Alpha-crystallin: An ATP-independent complete molecular chaperone toward sorbitol dehydrogenase

Cellular and Molecular Life Sciences

Volumn 62, Issue 5, 2005, Pages 599-605

  Marini, I ^a   Moschini, R ^a   Del Corso, A ^a   Mura, U ^a  

^a UNIVERSITY OF PISA   (Italy)

Author keywords

Crystallin; Enzyme renaturation; Molecular chaperone; Protein refolding; Small heat shock protein; Sorbitol dehydrogenase

Indexed keywords

ADENOSINE TRIPHOSPHATE; ALPHA CRYSTALLIN; CHAPERONE; IDITOL DEHYDROGENASE; REDUCED NICOTINAMIDE ADENINE DINUCLEOTIDE;

ANIMAL TISSUE; ARTICLE; CATTLE; CONTROLLED STUDY; ENZYME ACTIVATION; ENZYME ACTIVITY; ENZYME DENATURATION; ENZYME INACTIVATION; ENZYME RENATURATION; LENS; MOLECULAR BIOLOGY; NONHUMAN; PROTEIN AGGREGATION; PROTEIN DENATURATION; PROTEIN HYDROLYSIS; PROTEIN INTERACTION; PROTEIN RENATURATION; THERMODYNAMICS;

ADENOSINE TRIPHOSPHATE; ALPHA-CRYSTALLINS; ANIMALS; CATTLE; ENZYME ACTIVATION; GUANIDINE; L-IDITOL 2-DEHYDROGENASE; NAD; PROTEIN DENATURATION; PROTEIN FOLDING;

EID: 15344341428     PISSN: 1420682X     EISSN: None     Source Type: Journal    
DOI: 10.1007/s00018-005-4474-z     Document Type: Article

References (45)

