Effect of a single AGE modification on the structure and chaperone activity of human αB-crystallin

Biochemistry

Volumn 46, Issue 50, 2007, Pages 14682-14692

  Bhattacharyya, Jaya ^a   Shipova, Ekaterina V ^a   Santhoshkumar, Puttur ^a   Sharma, K Krishna ^a   Ortwerth, Beryl J ^a  

^a UNIVERSITY OF MISSOURI   (United States)

Author keywords

[No Author keywords available]

Indexed keywords

CHEMICAL MODIFICATION; FLUORESCENCE; GLYCEROL; MOLECULAR INTERACTIONS; MOLECULAR STRUCTURE; MUTAGENESIS;

ADVANCED GLYCATION END PRODUCTS (AGE); CHAPERONING ABILITY; CYSTEINE RESIDUES; SMALL HEAT SHOCK PROTEINS (SHSP);

ENZYME ACTIVITY;

ADVANCED GLYCATION END PRODUCT; ALCOHOL DEHYDROGENASE; ALPHA CRYSTALLIN; BETA CRYSTALLIN; BROMINE DERIVATIVE; CHAPERONE; CITRATE SYNTHASE; INSULIN; LYSINE; LYSINE DERIVATIVE;

ARTICLE; FLUORESCENCE; HUMAN; PRIORITY JOURNAL; PROTEIN ANALYSIS; PROTEIN BINDING; PROTEIN FUNCTION; PROTEIN MODIFICATION; PROTEIN QUATERNARY STRUCTURE; PROTEIN STRUCTURE; WILD TYPE;

ALPHA-CRYSTALLIN B CHAIN; CIRCULAR DICHROISM; CYSTEINE; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; FLUORESCENCE; GLYCOSYLATION END PRODUCTS, ADVANCED; HUMANS; LYSINE; MOLECULAR CHAPERONES; MOLECULAR STRUCTURE; PROTEIN BINDING; PYRIDINIUM COMPOUNDS; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION; SPECTROPHOTOMETRY, ULTRAVIOLET; STRUCTURE-ACTIVITY RELATIONSHIP; TANDEM MASS SPECTROMETRY; TRYPTOPHAN;

EID: 37249017462     PISSN: 00062960     EISSN: None     Source Type: Journal    
DOI: 10.1021/bi701326b     Document Type: Article

References (31)

