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Simple non-invasive assessment of advanced glycation endproduct accumulation
TLDR
The Autofluorescence Reader (AFR) offers a simple alternative to invasive measurement of AGE accumulation and, to date, has been validated in non-pigmented skin and may prove to be a useful clinical tool for rapid risk assessment of A GE-related long-term complications in diabetes mellitus and in other conditions associated with A GE accumulation.
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Role of oxidative stress in diabetic complications: a new perspective on an old paradigm.
TLDR
It is proposed that the increased chemical modification of proteins by carbohydrates and lipids in diabetes is the result of overload on metabolic pathways involved in detoxification of reactivecarbonyl species, leading to a general increase in steady-state levels of reactive carbonyl compounds formed by both oxidative and nonoxidative reactions.
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Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein.
TLDR
The browning of fFL incubation mixtures proceeded to a greater extent under a nitrogen versus an air atmosphere, suggesting that oxidative degradation of Amadori adducts to form CML may limit the browning reactions of glycated proteins.
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N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins.
TLDR
Levels of CML and CEL are proposed to provide an index of glyoxal and methylglyoxal concentrations in tissues, alterations in glutathione homoeostasis and dicarbonyl metabolism in disease, and sources of advanced glycation end-products in tissue proteins in aging and disease.
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Maillard reaction products in tissue proteins: New products and new perspectives
TLDR
A new class of intracellular sulfhydryl modifications, Cys-AGE/ALEs, that may play an important role in regulatory biology and represent a primitive link between nonenzymatic and enzymatic chemistry in biological systems are described.
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Overexpression of glyoxalase-I in bovine endothelial cells inhibits intracellular advanced glycation endproduct formation and prevents hyperglycemia-induced increases in macromolecular endocytosis.
TLDR
Overexpression of glyoxalase-I completely prevented both hyperglycemia-induced AGE formation and increased macromolecular endocytosis.
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Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products*
TLDR
First experimental evidence that protein turnover is a major determinant in AGE accumulation in different collagen types is provided, thereby providing the first reasonable estimates of the half-lives of these collagens.
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The Advanced Glycation End Product, N-(Carboxymethyl)lysine, Is a Product of both Lipid Peroxidation and Glycoxidation Reactions (*)
TLDR
The results suggest that lipid peroxidation, as well as glycoxidation, may be an important source of CML in tissue proteins in vivo and that CML may be a general marker of oxidative stress and long term damage to protein in aging, atherosclerosis, and diabetes.
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Life-long reduction in MnSOD activity results in increased DNA damage and higher incidence of cancer but does not accelerate aging.
TLDR
Life-long reduction of MnSOD activity leads to increased levels of oxidative damage to DNA and increased cancer incidence but does not appear to affect aging.
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N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins.
TLDR
It is concluded that AGEs are largely glycoxidation products and that CML is a major AGE recognized in tissue proteins by polyclonal antibodies to AGE proteins.
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