Importance of eye lens α-crystallin heteropolymer with 3:1 αA to αB ratio: Stability, aggregation, and modifications

IUBMB Life

Volumn 62, Issue 9, 2010, Pages 693-702

  Srinivas, Pasumarthi ^a   Narahari, Akkaladevi ^b   Petrash, J Mark ^c   Swamy, Musti J ^b   Reddy, Geereddy Bhanuprakash ^a  

^a NATIONAL INSTITUTE OF NUTRITION   (India)

^b UNIVERSITY OF HYDERABAD   (India)

^c UNIVERSITY OF COLORADO SCHOOL OF MEDICINE   (United States)

Author keywords

crystallin; 3:1 ratio; Aggregation; Differential scanning calorimetry; Heteropolymer; Stability; Unfolding

Indexed keywords

ALPHA CRYSTALLIN; MUTANT PROTEIN; POLYMER; PROTEIN SUBUNIT;

ARTICLE; DIFFERENTIAL SCANNING CALORIMETRY; GEL PERMEATION CHROMATOGRAPHY; GLYCATION; LENS; PROTEIN AGGREGATION; PROTEIN FOLDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN STABILITY; PROTEIN STRUCTURE; RNA TRANSLATION; TEMPERATURE; VERTEBRATE;

ALPHA-CRYSTALLIN A CHAIN; ALPHA-CRYSTALLIN B CHAIN; ANIMALS; CALORIMETRY, DIFFERENTIAL SCANNING; GOATS; POLYMERIZATION; PROTEIN FOLDING; PROTEIN STABILITY;

VERTEBRATA;

EID: 78649747482     PISSN: 15216543     EISSN: 15216551     Source Type: Journal    
DOI: 10.1002/iub.373     Document Type: Article

References (45)

