Increased levels of advanced glycation end products in human cataractous lenses

Franke, Sybille; Dawczynski, J.; Strobel, Jürgen; Niwa, Toshimitsu; Stahl, Peter J.; Stein, Günter

doi:10.1016/s0886-3350(02)01841-2

Cited by 73 publications

(62 citation statements)

References 11 publications

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“…Relative amounts of different AGEs in physiological proteins and fluids may differ according to the severity of disease or particular tissue, reflecting local differences in carbonyl formation and oxidative stress. In general, HI adducts are reported to be present at higher concentrations than CML on plasma and tissue proteins (23,24). For example, G-H1 has been reported to be present at about twice the level of CML on plasma proteins of healthy human subjects.…”

Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease

Cotham

Metz

Ferguson

et al. 2004

Molecular & Cellular Proteomics

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Accumulation of advanced glycation end-products (AGEs) on proteins is associated with the development of diabetic complications. Although the overall extent of modification of protein by AGEs is limited, localization of these modifications at a few critical sites might have a significant effect on protein structure and function. In the present study, we describe the sites of modification of RNase by glyoxal under physiological conditions. Arg 39 and Arg 85 , which are closest to the active site of the enzyme, were identified as the primary sites of formation of the glyoxal-derived dihydroxyimidazolidine and hydroimidazolone adducts. Lower amounts of modification were detected at Arg 10

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Section: Discussionmentioning

confidence: 99%

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease

Cotham

Metz

Ferguson

et al. 2004

Molecular & Cellular Proteomics

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“…Increased levels of fructose can be explained by that the lens is one of the most susceptible tissues to the glycation reaction because the half-life of lens proteins is very long, and sugars also accumulate there at relatively high levels [21]. The glycation of lens crystalline is thought to accelerate the aggregation of these proteins and to cause cataract formation via decreasing the transparency of the lens [22]. Tissues such as lens, kidney and peripheral nerves have a polyol-metabolizing pathway converting glucose to sorbitol by aldose reductase and then sorbitol to fructose by sorbitol dehydrogenase [8].…”

Section: Discussionmentioning

confidence: 99%

Role of fructose concentration on cataractogenesis in senile diabetic and non-diabetic patients

Gul

Rahman

Hasnain

2009

Graefes Arch Clin Exp Ophthalmol

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“…Os AGEs podem ser detectados nos vasos sangüí-neos da retina e acredita-se que sejam responsáveis pelo aumento da permeabilidade das células endoteliais e que contribuam para a oclusão vascular (39). Os pericitos expressam receptores RAGE que, ao interagirem com seus ligantes AGEs, desencadeiam o aumento na transdução de sinais celulares e causam um dos fenôme-nos característicos da retinopatia diabética: a perda dos pericitos.…”

Section: Retinopatia Diabéticaunclassified

O papel dos produtos finais da glicação avançada (AGEs) no desencadeamento das complicações vasculares do diabetes

Barbosa

Oliveira

Seara

2008

Arq Bras Endocrinol Metab

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RESUMOOs produtos finais da glicação avançada (AgEs [do inglês, Advanced Glycation End-products]) constituem uma classe de moléculas heterogêneas formadas a partir de reações aminocarbonilo de natureza não-enzimática, que ocorrem aceleradamente no estado hiperglicêmico do diabetes. considerados importantes mediadores patogênicos das complicações diabéticas, os AgEs são capazes de modificar, irreversivelmente, as propriedades químicas e funcionais das mais diversas estruturas biológicas. na presente revisão, são apresentados os dados recentes da literatura que descrevem as vias de formação de AgEs, seu metabolismo, os principais mecanismos de ação dessas substâncias no desencadeamento dos processos patológicos, bem como os méto-dos de determinação de AgEs em amostras biológicas. Este artigo aponta, ainda, novas perspectivas de terapias anti-AgEs, a exemplo de estudos envolvendo a ação de compostos naturais dos alimentos, que podem oferecer potencial terapêutico para os portadores de diabetes ou de outras patologias associadas ao acúmulo degenerativo de AgEs. the advanced glycation end-products (AgEs) constitute a class of heterogeneous molecules formed by amino-carbonyl reactions of a non-enzymatic nature, which occur at an accelerated rate in the hyperglycemic state of diabetes. considered important pathogenic mediators of diabetic complications, AgEs are capable of irreversibly modifying the chemical properties and functions of diverse biological structures. In this review, recent data from literature is presented describing the pathways of AgEs formation, their metabolism, the main mechanisms of action of these substances in the triggering of pathological processes associated with diabetes, as well as methods of AgEs determination in biological samples. this text also points to new perspectives in anti-AgE therapies, an example of which is the studies involved with the action of natural compounds of food, which can represent a potential coadjuvant therapy for people with diabetes or other pathologies associated with the degenerative accumulation of AgEs.

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Increased levels of advanced glycation end products in human cataractous lenses

Cited by 73 publications

References 11 publications

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease

Proteomic Analysis of Arginine Adducts on Glyoxal-modified Ribonuclease

Role of fructose concentration on cataractogenesis in senile diabetic and non-diabetic patients

O papel dos produtos finais da glicação avançada (AGEs) no desencadeamento das complicações vasculares do diabetes

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