Chemistry of Nonenzymic Browning II

Reynolds, T. M.

doi:10.1016/s0065-2628(08)60149-4

Cited by 279 publications

(106 citation statements)

References 220 publications

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“…REACTIONS [3][4][5] This kind of reaction by long-lived glycated protein may contribute to the increased peroxidation of lipids when glycated protein was added in vitro and may also contribute to accelerating oxidative modification of vascular wall lipid in diabetes and atherosclerosis. …”

Section: Discussionmentioning

confidence: 99%

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Free Radicals Generated during the Glycation Reaction of Amino Acids by Methylglyoxal

Yim

Kang

Hah

et al. 1995

Journal of Biological Chemistry

237

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The formation of ␣-dicarbonyl compounds seems to be an important step for cross-linking proteins in the glycation or Maillard reaction. To elucidate the mechanism for the cross-linking reaction, we studied the reaction between a three-carbon ␣-dicarbonyl compound, methylglyoxal, and amino acids. Our results showed that this reaction generated yellow fluorescent products as formed in some glycated proteins. In addition, three types of free radical species were also produced, and their structures were determined by EPR spectroscopy. These free radicals are 1) the cross-linked radical cation, 2) the methylglyoxal radical anion as the counterion, and 3) the superoxide radical anion produced only in the presence of oxygen. The generation of the crosslinked radical cations and the methylglyoxal radical anions does not require metal ions or oxygens. These results indicate that dicarbonyl compounds cross-link free amino groups of protein by forming Schiff bases, which donate electrons directly to dicarbonyl compounds to form the cross-linked radical cations and the methylglyoxal radical anions. Oxygen can accept an electron from the radical anion to generate a superoxide radical anion, which can initiate damaging chain reactions. Time course studies suggest that the cross-linked radical cation is a precursor of yellow fluorescent glycation end products.

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Section: Discussionmentioning

confidence: 99%

“…This process is initiated by the condensation reaction of reducing sugars with free amino groups to form Schiff bases (Fig. 1A), which undergo rearrangement to form the relatively stable Amadori products (2,3). The Amadori products subsequently degrade into ␣-dicarbonyl compounds, deoxyglucosones (4,5).…”

mentioning

confidence: 99%

Free Radicals Generated during the Glycation Reaction of Amino Acids by Methylglyoxal

Yim

Kang

Hah

et al. 1995

Journal of Biological Chemistry

237

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“…The binding of a soluble ligand to a cell-surface receptor, however, may be quite a different phenomenon from the adherence of an entire cell to a protein substrate possessing that ligand. Proteins which accumulate significant amounts of AGE in vivo are insoluble interstitial proteins rather than soluble ligands [4][5][6][7][8]. If one is to evaluate receptor-mediated binding of activated monocytes to AGE-proteins, therefore, we believe it is more physiologically relevant to perform cellular adhesion assays to a protein substrate.…”

Section: Discussionmentioning

confidence: 99%

“…A slow rearrangement of the ketoamines takes place, however, which is not reversible. Advanced glycosylation end products (AGE) are formed by this rearrangement, and they continue to accumulate throughout the lifetime of the protein [2,[4][5][6][7][8][9].…”

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confidence: 99%

Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate

Gilcrease

Hoover

1990

Diabetologia

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Summary.Non-enzymatic glycosylation of proteins is thought to play an important role in the development of diabetic vascular disease. Advanced glycosylation end products have been shown to accumulate on basement membranes and collagen in diabetes, and receptors for such adducts have recently been found on murine macrophages. We have observed that human monocytes activated by endotoxin express receptors for advanced glycosylation end products of similar affinity and number as has been previously reported for murine macrophages. In addition, there is an increased adherence of activated human monocytes to a nonenzymatically glycosylated albumin substrate, and such adhesion can be competitively inhibited up to 50% by soluble, non-enzymatically glycosylated albumin. We suggest that increased adherence of activated monocytes to non-enzymatically glycosylated proteins in the vessel wall may result in monocyte stimulation and/or local monocyte accumulation and thereby contribute to vascular disease in diabetes.

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“…With time, the Amadori products dehydrate, rearrange and form irreversible structures referred to as advanced glycation end-products (AGEs) (82). The AGE moieties are brown, fluorescent chromophores that can crosslink proteins (83). In collagen samples obtained from the dura mater of normal human subjects, both the fluorescence and absorbance at 340 nm increased linearly with age of the subject (84).…”

Section: Glycation Hypothesis Of Aging and Its Potential Contributionmentioning

confidence: 99%

Aging and atherosclerosis in human and nonhuman primates

Cefalu

Wagner

1997

AGE

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Atherosclerosis is a major age-related process and public health problem and its clinical manifestations (coronary heart disease [CHD] and cerebrovascular disease) continue to be responsible for approximately 50% ofaU deaths occurring annually. In addition, CHD is responsible for over 70 to 80% of deaths among men and women over 65 years old. As our population ages (35 million people over the age of 65 in the U.S. by the year 2030) and because of the increased morbidity and mortality associated with atherosclerosis, an understanding of the role of aging in the development of atherosclerosis is needed.Multiple risk factors such as smoking, gender, hypertension, and lipids contribute to the development of atherosclerosis. However, these risk factors in combination explain only about half of the individual variability in incidence of CHD, and it has been hypothesized that age-related conditions may play a role. To propectively evaluate the effects of age per se on atherosclerosis progression in humans would require observation over many years.Thus, animal models that are representative of both aging processes and atherosclerosis would be extremely valuable. As such, nonhuman primates have been used extensively in atherosclerosis research. However, studies that will specifically evaluate the role of aging per se in contributing to development of atherosclerosis in nonhuman primates have only recently been initiated.In this review, the contribution of nonhuman primates to atherosclerosis research will be discussed, as will the development of atherosclerosis in both human and nonhuman primates. In addition, a role for age-related conditions in atherosclerosis development in both human and nonhuman primates will be outlined.

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Chemistry of Nonenzymic Browning II

Cited by 279 publications

References 220 publications

Free Radicals Generated during the Glycation Reaction of Amino Acids by Methylglyoxal

Free Radicals Generated during the Glycation Reaction of Amino Acids by Methylglyoxal

Activated human monocytes exhibit receptor-mediated adhesion to a non-enzymatically glycosylated protein substrate

Aging and atherosclerosis in human and nonhuman primates

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