Ribose sugars generate internal glycation cross-links in horse heart myoglobin

Biochemical and Biophysical Research Communications

Volumn 407, Issue 1, 2011, Pages 191-196

  Bokiej, Magdalena ^a   Livermore, Andrew T ^a   Harris, Andrew W ^a   Onishi, Anne C ^a   Sandwick, Roger K ^a  

^a MIDDLEBURY COLLEGE   (United States)

Author keywords

Cross linking; Glycation; Heme degradation; Protein modification; Ribose 5 phosphate

Indexed keywords

ADVANCED GLYCATION END PRODUCT; AMINE; APOMYOGLOBIN; HYDROGEN PEROXIDE; MYOGLOBIN; OXYGEN; PENTOSE; RIBOSE 5 PHOSPHATE;

AMINO TERMINAL SEQUENCE; ARTICLE; GLYCATION; MATRIX ASSISTED LASER DESORPTION IONIZATION TIME OF FLIGHT MASS SPECTROMETRY; POLYACRYLAMIDE GEL ELECTROPHORESIS; PRIORITY JOURNAL; PROTEIN CROSS LINKING; PROTEIN DEGRADATION; PROTEIN MODIFICATION;

ANIMALS; GLYCOSYLATION; HEME; HORSES; METMYOGLOBIN; MYOCARDIUM; MYOGLOBIN; OXIDATION-REDUCTION; RIBOSE; SPECTROMETRY, MASS, MATRIX-ASSISTED LASER DESORPTION-IONIZATION;

EQUIDAE;

EID: 79953164207     PISSN: 0006291X     EISSN: 10902104     Source Type: Journal    
DOI: 10.1016/j.bbrc.2011.02.138     Document Type: Article

References (25)

1. Wautier J.L., Schmidt A.M. Protein glycation: a firm link to endothelial cell dysfunction. Circ. Res. 2004, 95:233-238.
2. Cussimanio B.L., Booth A.A., Todd P., Hudson B.G., Khalifah R.G. Unusual susceptibility of heme proteins to damage by glucose during non-enzymatic glycation. Biophys. Chem. 2003, 105:743-755.
3. Catalano C.E., Choe Y.S., Ortiz de Montellano P.R. Reactions of the protein radical in peroxide-treated myoglobin. Formation of a heme-protein cross-link. J. Biol. Chem. 1989, 264:10534-10541.
4. Nagababu E., Rifkind J.M. Reaction of hydrogen peroxide with ferrylhemoglobin: superoxide production and heme degradation. Biochemistry 2000, 39:12503-12511.
5. Roy A., Sen S., Chakraborti A.S. In vitro nonenzymatic glycation enhances the role of myoglobin as a source of oxidative stress. Free Radic. Res. 2004, 38:139-146.
6. 2. J. Biol. Chem. 1992, 267:8827-8833.
7. 2-mediated cross-linking of sperm whale myoglobin. J. Biol. Chem. 1988, 263:17880-17886.
8. 2-mediated cross-linking between lactoperoxidase and myoglobin: elucidation of protein-protein radical transfer reactions. J. Biol. Chem. 2001, 276:23186-23191.
9. Smith P.R., Thornalley P.J. Mechanism of the degradation of non-enzymatically glycated proteins under physiological conditions. Studies with the model fructosamine, N epsilon-(1-deoxy-d-fructos-1-yl)hippuryl-lysine. Eur. J. Biochem. 1992, 210:729-739.
10. Gersten R.A., Gretebeck L.M., Hildick-Smith G., Sandwick R.K. Maillard reaction of ribose 5-phosphate generates superoxide and glycation products for bovine heart cytochrome c reduction. Carbohydr. Res. 2010, 345:2499-2506.
11. 2+) form. Int. J. Biol. Macromol. 2011, 48:202-209.
12. Gill S.C., Von Hippel P.H. Calculation of protein extinction coefficients from amino acid sequence data. Anal. Biochem. 1989, 182:319-326.
13. Tang J., Faustman C., Hoagland T.A. Krzywicki revisited: equations for spectrophotometric determination of myoglobin redox forms in aqueous meat extracts. J. Food Sci. 2004, 69:C717-C720.
14. Sandwick R., Johanson M., Breuer E. Maillard reactions of ribose 5-phosphate and amino acids. Ann. N. Y. Acad. Sci. 2005, 1043:85-96.
15. Munanairi A., O'Banion S.K., Gamble R., Breuer E., Harris A.W., Sandwick R.K. The multiple Maillard reactions of ribose and deoxyribose sugars and sugar phosphates. Carbohydr. Res. 2007, 342:2575-2592.
16. Finkelstein E., Rosen G.M., Rauckman E.J., Paxton J. Spin trapping of superoxide. Mol. Pharmacol. 1979, 16:676-685.
17. Tal M., Silberstein A., Nusser E. Why does Coomassie Brilliant Blue R interact differently with different proteins? A partial answer. J. Biol. Chem. 1985, 260:9976-9980.
18. Hunt J.V., Dean R.T., Wolff S.P. Hydroxyl radical production and autoxidative glycosylation. Glucose autoxidation as the cause of protein damage in the experimental glycation model of diabetes mellitus and ageing. Biochem. J. 1988, 256:205-212.
19. Hunt J.V., Simpson J.A., Dean R.T. Hydroperoxide-mediated fragmentation of proteins. Biochem. J. 1988, 250:87-93.
20. Puchala M., Schuessler H. Oxygen effect in the radiolysis of proteins: IV. Myoglobin. Int. J. Pept. Protein Res. 1995, 46:326-332.
21. Mozziconacci O., Mirkowski J., Rusconi F., Pernot P., Bobrowski K., Houee-Levin C. Superoxide radical anions protect enkephalin from oxidation if the amine group is blocked. Free Radic. Biol. Med. 2007, 43:229-240.
22. Nagy P., Kettle A.J., Winterbourn C.C. Superoxide-mediated formation of tyrosine hydroperoxides and methionine sulfoxide in peptides through radical addition and intramolecular oxygen transfer. J. Biol. Chem. 2009, 284:14723-14733.
23. Winterbourn C.C., Parsons-Mair H.N., Gebicki S., Gebicki J.M., Davies M.J. Requirements for superoxide-dependent tyrosine hydroperoxide formation in peptides. Biochem. J. 2004, 381:241-248.
24. Tressl R., Wondrak G.T., Kruger R.P., Rewicki D. New melanoidin-like Maillard polymers from 2-deoxypentoses. J. Agric. Food Chem. 1998, 46:104-110.
25. Finley E.L., Dillon J., Crouch R.K., Schey K.L. Identification of tryptophan oxidation products in bovine alpha-crystallin. Protein Sci. 1998, 7:2391-2397.