1. Groenen, P. J., Merck, K. B., de Jong, W. W., and Bloemendal, H. (1994) Structure and modifications of the junior chaperone alpha-crystallin. From lens transparency to molecular pathology. Eur. J. Biochem. 225, 1-19.
2. Bloemendal, H., de Jong, W., Jaenicke, R., Lubsen, N. H., Slingsby, C., and Tardieu, A. (2004) Ageing and vision: Structure, stability and function of lens crystallins. Prog. Biophys. Mol. Biol. 86, 407-485.
3. Harding, J. J. (1991) Cataract: Biochemistry, Epidemiology and Pharmacology. Chapman and Hall, London.
4. Horwitz, J. (2003) Alpha-crystallin. Exp. Eye Res. 76, 145-153.
5. Reddy, G. B., Kumar, P. A., and Kumar, M. S. (2006) Chaperone-like activity and hydrophobicity of alpha-crystallin. IUBMB Life 58, 632-641.
6. Horwitz, J. (1992) Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA 89, 10449-10453.
7. Merck, K. B., Groenen, P. J., Voorter, C. E., de Haard-Hoekman, W. A., Horwitz, J., Bloemendal, H., and de Jong, W. W. (1993) Structural and functional similarities of bovine alpha-crystallin and mouse small heat-shock protein. A family of chaperones. J. Biol. Chem. 268, 1046-1052.
8. Reddy, G. B., Das, K. P., Petrash, J. M., and Surewicz, W. K. (2000) Temperature-dependent chaperone activity and structural properties of human alphaA- and alphaB-crystallins. J. Biol. Chem. 275, 4565-4570.
9. Das, K. P. and Surewicz, W. K. (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 369, 321-325.
10. Lindner, R. A., Treweek, T. M., and Carver, J. A. (2001) The molecular chaperone alpha-crystallin is in kinetic competition with aggregation to stabilize a monomeric molten-globule form of alpha-lactalbumin. Biochem. J. 354, 79-87.
11. Raman, B., Ramakrishna, T., and Rao, C. M. (1995) Temperature dependent chaperone-like activity of alpha-crystallin. FEBS Lett. 365, 133-136.
12. Thomson, J. A. and Augusteyn, R. C. (1989) On the structure of alphacrystallin: Construction of hybrid molecules and homopolymers. Biochim. Biophys. Acta 994, 246-252.
13. van den Oetelaar, P. J., van Someren, P. F., Thomson, J. A., Siezen, R. J., and Hoenders, H. J. (1990) A dynamic quaternary structure of bovine alpha-crystallin as indicated from intermolecular exchange of subunits. Biochemistry 29, 3488-3493.
14. Sun, T. X. and Liang, J. J. (1998) Intermolecular exchange and stabilization of recombinant human alphaA- and alphaB-crystallin. J. Biol. Chem. 273, 286-290.
15. Srinivas, P. N., Reddy, P. Y., and Reddy, G. B. (2008) Significance of alpha-crystallin heteropolymer with a 3:1 alphaA/alphaB ratio: Chaperone- like activity, structure and hydrophobicity. Biochem. J. 414, 453-460.
16. Bhat, S. P. (2003) Crystallins, genes and cataract. Prog. Drug Res. 60, 205-262.
17. Iwaki, T., Kume-Iwaki, A., Liem, R. K., and Goldman, J. E. (1989) Alpha B-crystallin is expressed in non-lenticular tissues and accumulates in Alexander's disease brain. Cell 57, 71-78.
18. Kumar, P. A., Haseeb, A., Suryanarayana, P., Ehtesham, N. Z., and Reddy, G. B. (2005) Elevated expression of alphaA- and alphaB-crystallins in streptozotocin-induced diabetic rat. Arch. Biochem. Biophys. 444, 77-83.
19. Vicart, P., Caron, A., Guicheney, P., Li, Z., Prevost, M. C., Faure, A., Chateau, D., Chapon, F., Tome, F., Dupret, J. M., Paulin, D., and Fardeau, M. (1998) A missense mutation in the alphaB-crystallin chaperone gene causes a desmin-related myopathy. Nat. Genet. 20, 92-95.
20. Kumar, P. A. and Reddy, G. B. (2009) Modulation of alpha-crystallin chaperone activity: A target to prevent or delay cataract? IUBMB Life 61, 485-495.
21. Bhagyalaxmi, S. G., Srinivas, P., Barton, K. A., Kumar, K. R., Vidyavathi, M., Petrash, J. M., Bhanuprakash Reddy, G., and Padma, T. (2009) A novel mutation (F71L) in alphaA-crystallin with defective chaperonlike function associated with age-related cataract. Biochim. Biophys. Acta 1792, 974-981.
22. Horwitz, J., Bova, M. P., Ding, L. L., Haley, D. A., and Stewart, P. L. (1999) Lens alpha-crystallin: Function and structure. Eye (Lond). 13, 403-408.
23. de Jong, W. W., Lubsen, N. H., and Kraft, H. J. (1994) Molecular evolution of the eye lens. Prog. Retinal Eye Res. 13, 391-442.
24. Yu, C. M., Chang, G. G., Chang, H. C., and Chiou, S. H. (2004) Cloning and characterization of a thermostable catfish alphaB-crystallin with chaperone-like activity at high temperatures. Exp. Eye Res. 79, 249-261.