1. Harding J. J. (1997) Lens. In Biochemistry of the Eye, pp. 104-112, Harding J. E. (ed.) Chapman & Hall Medical, London
2. Iwaki T., Kume-Iwaki A. and Goldman J. E. (1990) Cellular distribution of αB-crystallin in non-lenticular tissues. J. Histochem. Cytochem. 38: 31-39
3. Srinivasan A. N., Nagineni C. N. and Bhat S. P. (1992) Alpha A-crystallin is expressed in non-ocular tissues. J. Biol. Chem. 267: 23337-23341
4. Head M. W., Corbin E. and Goldmann J. E. (1994) Coordinate and independent regulation of αB-crystallin and Hsp27 expression in response to physiological stress. J. Cell Physiol. 159: 41-50
5. Head M. W., Hurwitz L. and Goldman J. E. (1996) Transcriptional regulation of αB-crystallin in astrocytes: analysis of HSF and AP1 activation by different types of physiological stress. J. Cell. Sci. 109: 1029-1039
6. Iwaki T., Wisniewski T., Iwaki A. Corbin E., Tomokane N., Tateishi J. et al. (1992) Accumulation of αB-crystallin in central nervous system glia and neurons in pathologic conditions. Am. J. Pathol. 140: 345-356
7. Hitotsumatsu T., Iwaki T., Fukui M. and Tateishi J. (1996) Distintive immunohistochemical profiles of small heat shock proteins (hsp27 and alpha B-crystallin) in human brain tumors. Cancer 77: 352-361
8. Van Noort J. M. (1996) Multiple sclerosis: an altered immune response or an altered stress response. J. Mol. Med. 74: 285-296
9. Renkawek K., Stege G. J. and Bosnian G. J. (1999) Dementia, gliosis and expression of the small heat shock proteins hsp27 and αB-crystallin in Parkinson's disease. Neuroreport 10: 2273-2276
10. Clark J. I. and Muchowski P. J. (2000) Small heat-shock proteins and their potential role in human disease. Curr. Opin. Struct. Biol. 10: 52-59
11. Mehlen P., Schulze-Osthoff K. and Arrigo A. P. (1996) Small stress proteins as novel regulators of apoptosis. J. Biol. Chem. 271: 16510-16514
12. Kamradt M. C., Chen F., Sam S. and Crynst V. L. (2002) The small heat shock protein αB-crystallin negatively regulates apoptosis during myogenic differentiation by inhibiting caspase-3 activation. J. Biol. Chem. 277: 38731-38736
13. 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 inclusion bodies containing the small heat shock protein alpha B-crystallin. Proc. Natl. Acad. Sci. USA. 94: 884-889
14. Bova M. P., Yaron O., Huang Q., Ding L., Haley D. A., Stewart P. L. et al. (1999) Mutation R120G in αB-crystallin, which is linked to a desmin-related myopathy, results in an irregular structure and defective chaperone-like function. Proc. Natl. Acad. Sci. USA 96: 6137-6142
15. Andley U. P., Song Z., Wawrousek E. F., Brady J. P., Bassnett S. and Fleming T. P. (2001) Lens epithelial cells derived from alphaB-crystallin knockout mice demonstrate hyperproliferation and genomic instability. FASEB J. 15: 221-229
16. Bai F., Xi J. H., Wawrousek E. F., Fleming T. P. and Andley U. P. (2003) Hyperproliferation and p53 status of lens epithelial cells derived from alphaB-crystallin knockout mice. J. Biol. Chem. 278: 36876-36886
17. Horwitz J. (1992) α-Crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA 89: 10449-10453
18. Marini I., Bucchioni L., Voltarelli M., Del Corso A. and Mura U. (1995) Alpha-crystallin-like molecular chaperone against the thermal denaturation of lens aldose reductase: the effect of divalent metal ions. Biochem. Biophys. Res. Commun. 212: 413-420
19. Hess, J. F. and Fitzgerald P. G. (1998) Protection of a restriction enzyme from heat inactivation by α-crystallin. Mol. Vis 4: 29-32
20. Hook D. W. A. and Harding J. J. (1998) Protection of enzymes by α-crystallin acting as a molecular chaperone. Int. J. Biol. Macromol. 22: 295-306
21. Marini I., Moschini R., Del Corso A. and Mura U. (2000) Complete protection by α-crystallin on lens sorbitol dehydrogenase undergoing thermal stress. J. Biol. Chem. 275: 32559-32565
22. Ganea E. and Harding J. J. (2000) α-Crystallin assists the renaturation of glyceraldehyde-3-phosphate dehydrogenase. Biochem. J. 345: 467-472
23. Rawat U. and Rao M. (1998) Interactions of chaperone α-crystallin with the molten globule state of xylose reductase. J. Biol. Chem. 273: 9415-9423
24. Nath D., Rawat U., Anish R. and Rao M. (2002) α-Crystallin and ATP facilitate the in vitro renaturation of xylanase: enhancement of refolding by metal ions. Prot. Sci. 11: 2727-2734
25. Plater M. L, Goode D. and Crabbe M. J. (1996) Effects of site-directed mutations on the chaperone-like activity of alphaB-crystallin. J. Biol. Chem. 271: 28558-28566
26. Aquilina J. A., Benesch J. L. P., Ding L. L., Yaron O., Horwitz J. and Robinson C. V. (2004) Phosphorylation of αB-crystallin alters chaperone function through loss of dimeric substructure. J. Biol. Chem. 297: 29675-28680
27. Koteiche H. A. and Mchaourab H. S. (2003) Mechanism of chaperone function in small heat-shock proteins: phosphorylation-induced activation of two-mode binding in alphaB-crystallin. J. Biol. Chem. 278: 10361-10367
28. Ito H., Okamoto K., Nakayama H., Isobe T. and Kato, K. (1997) Phosphorylation of αB-crystallin in response to various types of stress. J. Biol. Chem. 272: 29934-29941
29. Wang K. and Spector A. (1996) α-Crystallin stabilizes actin filaments and prevents cytocalasin-induced depolymerization in a phosphorylation-dependent manner. Eur. J. Biochem. 242: 56-66
30. Horwitz J. (2003) Alpha-crystallin. Exp. Eye Res. 76: 145-153
31. Muchowski P. J., Hays L. G., Yates J. R. and Clark J. I. (1999) ATP and the core 'α-crystallin' domain of the small heat shock protein human αB-crystallin. J. Biol. Chem. 274: 30190-30195
32. Palmisano D. V., Groth-Vasselli B., Farnsworth P. N. and Reddy M. C. (1995) Interaction of ATP and lens Alpha-cry stallin characterized by equilibrium binding studies and intrinsic tryptophan fluorescence spectroscopy. Biochim. Biophys. Acta 1246: 91-97
33. 31P NMR studies of the ATP/α-crystallin complex: functional implication. Biochem. Biophys. Res. Commun. 189: 1578-1584
34. Kasan A., Smith D. L. and Smith J. B. (2002) Alpha-crystallin regions affected by adenosine 5′-triphosphate identified by hydrogen-deuterium exchange. Biochemistry 41: 15876-15882
35. Muchowski P. J. and Clark J. I. (1998) ATP-enhanced chaperone functions of the small heat shock protein human αB-crystallin. Proc. Natl. Acad. Sci. USA 95: 1004-1009
36. Smykal P., Masin J., Konopasek I. and Zarsky V. (2000) Chaperone activity of tobacco hsp18, a small heat shock protein, is inhibited by ATP. Plant J. 23: 703-713
37. Jakob U., Gaestel M., Engel K. and Buchner J. (1993) Small heat shock proteins are molecular chaperones. J. Biol. Chem. 268: 1517-1520
38. Del Fierro D., Zardeneta G. and Mendoza J. A. (2000) α-Crystallin facilitates the reactivation of hydrogen peroxide-inactivated rhodanese. Biochim. Biophys. Res. Commun. 274: 461-466
39. Biswas A. and Das, K.P. (2004) Role of ATP on the interaction of α-crystallin with its substrates and its implications for the molecular chaperone function. J. Biol. Chem. 279: 42648-42657
40. Wang K. and Spector A. (2000) α-Crystallin prevents irreversible protein denaturation and acts cooperatively with other heat-shock proteins to renature the stabilized partially denatured protein in an ATP-dependent manner. Eur. J. Biochem. 267: 4705-4712
41. Wang K. and Spector A. (2001) ATP causes small heat shock proteins to release denatured protein. Eur. J. Biochem. 268: 6335-6345
42. Marini I., Bucchioni L., Borella P., Del Corso A. and Mura U. (1997) Sorbitol dehydrogenase from bovine lens: purification and properties. Arch. Biochem. Biophys. 340: 383-391
43. Bradford M. M. (1976) A rapid and sensitive method for the quantitation of microgram quantities of protein utilizing the principle of protein-dye binding. Anal. Biochem. 72: 248-254
44. Laemmli U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227: 680-685
45. Wray W., Boulikas T., Wray V. P. and Hancock R. (1981) Silver staining of proteins in polyacrylamide gels. Anal. Biochem. 118: 197-203