1. Higgins, P. J., and Bunn, H. F. (1981) Kinetic analysis of the nonenzymatic glycosylation of hemoglobin, J. Biol. Chem. 256, 5204-5208.
2. Brownlee, M. (2001) Biochemistry and molecular cell biology of diabetic complications, Nature 414, 813-820.
3. Cheng, R., Lin, B., Lee, K. W., and Ortwerth, B. J. (2001) Similarity of the yellow chromophores isolated from human cataracts with those from ascorbic acid-modified calf lens proteins: evidence for ascorbic acid glycation during cataract formation, Biochim. Biophys. Acta 1537, 14-26.
4. Sugimoto, H., Shikata, K., Wada, J., Horiuchi, S., and Makino, H. (1999) Advanced glycation end products-cytokine-nitric oxide sequence pathway in the development of diabetic nephropathy: aminoguanidine ameliorates the overexpression of tumour necrosis factor-alpha and inducible nitric oxide synthase in diabetic rat glomeruli, Diabetologia 42, 878-886.
5. Chibber, R., Molinatti, P. A., Rosatto, N., Lambourne, B., and Kohner, E. M. (1997) Toxic action of advanced glycation end products on cultured retinal capillary pericytes and endothelial cells: relevance to diabetic retinopathy, Diabetologia 40, 156-164.
6. Robinson, N. E., Lampi, K. J., Speir, J. P., Kruppa, G., Easterling, M., and Robinson, A. E. (2006) Quantitative measurement of young human eye lens crystalline by direct injection fourier transform ion cyclotron resonance mass spectrometry, Mol. Vision 12, 704-711.
7. Lampi, K. J., Ma, Z., Shih, M., Shearer, T. R., Smith, J. B., Smith, D. L. and David, L. L. (1997) Sequence analysis of betaA3, betaB3, and betaA4 crystallins completes the identification of the major proteins in young human lens, J. Biol. Chem. 272, 2268-2275.
8. 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.
9. Klemenz, R., Andres, A. C., Frohli, E., Schafer, R., and Aoyama, A. (1993) Expression of the murine small heat shock proteins hsp 25 and alpha B crystallin in the absence of stress, J. Cell Biol. 210, 639-645.
10. Horwitz, J. (1992) Alpha-crystallin can function as a molecular chaperone, Proc. Natl. Acad. Sci. U.S.A. 89, 10449-10453.
11. Rao, P. V., Huang, Q.-L., Horwitz, J., and Zigler, J. S. (1995) Evidence that alpha-crystallin prevents non-specific protein aggregation in the intact eye lens, Biochim. Biophys. Acta 1245, 439-447.
12. Renkawek, K., Voorter, C. E. M., Bosman, G. J., van Workum, F. P., and de Jong, W. W. (1994) Expression of alpha B-crystallin in Alzheimer's disease, Acta Neuropathol. 87, 155-160.
13. Lowe, J., Landon, M., Pike, I., Spendlove, I., McDermott, H., and Mayer, R. J. (1990) Dementia with beta-amyloid deposition: involvement of alpha B-crystallin supports two main diseases, Lancet 336, 515-516.
14. Renkawek, K., de Jong, W. W., Merck, K. B., Frenken, C. W., van Workum, F. P., and Bosman, G. J. (1992) alpha B-crystallin is present in reactive glia in Creutzfeldt-Jakob disease, Acta Neuropathol. 83, 324-327.
15. Head, M. W., Corbin, E., and Goldman, J. E. (1993) Overexpression and abnormal modification of the stress proteins alpha B-crystallin and HSP27 in Alexander disease, Am. J. Pathol. 143, 1743-1753.
16. Argirov, O. K., Lin, B., and Ortwerth, B. J. (2004) 2-Ammonio-6-(3- oxidopyridinium-1-yl)hexanoate (OP-lysine) is a newly identified advanced glycation end product in cataractous and aged human lenses, J. Biol. Chem. 279, 6487-6495.
17. Santhoshkumar, P., and Sharma, K. K. (2006) Conserved F84 and P86 residues in αB-crystallin are essential to effectively prevent the aggregation of substrate proteins, Protein Sci. 15, 2488-2498.
18. Ortwerth, B. J., Slight, S. H., Prabhakaram, M., Sun, Y., and Smith, J. B. (1992) Site-specific glycation of lens crystallins by ascorbic acid, Biochim. Biophys. Acta 117, 207-215.
19. Baynes, J. W., Watkins, N. G., Fisher, C. I., Hull, C. J., Patrick, J. S., Ahmed, M. U., Dunn, J. A., and Thorpe, S. R. (1989) The Amadori product on protein: structure and reactions, Prog. Clin. Biol. Res. 304, 43-67.
20. Sakai, H. (2005) Mutagenesis of the active site lysine 221 of the pyruvate kinase from Bacillus stearothermophilus, J. Biochem. 137, 141-145.
21. Horwitz, J., Huang, Q. L., Ding, L., and Bova, M. P. (1998) Lens alpha-crystallin: chaperone-like properties, Methods Enzymol. 290, 365-383.
22. Bhattacharyya, J., Padmanabha Udupa, E. G., Wang, J., and Sharma, K. K. (2006) Mini-alphaB-crystallin: a functional element of alphaB-crystallin with chaperone-like activity, Biochemistry 45, 3069-3076.
23. Nagaraj, R. H., Oya-Ito, T., Padayatti, P. S., Kumar, R., Mehta, S., West, K., Levison, B., Sun, J., Crabb, J. W., and Padival, A. K. (2003) Enhancement of chaperone function of alpha-crystallin by methylglyoxal modification, Biochemistry 42, 10746-10755.
24. Derham, B. K., and Harding, J. J. (2002) Effects of modifications of alpha-crystallin on its chaperone and other properties, Biochem. J. 364, 711-717.
25. 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.
26. Cheng, R., Lin, B., and Ortwerth, B. J. (2003) Separation of the yellow chromophores in individual brunescent cataracts, Exp. Eye Res. 77, 313-325.
27. Kimchi-Sarfaty, C., Oh, J. M., Kim, I. W., Sauna, Z. E., Calcagno, A. M., Ambudkar, S. V., and Gottesman, M. M. (2007) A "silent" polymorphism in the MDR1 gene changes substrate specificity, Science 315, 525-528.
28. Bhattacharyya, J., Bhattacharyya, M., Chakrabarty, A. S., Chaudhuri, U., and Poddar, R. K. (1994) Interaction of chlorpromazine with myoglobin and hemoglobin. A comparative study, Biochem. Pharmacol. 47, 2049-2053.
29. Ghosh, J. G., and Clark, J. I. (2005) Insights into the domains required for dimerization and assembly of human αB-crystallin, Protein Sci. 14, 684-695.
30. 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.
31. Cheng, R., Feng, Q., and Ortwerth, B. J. (2006) LC-MS display of the total modified amino acids in cataract lens proteins and in lens proteins glycated by ascorbic acid in vitro, Biochim. Biophys. Acta 1762, 533-543.