Conformational study of Nε-(carboxymethyl)lysine adducts of recombinant α-crystallins

Current Eye Research

Volumn 18, Issue 4, 1999, Pages 270-276

  Akhtar, Nila J ^a   Sun, Tian Xiao ^a   Liang, Jack J N ^a,b  

^a BRIGHAM AND WOMEN S HOSPITAL   (United States)

^b Center for Ophthalmic Research   (United States)

Author keywords

Advanced glycation end products; Chaperone like activity; Conformational change; Glycation; N (carboxymethyl)lysine; Recombinant crystallin

Indexed keywords

ADVANCED GLYCATION END PRODUCT; ALPHA CRYSTALLIN; CHAPERONE; GLYOXYLIC ACID; INSULIN; LENS PROTEIN; LYSINE;

ARTICLE; CIRCULAR DICHROISM; CONFORMATIONAL TRANSITION; FLUORESCENCE; GEL PERMEATION CHROMATOGRAPHY; HUMAN; HUMAN CELL; LENS EPITHELIUM; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL;

CHROMATOGRAPHY, GEL; CIRCULAR DICHROISM; CRYSTALLINS; ELECTROPHORESIS, GEL, TWO-DIMENSIONAL; FLUORESCENCE; HUMANS; LYSINE; MOLECULAR CHAPERONES; MOLECULAR CONFORMATION; RECOMBINANT PROTEINS;

EID: 0032911347     PISSN: 02713683     EISSN: None     Source Type: Journal    
DOI: 10.1076/ceyr.18.4.270.5364     Document Type: Article

References (45)

