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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Public Library of Science (PLoS)
2014-01-01
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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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institution | Directory Open Access Journal |
issn | 1932-6203 |
language | English |
last_indexed | 2024-12-11T08:43:34Z |
publishDate | 2014-01-01 |
publisher | Public Library of Science (PLoS) |
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series | PLoS ONE |
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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