25. den Engelsman, J., Boros, S., Dankers, P. Y., Kamps, B., Vree Egberts, W. T., Bode, C. S., Lane, L. A., Aquilina, J. A., Benesch, J. L., Robinson, C. V., de Jong, W. W., and Boelens, W. C. (2009) The small heatshock proteins HSPB2 and HSPB3 form well-defined heterooligomers in a unique 3 to 1 subunit ratio. J. Mol. Biol. 393, 1022-1032.
26. Sun, T. X., Akhtar, N. J., and Liang, J. J. (1999) Thermodynamic stability of human lens recombinant alphaA- and alphaB-crystallins. J. Biol. Chem. 274, 34067-34071.
27. Datta, S. A. and Rao, C. M. (1999) Differential temperature-dependent chaperone-like activity of alphaA- and alphaB-crystallin homoaggregates. J. Biol. Chem. 274, 34773-34778.
28. Liang, J. J., Sun, T. X., and Akhtar, N. J. (2000) Heat-induced conformational change of human lens recombinant alphaA- and alphaB-crystallins. Mol. Vis. 6, 10-14.
29. Satish Kumar, M., Mrudula, T., Mitra, N., and Bhanuprakash Reddy, G. (2004) Enhanced degradation and decreased stability of eye lens alphacrystallin upon methylglyoxal modification. Exp. Eye Res. 79, 577-583.
30. Kumar, M. S., Reddy, P. Y., Kumar, P. A., Surolia, I., and Reddy, G. B. (2004) Effect of dicarbonyl-induced browning on alpha-crystallin chaperone-like activity: Physiological significance and caveats of in vitro aggregation assays. Biochem. J. 379, 273-282.
31. Kumar, M. S., Reddy, P. Y., Sreedhar, B., and Reddy, G. B. (2005) Alphab-crystallin-assisted reactivation of glucose-6-phosphate dehydrogenase upon refolding. Biochem. J. 391, 335-341.
32. Gesierich, U. and Pfeil, W. (1996) The conformational stability of alphacrystallin is rather low: Calorimetric results. FEBS Lett. 393, 151-154.
33. Steadman, B. L., Trautman, P. A., Lawson, E. Q., Raymond, M. J., Mood, D. A., Thomson, J. A., and Middaugh, C. R. (1989) A differential scanning calorimetric study of the bovine lens crystallins. Biochemistry 28, 9653-9658.
34. Surewicz, W. K. and Olesen, P. R. (1995) On the thermal stability of alpha-crystallin: A new insight from infrared spectroscopy. Biochemistry 34, 9655-9660.
35. Das, B. K. and Liang, J. J. (1997) Detection and characterization of alpha-crystallin intermediate with maximal chaperone-like activity. Biochem. Biophys. Res. Commun. 236, 370-374.
36. Saha, S. and Das, K. P. (2007) Unfolding and refolding of bovine alpha-crystallin in urea and its chaperone activity. Protein J. 26, 315-326.
37. van den Oetelaar, P. J. and Hoenders, H. J. (1989) Folding-unfolding and aggregation-dissociation of bovine alpha-crystallin subunits; evidence for unfolding intermediates of the alpha A subunits. Biochim. Biophys. Acta 995, 91-96.
38. Datta, P., Kallur, L., and Abraham, E. C. (2008) Reversal of chaperone activity loss of glycated alphaA-crystallin by a crosslink breaker. Mol. Cell. Biochem. 315, 137-142.
39. Kumar, P. A., Kumar, M. S., and Reddy, G. B. (2007) Effect of glycation on alpha-crystallin structure and chaperone-like function. Biochem. J. 408, 251-258.
40. Brady, J. P., Garland, D. L., Green, D. E., Tamm, E. R., Giblin, F. J., and Wawrousek, E. F. (2001) AlphaB-crystallin in lens development and muscle integrity: A gene knockout approach. Invest. Ophthalmol. Vis. Sci. 42, 2924-2934.
41. Brady, J. P., Garland, D., Duglas-Tabor, Y., Robison, W. G. Jr., Groome, A., and Wawrousek, E. F. (1997) Targeted disruption of the mouse alpha A-crystallin gene induces cataract and cytoplasmic inclu-sion bodies containing the small heat shock protein alpha B-crystallin. Proc. Natl. Acad. Sci. USA 94, 884-889.
42. Boyle, D. L., Takemoto, L., Brady, J. P., and Wawrousek, E. F. (2003) Morphological characterization of the Alpha A- and Alpha B-crystallin double knockout mouse lens. BMC Ophthalmol. 3, 3.
43. Andley, U. P., Song, Z., Wawrousek, E. F., Fleming, T. P., and Bassnett, S. (2000) Differential protective activity of alpha A- and alphaBcrystallin in lens epithelial cells. J. Biol. Chem. 275, 36823-36831.
44. Andley, U. P., Song, Z., Wawrousek, E. F., and Bassnett, S. (1998) The molecular chaperone alphaA-crystallin enhances lens epithelial cell growth and resistance to UVA stress. J. Biol. Chem. 273, 31252-31261.
45. Kumar, M. S., Kapoor, M., Sinha, S., and Reddy, G. B. (2005) Insights into hydrophobicity and the chaperone-like function of alphaA- and alphaB-crystallins: An isothermal titration calorimetric study. J. Biol. Chem. 280, 21726-21730.