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Role of Oxidative Stress in Development of Complications in Diabetes
  • J. Baynes
  • Chemistry, Medicine
  • Diabetes
  • 1 April 1991
Structural characterization of the cross-links and other products accumulating in collagen in diabetes is needed to gain a better understanding of the relationship between oxidative stress and the development of complications in diabetes. Expand
Simple non-invasive assessment of advanced glycation endproduct accumulation
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. Expand
Role of oxidative stress in diabetic complications: a new perspective on an old paradigm.
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. Expand
Identification of N epsilon-carboxymethyllysine as a degradation product of fructoselysine in glycated protein.
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. Expand
N-epsilon-(carboxyethyl)lysine, a product of the chemical modification of proteins by methylglyoxal, increases with age in human lens proteins.
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. Expand
Maillard reaction products in tissue proteins: New products and new perspectives
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. Expand
Effect of Collagen Turnover on the Accumulation of Advanced Glycation End Products*
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. Expand
The Advanced Glycation End Product, N-(Carboxymethyl)lysine, Is a Product of both Lipid Peroxidation and Glycoxidation Reactions (*)
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. Expand
N epsilon-(carboxymethyl)lysine is a dominant advanced glycation end product (AGE) antigen in tissue proteins.
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. Expand
Skin autofluorescence, a measure of cumulative metabolic stress and advanced glycation end products, predicts mortality in hemodialysis patients.
A role for AGE as a contributor to mortality and CVD and warrants interventions specifically aimed at AGE accumulation is supported and skin AF is a strong and independent predictor of mortality in ESRD. Expand