1. Monnier VM, Cerami A. Nonenzymatic browning in vivo: possible process for aging of long-lived proteins. Science 1981;211:491-493.
2. Liang JN, Rossi MT. In vitro non-enzymatic glycation and formation of browning products in the bovine lens α-crystallin. Exp Eye Res. 1990;50:367-371.
3. Nagaraj RH, Monnier VM. Isolation and characterization of a blue fluorophore from human eye lens crystallins: in vitro formation from Maillard reaction with ascorbate and ribose. Biochim Biophys Acta 1992;1116: 34-42.
4. Prabhakaram M, Ortwerth BJ. The glycation and crosslinking of isolated lens crystalline by ascorbic acid. Exp Eye Res. 1992;55:451-459.
5. Cohen MP. Diabetes and protein glycation. Philadelphia, PA: JC Press. 1996:5-31.
6. Lyons TJ, Silvestri G, Dunn JA, Dyer DG, Baynes JW. Role of glycation in modification of lens crystalline in diabetic and non-diabetic senile cataracts. Diabetes 1991;40:1010-1015.
7. Nagaraj RH, Sell DR, Prabhakaram M, Ortwerth BJ, Monnier VM. High correlation between pentosidine protein crosslinks and pigmentation implicates ascorbate oxidation in human lens senescence and cataractogenesis. Proc Natl Acad Sci USA. 1991;88: 10257-10261.
8. ε-(carboxymethyl) lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins. Biochemistry 1995;34:10872-10878.
9. ε-(carboxymethyl)lysine protein adduct is a major immunological epitope in proteins modified with advanced glycation end products of the Maillard reaction. Biochemistry 1996;35:8075-8083.
10. Stevens VJ, Rouzer CA, Monnier VM, Cerami A. Diabetic cataract formation: potential role of glycosylation of lens crystalline. Proc Natl Acad Sci USA 1978;75: 2918-2922.
11. Brownlee M, Cerami A, Vlassara H. Advanced glycosylation end products in tissue and the biochemical basis of diabetic complications. N Engl J Med. 1988;318: 1315-1321.
12. Bucala R, Cerami A. Advanced glycosylation: chemistry, biology, and implications for diabetes and aging. Adv Pharmacol. 1992;23:1-34.
13. Beswick HT, Harding JJ. Conformational changes induced in lens alpha- and gamma-crystallins by modification with glucose 6-phosphate. Implications for cataract. Biochem J. 1987;246:761-769.
14. Santini SA, Mordente A, Meucci E, Miggiano GA, Martorana GE. Conformational stability of bovine α-crystallin. Evidence for a destabilizing effect of ascorbate. Biochem J. 1992;287:107-112.
15. Luthra M, Balasubramanian D. Nonenzymatic glycation alters protein structure and stability. A study of two eye lens crystalline. J Biol Chem. 1993;268:18119-18127.
16. Sun TX, Das BK, Liang JJN. Conformational and functional differences between recombinant human lens αA- and αB-crystallin. J Biol Chem. 1997;272:6220-6225.
17. Sun TX, Liang JJN. Intermolecular exchange and stabilization of human lens recombinant αA- and αB-crystallins. J Biol Chem. 1998;273:286-290.
18. Sun TX, Akhtar NJ, Liang JJN. Subunit exchange of lens α-crystallin: A fluorescence energy transfer study with the fluorescent labeled αA-crystallin mutant W9F as a probe. FEBS Lett. 1998;430:401-404.
19. Habeeb AFSA. Determination of free amino groups in proteins by trinitrobenzenesulfonic acid. Anal Biochem. 1966;14:328-336.
20. Mach H, Middaugh CR, Lewis RV. Statistical determination of the average values of the extinction coefficients of tryptophan and tyrosine in native proteins. Anal Biochem. 1992;200:74-80.
21. Laemmli UK. Cleavage of structural protein during assembly of the head of bacteriophage T4. Nature 1970; 227:680-685.
22. Liang JN, Li XY. Interaction and aggregation of lens crystalline. Exp Eye Res. 1991;53:61-66.
23. Sharma KK, Kaur H, Kumar GS, Kester K. Interaction of 1,1′-bis(4-anilino)naphthalene-5,5′-disulfonic acid with α-crystallin. J Biol Chem. 1998;273:8965-8970.
24. Sun TX, Akhtar NJ, Liang JJN. Conformational change of human lens insoluble a-crystallin. J Protein Chem. 1998;17:685-690.
25. Farahbakhsh ZT, Huang QL, Ding LL, Altenbach C, Steinhoff HJ, Horwitz J, Hubbell WL. Interaction of α-crystallin with spin-labeled peptides. Biochemistry 1995;34:509-516.
26. Lakowicz JR. Principles of fluorescence spectroscopy. New York, NY. Plenum Press. 1983:342-381.
27. Musci G, Berliner LJ. Probing different conformational states of bovine α-lactalbumin: fluorescence studies with 4,4′-bis[1-(phenylamino)-8-naphthalenesulfonate]. Biochemistry 1985;24:3852-3856.
28. Das KP, Surewicz WK. Temperature-induced exposure of hydrophobic surfaces and its effect on the chaperone activity of α-crystallin. FEBS Lett. 1995;369:321-325.
29. Das BK, Liang JJN, Chakrabarti B. Heat-induced conformational change and increased chaperone activity of lens α-crystallin. Curr Eye Res. 1997;16:303-309.
30. Cantor CR, Timasheff SN. Optical spectroscopy of proteins. In The Proteins, Vol V. New York, NY: Academic Press. 1982:145-306.
31. Smith PK, Krohn RI, Hermanson GT, Mallia AK, Gartner FH, Provenzano MD, Fujimoto EK, Goeke NM, Olson BJ, Klent DC. Measurement of protein using bicinchoninic acid. Anal Biochem. 1986;150:76-80.
32. Horwitz J, Huang QL, Ding L, Bova MP. Lens α-crystallin: chaperone-like properties. Methods Enzymol. 1998;290:365-383.
33. Horwitz J, Bova M, Huang QL, Ding L, Yaron O, Lowman S. Mutation of αB-crystallin: effects on chaperone-like activity. Int J Biol Macromol. 1998;22:263-269.
34. Ikeda K, Nagai R, Sakamoto T, Sano H, Araki T, Sakata N, Nakayama H, Yoshida M, Ueda S, Horiuchi S. Immunochemical approaches to AGE-structures: characterization of anti-AGE antibodies. J Immunol Methods 1998;215:95-104.
35. Liang JN, Pelletier MR. Destabilization of lens protein conformation by glutathione mixed disulfide. Exp Eye Res. 1988;47:17-25.
36. Kono M, Sen AC, Chakrabarti B. Thermodynamics of thermal and athermal denaturation of γ-crystallins: changes in conformational stability upon glutathione reaction. Biochemistry 1990;29:464-470.
37. Raman B, Rao CM. Chaperone-like activity and temperature-induced structural changes of α-crystallin. J Biol Chem. 1997;272:23559-23564.
38. Das BK, Liang JJN. Detection and characterization of α-crystallin intermediate with maximal chaperone-like activity. Biochem Biophys Res Commun. 1997;236:370-374.
39. Phipps BM, Typke D, Hegerl R, Volker S, Hoffmann A, Stetter KO, Baumeister W. Structure of a molecular chaperone from a thermophilic archaebacterium. Nature 1993;361:475-477.
40. Smulders RH, van Boekel MA, de Jong WW. Mutations and modifications support a 'pitted-flexiball' model for a-crystallin. Int J Biol Macromol. 1998;22:187-196.
41. Cherian M, Abraham EC. Decreased molecular chaperone property of α-crystallins due to posttranslational modifications. Biochem Biophys Res Commun. 1995;208: 675-967.
42. van Boekel MA, Hoogakker SE, Harding JJ, de Jong WW. The influence of some post-translational modifications on the chaperone-like activity of α-crystallin. Ophthalmic Res. 1996;28 (Suppl 1):32-38.
43. Sharma KK, Kumar GS, Murphy AS, Kester K. Identification of 1,1′-bi(4-anilino)naphthalene-5,5′-disulfonic acid binding sequences in alpha-crystallin. J Biol Chem. 1998;273:15474-15478.
44. Das BK, Sun TX, Akhtar NJ, Chylack Jr LT, Liang JJN. Fluorescence and Immunochemical Studies of Advanced Glycation Related Lens Pigments. Invest Ophthalmol Vis Sci. 1998;39:2058-2066.
45. ε-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins. Biochem J. 1997;324:565-570.