O2− generation and lipid peroxidation during the oxidation of a glycated polypeptide, glycated polylysine, in the presence of iron-ADP

Sakurai, Tamiko; Sugioka, Katsuaki; Nakano, Minoru

doi:10.1016/0005-2760(90)90106-8

Cited by 85 publications

(51 citation statements)

References 29 publications

Supporting

Mentioning

Contrasting

Order By: Relevance

“…through lipid peroxidation (44) or direct formation of carbonyl groups on the protein as proposed by Stadtman (45). Lipid peroxidation, however, is unlikely to be involved since many studies have shown that it is not preventable by catalase (46,47). Another possibility is based on Brennan's work (26) in which no evidence for the formation of new cross-links in tendons from diabetic rats could be found, suggesting that maturation of labile into stable cross-links may be occurring in diabetes.…”

Section: Discussionmentioning

confidence: 99%

Involvement of Hydrogen Peroxide in Collagen Cross-linking by High Glucose in Vitro and in Vivo

Elgawish

Glomb

Friedlander

et al. 1996

Journal of Biological Chemistry

183

101

View full text Add to dashboard Cite

The Maillard reaction has been implicated in crosslinking and fluorescence formation of collagen exposed to high glucose in vitro. However, several pharmacologic agents, whose action seems unrelated to pathways of nonenzymatic glycation, have been demonstrated to prevent cross-linking in diabetes. To clarify this discrepancy, kinetic changes in glycation, glycoxidation (carboxymethyllysine, CML), and cross-linking (measured as tendon breaking time, TBT) were evaluated in rat tail tendons incubated in 5 and 30 mM glucose in vitro and in tendons implanted in vivo into diabetic rat peritoneal cavity. In vitro, rates were found to be both O 2 -and glucose-dependent. Tendon preglycation and presence of added 2 mM glycosylamine and Amadori compounds (Amadori product of glucose and propylamine) catalyzed these changes in a primarily O 2 -dependent manner. In the presence of Amadori compounds, kinetic changes were dramatically increased and were preventable by addition of catalase to the medium. Tendons implanted into diabetic rat peritoneum became more rapidly glycoxidized and cross-linked when implanted at day 30 from diabetes onset (high tissue glycation) compared to day 3 (low tissue glycation) in spite of similar glycation kinetics, suggesting a mechanistic dissociation between glycation, glycoxidation, and crosslinking in diabetes. Indeed, intraperitoneal injection of catalase and other antioxidants dramatically suppressed cross-linking, fluorescence formation, and, to some extent, glycoxidation, without affecting glycation. This study confirms the role of oxidative stress in protein cross-linking by the Maillard reaction in vitro and provides the first evidence for a role of H 2 O 2 in crosslinking in diabetes. Whereas Amadori products are a potent source of H 2 O 2 formation in vitro, their precise contribution to H 2 O 2 generation and the actual role of Maillard reaction products in collagen cross-linking in diabetes requires further investigation.Considerable efforts have been devoted in recent years toward understanding of the pathogenetic mechanisms leading to collagen insolubilization in diabetes and aging (1-3). The rationale for this research lies in the hope that understanding the biochemical basis of stochastic mechanisms of damage to collagen will help elucidate their role in diabetic complications and aging. One key proposition is that protein cross-links are generated in the advanced Maillard reaction (4, 5). According to the original concept proposed by Hodge (6), the central molecule responsible for the advanced Maillard reaction is the Amadori product which, upon dehydration and rearrangement, forms highly reactive deoxyosones Ϫ potent precursors of protein cross-links. This concept was challenged by Namiki (7) who found that sugar fragmentation can also occur at the stage of the glycosylamine, or Schiff base, i.e. prior to the Amadori rearrangement. Glyoxal is then formed which can serve as a protein cross-link (8 -10). More recently, Wolff et al. (11) obtained evidence from in vitro experimenta...

show abstract

Section: Discussionmentioning

confidence: 99%

Involvement of Hydrogen Peroxide in Collagen Cross-linking by High Glucose in Vitro and in Vivo

Elgawish

Glomb

Friedlander

et al. 1996

Journal of Biological Chemistry

183

101

View full text Add to dashboard Cite

show abstract

“…However, there are some initial experimental observations which imply that the early products of protein glycation, such as the Schiff base and Amadori compound, may be key structural components involved in the generation of a superoxide anion. [7][8][9] In an effort to better understand the role of a superoxide anion in the relationship between the Maillard reaction and biological disorders, the generation of a superoxide anion was determined in various combinations of carbonyls with amines and a number of Amadori compounds. 8,10,11 Generally, the detection of a superoxide anion was performed by the cytochrome c method and the NBT (nitroblue tetrazolium) method.…”

mentioning

confidence: 99%

Spectrophotometric Assay of Superoxide Anion Formed in Maillard Reaction Based on Highly Water-soluble Tetrazolium Salt

et al. 2002

View full text Add to dashboard Cite

“…2) [14]. It has been shown that AGEs produce reactive oxygen species thereby enhancing cellular oxidant stress [5,[15][16][17][18].…”

Section: Resultsmentioning

confidence: 99%

Advanced Glycation Endproducts Act as An Initiator of Skin Tumors in Mice

Ogata

Hasegawa

Nakamura

et al. 2006

J. Clin. Biochem. Nutr.

View full text Add to dashboard Cite

Summary The role of advanced glycation endproducts (AGEs) as the initiator of tumor induction was investigated in SENCAR mice. Initiation with AGEs-modified bovine serum albumin (AGEs-BSA) increased both the incidence of tumor-bearing mice and the mean number of tumors per mouse. An immunohistochemical study revealed an increase in 8-hydroxy-2'-deoxyguanosine (8-OhdG) in nuclei of epidermal cells in the AGEs-BSA treated mice. Furthermore, a Salmonella mutagenicity test revealed that AGEs-BSA was mutagenic only in Salmonella TA104, a strain more sensitive to oxidative stress than other strains. These results suggest that AGEs are mutagenic through a mechanism associated with oxidative stress.

show abstract

O2− generation and lipid peroxidation during the oxidation of a glycated polypeptide, glycated polylysine, in the presence of iron-ADP

Cited by 85 publications

References 29 publications

Involvement of Hydrogen Peroxide in Collagen Cross-linking by High Glucose in Vitro and in Vivo

Involvement of Hydrogen Peroxide in Collagen Cross-linking by High Glucose in Vitro and in Vivo

Spectrophotometric Assay of Superoxide Anion Formed in Maillard Reaction Based on Highly Water-soluble Tetrazolium Salt

Advanced Glycation Endproducts Act as An Initiator of Skin Tumors in Mice

Contact Info

Product

Resources

About