Dynamics of rat hepatocyte histone glycoxidation after general X-ray irradiation

Tsitologiya

Volumn 48, Issue 6, 2006, Pages 515-521

  Kuleva, N V ^a   Fedorova, M A ^a   Frolov, A A ^a  

^a ST PETERSBURG STATE UNIVERSITY   (Russian Federation)

Author keywords

Advanced glycation end products; DNA; Glycoxidative modification; Hepatocytes; Histones; X ray irradiation

Indexed keywords

FRUCTOSAMINE; HISTONE; MALONALDEHYDE;

ANIMAL; ARTICLE; BLOOD; GLUCOSE BLOOD LEVEL; GLYCOLYSIS; LIPID PEROXIDATION; LIVER CELL; MALE; METABOLISM; RADIATION EXPOSURE; RAT; WHOLE BODY RADIATION; WISTAR RAT;

ANIMALS; BLOOD GLUCOSE; FRUCTOSAMINE; GLYCOLYSIS; HEPATOCYTES; HISTONES; LIPID PEROXIDATION; MALE; MALONDIALDEHYDE; RATS; RATS, WISTAR; WHOLE-BODY IRRADIATION;

EID: 33750102362     PISSN: 00413771     EISSN: None     Source Type: Journal    
DOI: None     Document Type: Review

References (29)

1. Russian source
2. Russian source
3. Russian source
4. Russian source
5. Russian source
6. Russian source
7. Russian source
8. Russian source
9. Russian source
10. Russian source
11. Russian source
12. Russian source
13. Russian source
14. Ahmed N., Arginov K., Minhas H. S. 2002. Assay of advanced glycation end product. Biochem. J. 364: 1-14.
15. Cervantes-Lauren D., Jacobson E. L., Jacobson M. K. 1996. Glycation and glycoxidation of histones by ADP-ribose. J. Biol. Chem. 271: 10461-10469.
16. Davies K. J. A. 1987. Protein damage and degradation by oxygen radicals. J. Biol. Chem. 262: 9895-9900.
17. Gordon J. S., Rosenfeld B. A., Kaufman A. 1980. Evidence for a quantitative tissue-specific distribution of the high-motility group chromosomal proteins. Biochemistry. 19: 4395-4400.
18. Ithaki N. F., Gill H. H. 1964. A micro-biuret method for estimating proteins. Analyt. Biochem. 9: 401-408.
19. Jacobson E. L., Cervantes-Lauren D., Jacobson M. K. 1997. ADP-ribose in glycation and glycoxidation reaction. Adv. Exp. Med. Biol. 419: 371-379.
20. Kong S., Chock B. 1995. Enzyme-like activity of glycated cross-linked proteins in free radical generation. Ann. N. Y. Acad. Sci. 1: 169-181.
21. Kornberg R. D. 1974. Chromatin structure: a repeating unit of histone and DNA. Chromatin structure is based on a repeating unit of eighth histones molecules and about 200 DNA base pairs. Science. 184: 868-875.
22. Monnier Y. H., Vishwanath V., Frank K. E., Elmets C. A., Dauchot P., Kohr R. R. 1986. Relation between complication of type I diabetes and collagen-linked fluorescence. New England J. Med. 314: 403-408.
23. Moore J., Krebs J. 2004. Histone modification and DNA double-strands break repair. Biochem, Cell Biol. 82: 446-452.
24. Shringarpure R., Grune T., Davies K. J. 2001. Protein oxidation and 20S-proteasome-dependent proteolysis in mammalian cells. Cell Mol. Life Sci. 58: 1442-1450.
25. Stadman E. R. 1990. Metall ion-catalyzed oxidation of proteins: biochemical mechanism and biological consequences. Free Rad. Biol. Med. 9: 315-319.
26. Strahl B. D., Allis D. 2000. A language of covalent histone modification. Nature. 403: 41-45.
27. Timmermann S., Lehrmann H., Polesskaya A., Harel-Ballan A. 2001. Histone acetylation and disease. Cell Mol. Life Sci. 58: 728-736.
28. Traverso N., Menini S., Maineri E. 2004. Malondialdehyde, a lipoperoxidation-derived aldehyde, can bring about secondary oxidative damage to proteins. J. Gerontol. 59A: 890-895.
29. Wondrak G., Cervantes-Lauren D., Jacobson E. L., Jacobson M. K. 2000. Histone carbonylation in vivo and in vitro. Biochem. J. 315: 769-777.