The glycation of bovine lens β(L)-, β(S)- and γ-crystallins demonstrated by isoelectric focusing and lectin staining

Experimental Eye Research

Volumn 65, Issue 5, 1997, Pages 711-715

  Ahrend, Michael H J ^a   Bours, Johan ^a  

^a UNIVERSITY OF BONN   (Germany)

Author keywords

Coomassie blue staining; isoelectric focusing; lectin staining; (S) and crystallins

Indexed keywords

BETA CRYSTALLIN; GAMMA CRYSTALLIN; LECTIN;

ANIMAL TISSUE; ARTICLE; CATTLE; GLYCATION; ISOELECTRIC FOCUSING; LENS; NONHUMAN; PRIORITY JOURNAL; PROTEIN MODIFICATION; STAIN;

EID: 0030665259     PISSN: 00144835     EISSN: None     Source Type: Journal    
DOI: 10.1006/exer.1997.0378     Document Type: Article

References (29)

1. Abraham, E. C. Cherian, M. Smith, J. B. 1994, Site selectivity in the glycation of αA- and αB-crystallins by glucose. Biochem. Biophys. Res. Commun. 201, 1451, 6.
2. Ahrend, M. H. J. Bours, J. Födisch, H. J. 1987, Water-soluble and -insoluble crystallins in the developing human fetal lens, analyzed by agarose/polyacrylamide isoelectric focusing. Ophthalmic Res. 19, 150, 6.
3. 1, J. Histochem. Cytochem. 24, 908, 14.
4. Bours, J. 1973, Free isoelectric focusing of bovine lens γ-crystallins. Exp. Eye Res. 16, 501, 15.
5. S, Ophthalmic Res. 27 (Suppl. 1), 23, 31.
6. Bours, J. Rabaey, M. 1975, Isoelectric focusing and immunochemistry of bovine lens crystallins. Exp. Eye Res. 20, 180, 1.
7. Bours, J. Ahrend, M. H. J. Breipohl, W. 1995, Regionality of calf lens crystallin subunits, demonstrated by lectin staining. Ocular toxicology, 219, 25, Plenum Press, New York.
8. Bours, J. Ahrend, M. H. J. Wegener, A. Hockwin, O. 1987, Glycosylated crystallins in microsections of diabetic rat lenses. Concepts in toxicology, Homburger, F. 4, 350, 9.
9. Bours, J. Hofmann, D. Födisch, H. J. 1990a, The anodic shift in isoelectric point of human lens crystallins, demonstrated by immunoelectrophoresis with specific and polyvalent antisera. Docum. Ophthalmol. 76, 192.
10. Bours, J. Wegener, A. Hoffmann, D. Födisch, H. J. Hockwin, O. 1990b, Protein profiles of microsections of the fetal and adult human lens during development and ageing. Mechanisms of Ageing & Development, 54, 13, 27.
11. Carver, J. A. Aquilina, J. A. Truscott, J. W. 1994, A possible chaperone-like quaternary structure forα-crystallin. Exp. Eye Res. 59, 231, 4.
12. Chiou, S. H. Chylack Jr, L. T. Tung, W. H. Bunn, H. F. 1981, Nonenzymatic glycosylation of bovine lens crystallins. J. Biol. Chem. 256, 5176, 80.
13. Garlick, R. L. Mazer, J. S. Chylack, Jr, L. T. Tung, W. H. Bunn, H. F. 1984, Nonenzymatic glycation of human lens crystallin. Effect of aging and diabetes mellitus. J. Clin. Invest. 74, 1742, 9.
14. Harding, J. J. 1985, Nonenzymatic covalent posttranslational modification of proteins in vivo. Adv. Protein Chem. 37, 247, 334.
15. Harding, J. J. 1991, Nonenzymatic posttranslational modification of lens proteins in aging. Presbiopia research, Abrecht, G.Stark, L. W. 57, 60, Plenum Press, New York.
16. Harding, J. J. Dilley, K. J. 1976, Structural proteins of the mammalian lens: a review with emphasis on changes in development, aging and cataract. Exp. Eye Res. 22, 1, 73.
17. Hockwin, O. Schmutter, J. Müller, H. K. 1963, Untersuchungen über Gewicht und Volumen verschieden alter Rinderlinsen. Albr. v. Graefes Arch. Klin. Exp. Ophthalmol. 166, 136, 51.
18. Kabasawa, I. Tsunematsu, Y. Barber, G. W. Kinoshita, J. H. 1977, Low molecular weight proteins of the bovine lens. Exp. Eye Res. 24, 437, 48.
19. Leathem, A. J. C. Atkins, N. J. 1983, Lectin binding to paraffin sections. Immunocytochem. 2, 39, 70.
20. S, EMBO J. 4, 2597, 602.
21. Rink, H. Bours, J. Hoenders, H. J. 1982, Guidelines for the classification of lenses and the characterization of lens proteins. Notes from the EURAGE workshop in Louvain-La-Neuve, Belgium. Ophthalmic Res. 14, 284, 91.
22. S, Biochemistry, 29, 3929, 36.
23. Swamy, M. S. Abraham, E. C. 1987, Lens protein composition, glycation and high molecular weight aggregation in aging rats. Invest. Ophthalmol. Vis. Sci. 28, 1693, 701.
24. Swamy, M. S. Abraham, E. C. 1991, Differential glycation of rat α-,β- and γ-crystallins. Exp. Eye Res. 52, 439, 44.
25. Swamy, M. S. Abraham, A. Abraham, E. C. 1992, Glycation of human lens proteins: Preferential glycation of αA subunits. Exp. Eye Res. 54, 337, 45.
26. S, Current Eye Res. 8, 139, 49.
27. Trifonova, N. L. Alexiev, C. Stamenova, M. Goranov, M. 1993, Age-related changes of water-soluble proteins of human eye lens during the prenatal period. Ophthalmic Res. 25, 162, 71.
28. van Boekel, M. A. M. Hoenders, H. J. 1992, In vivo glycation of bovine lens crystallins. Biochim. Biophys. Acta, 1159, 99, 102.
29. S, Exp. Eye Res. 5, 255, 66.