallin forms a complex only with the aggregation-prone globule state of α-lactalbumin. Biochem. Biophys. Res. Commun. 28:1998;917-921.
15. Raman B., Rao Ch.M. Chaperone-like activity and temperature-induced structural changes of α-crystallin. J. Biol. Chem. 272:1997;23559-23564.
16. Das B.K., Liang J.J.-N. Detection and characterization of α-crystallin intermediate with maximal chaperone-like activity. Biochem. Biophys. Res. Commun. 236:1997;370-374.
17. Kato K., Shinohara H., Kurobe N., Goto S., Inaguma Y., Ohshima K. Immunoreactive αA-crystallin in rat non-lenticular tissues detected with a sensitive immunoassay method. Biochim. Biophys. Acta. 1080:1991;173-180.
18. Bhat S.P., Nagineni C.N. αB subunit of lens-specific protein α-crystallin is present in other ocular and non-ocular tissues. Biochem. Biophys. Res. Commun. 158:1989;319-325.
19. Rao P.V., Huang Q., Horwitz J., Zigler J.S. Evidence that α-crystallin prevents non-specific protein aggregation in the intact eye lens. Biochim. Biophys. Acta. 1245:1995;439-447.
20. M. Ehrnsperger, J. Buchner, M. Gaestel, Structure and function of small heat shock proteins, in: A.L. Fink, Y. Goto (Eds.), Molecular Chaperones in the Life Cycle of Proteins - Structure, Function and Mode of Action, Marcel Dekker, New York, 1997, pp. 533-575.
21. Stevens A., Augusteyn R.C. Acid induced dissociation of αA- and αB-crystallin homopolymers. Biophys. J. 65:1993;1648-1655.
22. Carver J.A., Aquilina J.A., Truscott R.J. An investigation into the stability of α-crystallin by NMR spectroscopy; evidence for a two-domain structure. Biochim. Biophys. Acta. 1164:1993;22-28.
23. Sun T.-X., Liang J.J.-N. Intermolecular exchange and stabilization of recombinant human αA- and αB-crystallin. J. Biol. Chem. 273:1998;286-290.
24. Hendriks W., Weetink H., Voorter C.E., Sanders J., Bloemendal H., de Jong W.W. The alternative splicing product αAins-crystallin is structurally equivalent to αA and αB subunits in the rat α-crystallin aggregate. Biochim. Biophys. Acta. 1037:1990;58-65.
25. 2 but phosphorylation has no effect on chaperone activity. Exp. Eye Res. 61:1995;115-124.
26. van Boekel M.A.M., Hoogakker S.E.A., Harding J.J., de Jong W.W. The influence of some post-translational modifications on the chaperone-like activity of α-crystallin. Ophthalm. Res. 28:1996;32-38.
27. Horwitz J., Huang Q.-L., Ding L., Bova M.P. Lens α-crystallin: chaperone-like properties. Methods Enzymol. 290:1998;365-383.
28. Smulders R.H.P.H., Merck K.B., Aendekerk J., Horwitz J., Takemoto L., Slingsby C., Bloemendal H., de Jong W.W. The mutation Asp69→Ser affects the chaperone-like activity of αA-crystallin. Eur. J. Biochem. 232:1995;834-838.
29. Bradford M.M. A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the priciple of protein-dye binding. Anal. Biochem. 72:1976;248-254.
30. Smulders R.H.P.H., Carver J.A., Lindner R.A., van Boekel M.A.M., Bloemendal H., de Jong W.W. Immobilization of the C-terminal extension of bovine αA-crystallin reduces chaperone-like activity. J. Biol. Chem. 271:1995;29060-29066.
31. Surewicz W.K., Olesen P.R. On the thermal stability of α-crystallin a new insight from infrared spectroscopy. Biochemistry. 34:1995;9655-9660.
32. Lee J.-S., Satoh T., Shinoda H., Samejima T., Wu S.-H., Chiou S.-H. Effect of heat-induced structural perturbation of secondary and tertiary structures on the chaperone activity of α-crystallin. Biochem. Biophys. Res. Commun. 237:1997;277-282.
33. Gesierich U., Pfeil W. The conformational stability of α-crystallin is rather low: calorimetric results. FEBS Lett. 393:1996;151-154.
34. Das B.K., Liang J.J.-N., Chakrabarti B. Heat-induced conformational change and increased chaperone activity of lens α-crystallin. Curr. Eye Res. 16:1996;303-306.
35. Maiti M., Kono M., Chakrabarti B. Heat-induced changes in the conformation of α- and β-crystallins: unique thermal stability of α-crystallin. FEBS Lett. 1:1988;109-114.
36. Farnsworth P.N., Groth-Vasselli B., Greenfield N.J., Singh K. Effect of temperature and concentration on bovine lens α-crystallin secondary structure: a circular dichroism spectroscopic study. Int. J. Biol. Macromol. 20:1997;283-291.
37. Bandekar J. Amide modes and protein conformation. Biochim. Biophys. Acta. 1120:1992;123-143.
38. Das K.P., Surewicz W.K. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin. FEBS Lett. 369:1995;321-325.
39. Stevens A., Augusteyn R.C. Binding of 1-anilinonaphthalene-8-sulfonic acid to α-crystallin. Eur. J. Biochem. 243:1997;792-797.
40. Sharma H.K., Kaur H., Kumar G.S., Kester K. Interaction of 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid with α-crystallin. J. Biol. Chem. 273:1998;8965-8970.
41. Raman B., Ramakrishna T., Rao C.M. Rapid refolding studies on the chaperone-like α-crystallin. Effect of α-crystallin on refolding of β- and γ-crystallins. J. Biol. Chem. 270:1995;19888-19892.
42. Groenen P.J., Merck K.B., de Jong W.W., Bloemendal H. Structure and modifications of the junior chaperone α-crystallin. Eur. J. Biochem. 225:1994;1-19.
43. Brady J.P, Garland D., Duglas-Tabor Y., Robinson W.G. Jr., Groome A., Wawrousek E.F. Targeted disruption of the mouse αA-crystallin gene induces cataract and cytoplasmic inclusion bodies containing the small heat shock protein αB-crystallin. Proc. Natl. Acad. Sci. USA. 94:1997;884-889.