Advanced glycation endproducts interfere with adhesion and neurite outgrowth.

Advanced glycation endproducts (AGEs) represent a non-enzymatic posttranslational protein modification. AGEs are generated by a series of chemical reactions of free reducing monosaccharides, such as glucose, fructose or metabolites of the monosaccharide metabolism with amino groups of proteins. Afte...

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Main Authors: Dorit Bennmann, Rüdiger Horstkorte, Britt Hofmann, Kathleen Jacobs, Alexander Navarrete-Santos, Andreas Simm, Kaya Bork, Vinayaga S Gnanapragassam
Format: Article
Language:English
Published: Public Library of Science (PLoS) 2014-01-01
Series:PLoS ONE
Online Access:http://europepmc.org/articles/PMC4227844?pdf=render
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author Dorit Bennmann
Rüdiger Horstkorte
Britt Hofmann
Kathleen Jacobs
Alexander Navarrete-Santos
Andreas Simm
Kaya Bork
Vinayaga S Gnanapragassam
author_facet Dorit Bennmann
Rüdiger Horstkorte
Britt Hofmann
Kathleen Jacobs
Alexander Navarrete-Santos
Andreas Simm
Kaya Bork
Vinayaga S Gnanapragassam
author_sort Dorit Bennmann
collection DOAJ
description Advanced glycation endproducts (AGEs) represent a non-enzymatic posttranslational protein modification. AGEs are generated by a series of chemical reactions of free reducing monosaccharides, such as glucose, fructose or metabolites of the monosaccharide metabolism with amino groups of proteins. After oxidation, dehydration and condensation, stable AGE-modifications are formed. AGE-modified proteins accumulate in all cells and tissues as a normal feature of ageing and correlate with the glucose concentration in the blood. AGEs are increased in diabetic patients and play a significant role in the pathogenesis of most age-related neural disorders, such as Alzheimer's disease. We examined the role of AGEs on neurite outgrowth of PC12 cells. We induced the formation of AGEs using the reactive carbonyl compound methylglyoxal (MGO) as a physiological metabolite of glucose. We found that AGE-modification of laminin or collagen interfered with adhesion but not with neurite outgrowth of PC12 cells. Furthermore, the AGE-modification of PC12 cell proteins reduced NGF-induced neurite outgrowth. In conclusion, our data show that AGEs negatively influence neural plasticity.
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spelling doaj.art-e3632f4142484439943b56518dbb4b232022-12-22T01:14:11ZengPublic Library of Science (PLoS)PLoS ONE1932-62032014-01-01911e11211510.1371/journal.pone.0112115Advanced glycation endproducts interfere with adhesion and neurite outgrowth.Dorit BennmannRüdiger HorstkorteBritt HofmannKathleen JacobsAlexander Navarrete-SantosAndreas SimmKaya BorkVinayaga S GnanapragassamAdvanced glycation endproducts (AGEs) represent a non-enzymatic posttranslational protein modification. AGEs are generated by a series of chemical reactions of free reducing monosaccharides, such as glucose, fructose or metabolites of the monosaccharide metabolism with amino groups of proteins. After oxidation, dehydration and condensation, stable AGE-modifications are formed. AGE-modified proteins accumulate in all cells and tissues as a normal feature of ageing and correlate with the glucose concentration in the blood. AGEs are increased in diabetic patients and play a significant role in the pathogenesis of most age-related neural disorders, such as Alzheimer's disease. We examined the role of AGEs on neurite outgrowth of PC12 cells. We induced the formation of AGEs using the reactive carbonyl compound methylglyoxal (MGO) as a physiological metabolite of glucose. We found that AGE-modification of laminin or collagen interfered with adhesion but not with neurite outgrowth of PC12 cells. Furthermore, the AGE-modification of PC12 cell proteins reduced NGF-induced neurite outgrowth. In conclusion, our data show that AGEs negatively influence neural plasticity.http://europepmc.org/articles/PMC4227844?pdf=render
spellingShingle Dorit Bennmann
Rüdiger Horstkorte
Britt Hofmann
Kathleen Jacobs
Alexander Navarrete-Santos
Andreas Simm
Kaya Bork
Vinayaga S Gnanapragassam
Advanced glycation endproducts interfere with adhesion and neurite outgrowth.
PLoS ONE
title Advanced glycation endproducts interfere with adhesion and neurite outgrowth.
title_full Advanced glycation endproducts interfere with adhesion and neurite outgrowth.
title_fullStr Advanced glycation endproducts interfere with adhesion and neurite outgrowth.
title_full_unstemmed Advanced glycation endproducts interfere with adhesion and neurite outgrowth.
title_short Advanced glycation endproducts interfere with adhesion and neurite outgrowth.
title_sort advanced glycation endproducts interfere with adhesion and neurite outgrowth
url http://europepmc.org/articles/PMC4227844?pdf=render
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