Correlation between the loss of the chaperone-like activity and the oxidation, isomerization and racemization of gamma-irradiated alpha-crystallin

Photochemistry and Photobiology

Volumn 74, Issue 3, 2001, Pages 477-482

  Fujii, N ^a   Hiroki, K ^a   Matsumoto, S ^a   Masuda, K ^b   Inoue, M ^c   Tanaka, Y ^c   Awakura, M ^a   Akaboshi, M ^a  

^a KYOTO UNIVERSITY   (Japan)

^b SUNTORY INSTITUTE FOR BIOORGANIC RESEARCH   (Japan)

^c Osaka Prefecture University   (Japan)

Author keywords

[No Author keywords available]

Indexed keywords

ALPHA CRYSTALLIN; AMINO ACID; ASPARTIC ACID; CHAPERONE; METHIONINE SULFOXIDE; PEPTIDE; TRYPSIN;

AMINO ACID ANALYSIS; ARTICLE; CHEMICAL STRUCTURE; CIRCULAR DICHROISM; CROSS LINKING; GAMMA IRRADIATION; HIGH PERFORMANCE LIQUID CHROMATOGRAPHY; IRRADIATION; ISOMERISM; OXIDATION; POLYACRYLAMIDE GEL ELECTROPHORESIS; PROTEIN ANALYSIS; RADIATION DOSE; SEQUENCE ANALYSIS; STRUCTURE ANALYSIS;

ANIMALS; ASPARTIC ACID; CATTLE; CRYSTALLINS; GAMMA RAYS; ISOMERISM; MOLECULAR CHAPERONES; OXIDATION-REDUCTION; PHOTOCHEMISTRY; PROTEIN STRUCTURE, SECONDARY; PROTEIN STRUCTURE, TERTIARY; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; STEREOISOMERISM;

EID: 0035470642     PISSN: 00318655     EISSN: None     Source Type: Journal    
DOI: 10.1562/0031-8655(2001)074<0477:CBTLOT>2.0.CO;2     Document Type: Article

References (33)

