Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention

Advanced glycation end-products (AGEs) are non-enzymatic protein and amino acid adducts as well as DNA adducts which form from dicarbonyls and glucose. AGE formation is enhanced in diabetes and is associated with the development of diabetic complications. In the current review, we discuss mechanisms...

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Autores principales: Brings, Sebastian, Fleming, Thomas, Freichel, Marc, Muckenthaler, Martina U., Herzig, Stephan, Nawroth, Peter P.
Formato: Online Artículo Texto
Lenguaje:English
Publicado: MDPI 2017
Materias:
Review
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454897/
https://www.ncbi.nlm.nih.gov/pubmed/28475116
http://dx.doi.org/10.3390/ijms18050984
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author Brings, Sebastian
Fleming, Thomas
Freichel, Marc
Muckenthaler, Martina U.
Herzig, Stephan
Nawroth, Peter P.
author_facet Brings, Sebastian
Fleming, Thomas
Freichel, Marc
Muckenthaler, Martina U.
Herzig, Stephan
Nawroth, Peter P.
author_sort Brings, Sebastian
collection PubMed
description Advanced glycation end-products (AGEs) are non-enzymatic protein and amino acid adducts as well as DNA adducts which form from dicarbonyls and glucose. AGE formation is enhanced in diabetes and is associated with the development of diabetic complications. In the current review, we discuss mechanisms that lead to enhanced AGE levels in the context of diabetes and diabetic complications. The methylglyoxal-detoxifying glyoxalase system as well as alternative pathways of AGE detoxification are summarized. Therapeutic approaches to interfere with different pathways of AGE formation are presented.
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spelling pubmed-54548972017-06-08 Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention Brings, Sebastian Fleming, Thomas Freichel, Marc Muckenthaler, Martina U. Herzig, Stephan Nawroth, Peter P. Int J Mol Sci Review Advanced glycation end-products (AGEs) are non-enzymatic protein and amino acid adducts as well as DNA adducts which form from dicarbonyls and glucose. AGE formation is enhanced in diabetes and is associated with the development of diabetic complications. In the current review, we discuss mechanisms that lead to enhanced AGE levels in the context of diabetes and diabetic complications. The methylglyoxal-detoxifying glyoxalase system as well as alternative pathways of AGE detoxification are summarized. Therapeutic approaches to interfere with different pathways of AGE formation are presented. MDPI 2017-05-05 /pmc/articles/PMC5454897/ /pubmed/28475116 http://dx.doi.org/10.3390/ijms18050984 Text en © 2017 by the authors. Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).
spellingShingle Review
Brings, Sebastian
Fleming, Thomas
Freichel, Marc
Muckenthaler, Martina U.
Herzig, Stephan
Nawroth, Peter P.
Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention
title Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention
title_full Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention
title_fullStr Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention
title_full_unstemmed Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention
title_short Dicarbonyls and Advanced Glycation End-Products in the Development of Diabetic Complications and Targets for Intervention
title_sort dicarbonyls and advanced glycation end-products in the development of diabetic complications and targets for intervention
topic Review
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5454897/
https://www.ncbi.nlm.nih.gov/pubmed/28475116
http://dx.doi.org/10.3390/ijms18050984
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