Protein glycation: Creation of catalytic sites for free radical generation

Annals of the New York Academy of Sciences

Volumn 928, Issue , 2001, Pages 48-53

  Yim, Moon B ^a   Yim, Hyung Soon ^a   Lee, Cheolju ^b   Kang, Sa Ouk ^b   Boon Chock, P ^a  

^a NATIONAL HEART LUNG AND BLOOD INSTITUTE   (United States)

^b Seoul National University   (South Korea)

Author keywords

Maillard reaction; Methylglyoxal; Nonenzymatic glycosylation

Indexed keywords

1,2 DICARBONYL DERIVATIVE; ADVANCED GLYCATION END PRODUCT; AMINO ACID; DEOXYGLUCOSE; FREE RADICAL; GLYOXAL; M PROTEIN; METHYLGLYOXAL; NERVE PROTEIN;

AGING; ATHEROSCLEROSIS; CATALYSIS; CHEMICAL STRUCTURE; CONFERENCE PAPER; CROSS LINKING; DIABETES MELLITUS; LENS; OXIDATION REDUCTION REACTION; PROTEIN GLYCOSYLATION; PROTEIN MODIFICATION;

EID: 0035028667     PISSN: 00778923     EISSN: None     Source Type: Book Series    
DOI: 10.1111/j.1749-6632.2001.tb05634.x     Document Type: Conference Paper

References (27)

1. Chemistry of non-enzymatic browning
2. 3-Deoxyglucosone cross-links proteins under physiological conditions
3. Mechanism of autoxidative glycosylation: Identification of glyoxal and arabinose as intermediates in the autoxidative modification of proteins by glucose
4. Formation of the N,N′-dialkylpyrazine cation radical from glyoxal dialkylimine produced on the reaction of sugar with an amine or amino acid
5. Role of the Maillard reaction in aging of tissue proteins. Advanced glycation end product - Dependent increase in imidazolium cross-links in human lens proteins
6. Implication of lysine residues in the loss of enzymatic activity in rat liver 6-phosphogluconate dehydrogenase found in aging
7. Accelerated age-related browning of human collagen in diabetes mellitus
8. Involvement of hydrogen peroxide in collagen cross-linking by high glucose in vitro and in vivo
9. Nonenzymatic browning in vivo: Possible process for aging of long-lived proteins
10. Excessive nonenzymatic glycosylation of peripheral and central nervous system myelin components in diabetic rats
11. Advanced glycation end-products in neurofilament conglomeration of motorneurons in familial and sporadic amyotrophic lateral sclerosis
12. Glycated tau protein in Alzheimer disease: A mechanism for induction of oxidant stress
13. Nonenzymatic glycosylation and pathogenesis of diabetic complications
14. Free radical generation by early glycation products: A mechanism for accelerated atherogenesis in diabetes
15. Superoxide production from nonenzymatically glycated protein
16. Structure elucidation of a senescence cross-link from human extracellular matrix. Implication of pentoses in the aging process
17. End-stage renal disease and diabetes catalyze the formation of a pentose-derived crosslink from aging human collagen
18. Mechanism of formation of the Maillard protein cross-link pentosidine. Glucose, fructose, and ascorbate as pentosidine precursors
19. Formation of pentosidine during nonenzymatic browning of proteins by glucose. Identification of glucose and other carbohydrates as possible precursors of pentosidine in vivo
20. Immunohistochemical detection of advanced glycosylation end products in diabetic tissues using monoclonal antibody to pyrraline
21. Identification of N-epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein
22. N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins
23. Binding and modification of proteins by methylglyoxal under physiological conditions. A kinetic and mechanistic study with N alpha-acetylarginine, N alpha-acetylcysteine, and N alpha-acetyllysine, and bovine serum albumin
24. New biomarkers of Maillard reaction damage to proteins
25. Protein cross-linking by the Maillard reaction. Isolation, characterization, and in vivo detection of a lysine-lysine cross-link derived from methylglyoxal
26. Free radicals generated during the glycation reaction of amino acids by methylglyoxal. A model study of protein-cross-linked free radicals
27. Oxidation-reduction properties of methylglyoxal-modified protein in relation to free radical generation