1. de Jong, W. W., E. C. Terwindt and H. Bloemendal (1975) The amino acid sequences of the A chain of human a-crystallin. FEBS Lett. 58, 310-313.
2. Dubin, R. A., A. H. Ally, S. Chung and J. Piatigorskym (1990) Alpha B-crystallin gene and preferential promoter function in lens. Genomics 7, 594-601.
3. Klemenz, R., E. Frohli, R. H. Steiger, R. Schafer and A. Aoyama (1991) Alpha B-crystallin is a small heat shock protein. Proc. Natl. Acad. Sci. USA 88, 3652-3656.
4. Horwitz, J. (1992) Alpha-crystallin can function as a molecular chaperone. Proc. Natl. Acad. Sci. USA 89, 10 449-10 453.
5. Boyle, D. and L. Takemoto (1994) Characterization of the alpha-gamma and alpha-beta complex: evidence for an in vivo functional role of alpha-crystallin as a molecular chaperone. Exp. Eye Res. 58, 9-16.
6. Raman, B. and C. M. Rao (1994) Chaperone-like activity and quaternary structure of alpha-crystallin. J. Biol. Chem. 269, 27 264-27 268.
7. Das, K. P. and W. K. Surewicz (1995) Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of alpha-crystallin. FEBS Lett. 369, 321-325.
8. Lee, J.-S., T. Samejima, J.-H. Liao, S.-H. Wu and S.H. Chiou (1998) Physiological role of the association complexes of alpha-crystallin and its substrates on the chaperone activity. Biophys. Biochem. Res. Commun. 244, 379-383.
9. Voorter, C. E. M., W. A. de Haard-Hoekman, P. J. M. van den Otelaar, H. Bloemendal and W. W. deJong (1988) Spontaneous peptide bond cleavage in aging alpha-crystallin through a succinimide intermediate. J. Biol. Chem. 263, 19 020-19 023.
10. Miesbauer, L. R., X. Zhou, Z. Yang, Z. Yang, Y. Sun, D. L. Smith and J. B. Smith (1994) Post-translational modifications of water-soluble human lens crystallins from young adults. J. Biol. Chem. 269, 12 494-12 502.
11. Masters, P. M., J. L. Bada and J. S. Zigler Jr. (1977) Aspartic acid racemization in the human lens during aging and in cataract formation. Nature 268, 71-73.
12. Masters, P. M., J. L. Bada and J. S. Zigler Jr. (1978) Aspartic acid racemization in heavy molecular weight crystallins and water insoluble protein from human lenses and cataracts. Proc. Natl. Acad. Sci. USA 75, 1204-1208.
13. Groenen, P. J. T. A., P. R. L. A. van den Ijssel, C. E. M. Voorter, H. Bloemendal and W. W. de Jong (1990) Site-specific racemization in aging alpha A-crystallin. FEBS Lett. 269, 109-112.
14. Fujii, N., Y. Ishibashi, K. Satoh, M. Fujino and K. Harada (1994) Simultaneous racemization and isomerization at specific aspartic acid residues in alpha B-crystallin from aged human lens. Biochim. Biophys. Acta 1204, 157-163.
15. Fujii, N., K. Satoh, K. Harada and Y. Ishibashi (1994) Simultaneous stereoinversion and isomerization at specific aspartic acid residues in alpha A-crystallin from aged human lens. J. Biochem. 116, 663-669.
16. Fujii, N., Y. Momose, Y. Yamagaki, T. Uemura, M. Takita, H. Nakanishi and N. Ishii (1997) The conformation formed by the domain after alanine-155 induces inversion of aspartic acid-151 in alpha A-crystallin from aged human lenses. Biophys. Biochem. Res. Commun. 239, 918-923.
17. Fujii, N., K. Harada, Y. Momose, N. Ishii and M. Akaboshi (1999) D- and beta-amino acid formation induced by a chiral field within a human lens protein during aging. Biophys. Biochem. Res. Commun. 263, 322-326.
18. Fujii, N., L. J. Takemoto, Y. Momose, S. Matsumoto, K. Hiroki and M. Akaboshi (1999) Formation of four isomers at Asp-151 residue of aged human alpha A-crystallin by natural aging. Biochem. Biophys. Res. Commun. 265, 746-751.
19. Emmons, T. and L. Takemoto (1992) Age-dependent loss of the C-terminal amino acid from alpha-crystallin. Exp. Eye Res. 55, 551-554.
20. Takemoto, L. (1991) Truncation of alpha A-crystallin from the human lens. Exp. Eye Res. 53, 811-813.
21. Kamei, A., H. Iwase and K. Masuda (1997) Cleavage of amino acid residues from the alpha A- and alpha B-crystallin in human crystallin lens during aging. Biochem. Biophys. Res. Commun. 231, 373-378.
22. Takemoto, L. (1996) Differential phosphorylation of alpha A-crystallin in human lens of different age. Exp. Eye Res. 62, 499-504.
23. Takemoto, L., J. Horwitz and T. Emmons (1992) Oxidation of the N-terminal methionine of lens alpha-A crystallin. Curr. Eye Res. 11, 651-655.
24. Finley, E. L., J. Dillon, R. K. Crouch and K. L. Schey (1998) Identification of tryptophan oxidation products in bovine alpha-crystallin. Protein Sci. 7, 2391-2397.
25. Finley, E. L., J. Dillon, R. K. Crouch and K. L. Schey (1998) Radiolysis-induced oxidation of bovine alpha-crystallin. Photochem. Photobiol. 68, 9-15.
26. Takemoto, L. (1996) Increase in the intramolecular disulfide bonding of alpha-A crystallin during aging of the human lens. Exp. Eye Res. 63, 585-590.
27. Cherian, M. and E. C. Abraham (1995) Decreased molecular chaperone property of alpha-crystallins due to posttranslational modifications. Biochem. Biophys. Res. Commun. 208, 675-679.
28. Laemmli, U. K. (1970) Cleavage of structural proteins during the assembly of the head of bacteriophage T4. Nature 227, 680-685.
29. Momose, Y., N. Fujii, T. Kodama, T. Yamagaki, H. Nakanishi and M. Kodama (1999) The effect of X-ray irradiation on alpha A-crystallin: the high molecular protein and modified alpha A-crystallin increase in lens by X-ray irradiation. Viva Origino 27, 119-131.
30. Fujii, N., L. J. Takemoto, S. Matsumoto, K. Hiroki, D. Boyle and M. Akaboshi (2000) The comparison of D-aspartic acid contents in alpha A-crystallin from normal and age-matched cataractous human lenses. Biochem. Biophys. Res. Commun. 278, 408-413.
31. Geiger, T. and S. J. Clarke (1987) Deamidation, isomerization and racemization at asparaginyl and aspartyl residues in peptides. Succinimide-linked reactions that contribute to protein degradation. J. Biol. Chem. 262, 785-794.
32. Stephenson, R. C. and S. Clarke (1989) Succinimide formation from aspartyl and asparginyl peptides as a model for the spontaneous degradation of proteins. J. Biol. Chem. 264, 6164-6170.
33. Tyler-Cross, R. and V. Schirch (1991) Effects of amino acid ssequence, buffers, and ionic strength on the rate and mechanism of deamidation of asparagine residues in small peptides. J. Biol. Chem. 266, 22 549-22 556.