Susceptibility of gamma-irradiated proteins to in vitro glycation: Exposure to oxygen free radicals increases glycation-induced modifications

Cell Biochemistry and Function

Volumn 14, Issue 2, 1996, Pages 149-154

  Traverso, Nicola ^a   Odetti, Patrizio ^b   Cheeseman, Kevin ^c   Cottalasso, Damiano ^a   Marinari, Umberto Maria ^a   Pronzato, Maria Adelaide ^a  

^a UNIVERSITY OF GENOA   (Italy)

^b UNIVERSITY OF GENOA   (Italy)

^c BRUNEL UNIVERSITY   (United Kingdom)

Author keywords

Albumin; Fluorescence; Free radicals; Glycation; Irradiation; Oxidation

Indexed keywords

OXYGEN RADICAL; TRYPTOPHAN;

ARTICLE; CONFORMATIONAL TRANSITION; CONTROLLED STUDY; FLUORESCENCE; GAMMA IRRADIATION; GLYCATION; OXIDATION; PRIORITY JOURNAL; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION; RADIOLYSIS;

EID: 0029993272     PISSN: 02636484     EISSN: None     Source Type: Journal    
DOI: 10.1002/cbf.658     Document Type: Article

References (24)

1. Fluckiger, R., Gallop, P. M., Baynes, J. W., Thorpe, S. R., Murtiashow, M. A. and Bada, J. L. (1984). Nonenzymatic Modifications, Methods in Enzymology, (Wolf, F. and Moldave, K., eds.) Academic Press, London, pp. 77-115.
2. Davies, K. J. A. and Goldberg, A. L. (1987). Oxygen radicals stimulate intracellular proteolysis and lipid peroxidation by independent mechanisms in erythrocytes. J. Biol. Chem., 262 (17), 8227-8234.
3. Satoh, M., Imazumi, K., Bessho, T. and Shiga, T. (1984). Increased erythrocytes aggregation in diabetes mellitus and its relationships to glycosylated haemoglobin and retinopathy. Diabetologia, 27, 517-521.
4. Jain, S. K., McVie, R., Duett, J. and Herbst, J. J. (1989). Erythrocytes membranes lipid peroxidation and glycosylated hemoglobin in diabetes. Diabetes, 38, 1539-1543.
5. Harman, D. (1992). Free radical theory of aging. Mutat. Res., 275, 257-266.
6. Monnier, V. M. (1990). Nonenzymatic glycosylation, the Maillard reaction and the aging process. J. Gerontol., 45, B105-B111.
7. Davies, K. J. A. (1987). Protein damage and degradation by oxygen radicals. I. General aspects. J. Biol. Chem., 262 (20), 9895-9901.
8. 2+ in rat liver microsomes. Biochem. J., 208, 129-140.
9. Wolff, S. P., Jiang, Z. Y. and Hunt, J. V. (1991). Protein glycation and oxidative stress in diabetes mellitus and ageing. Free Rad. Biol. Med., 10, 339-352.
10. Baynes, J. W. (1991). Role of oxidative stress in development of complications in diabetes mellitus. Diabetes, 40, 405-412.
11. Odetti, P., Pronzato, M. A., Noberasco, G., Cosso, L., Traverse, N., Cottalasso, D. and Marinari, U. M. (1994). Relationships between glycation and oxidation related fluorescences in rat collagen during aging. Lab. Invest., 70 (1), 61-67.
12. Asmus, K. D. (1984). Pulse radiolysis methodology. Meth. Enzymol., 105, 167-178.
13. Seccia, M., Brossa, O., Gravela, E., Slater, T. F., Cheseman, K. H. (1991), Exposure of βL-crystallin to oxidizing free radicals enhances its susceptibility to oxygen free radicals. Biochem. J., 274, 869-873.
14. Gebicki, S. and Gebicki, J. M. (1993). Formation of peroxide in amino acids and proteins exposed to oxygen free radicals. Biochem. J., 289, 743-749.
15. Fricke, H. and Hart, E. J. (1966). In: Radiation Dosimetry. (Attix, F. H. and Roesch, W. C., eds.), Academic Press: New York.
16. Kohn, R. R., Cerami, A. and Monnier, V. M. (1984). Collagen aging in vitro by nonenzymatic glycosylation and browning. Diabetes, 33, 57-59.
17. Wolff, S. P. and Dean, R. T. (1987). Glucose autoxidation and protein modification. Biochem. J., 245, 243-250.
18. Davies, K. J. A., Delsignore, M. E. and Lin, S. W. (1987). Protein damage and degradation by oxygen radicals. II. Modification of aminoacids. J. Biol. Chem., 262 (20), 9902-9907.
19. Davies, K. J. A., Linm, S. W. and Pacifici, R. E. (1987). Protein damage and degradation by oxygen radicals. III. Modification of secondary and tertiary structure. J. Biol. Chem., 262 (20), 9914-9920.
20. Dean, R. T., Thomas, S. M., Vince, M. and Wolff, S. P. (1986). Fragmentation of proteins by free radicals and its effect on their susceptibility to enzymic hydrolysis. Biomed. Biochim. Acta, 45, 1563-1573.
21. Hicks, M., Delbridge, L., Yue, D. K. and Reeve, T. S. (1988). Catalysis of lipid peroxidation by glucose and glycosylated collagen. Block. Biophys. Res. Commun., 151, 649-655.
22. Fujimori, E. (1989). Cross-linking and fluorescence changes of collagen by glycation and oxidation. Bioch. Biophys. Acta, 998, 105-110.
23. Chace, C. V., Carubelli, R. and Nordquist, R. E. (1991). The role of nonenzymatic glycosylation, transition metals and free radicals in the formation of collagen aggregates. Arch. Biochem. Biophys., 288, 473-480.
24. Fu, M. X., Knecht, K. J., Thorpe, S. R. and Baynes, J. W. (1992). Role of oxygen in cross-linking and chemical modification of collagen by glucose. Diabetes, 41 (suppl. 2), 42-48.