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Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model
During aging, alterations of extracellular matrix proteins contribute to various pathological phenotypes. Among these alterations, type I collagen cross-linking and associated glycation products accumulation over time detrimentally affects its physico-chemical properties, leading to alterations of t...
Autores principales: | , , , , , , , , , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Impact Journals LLC
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4890986/ https://www.ncbi.nlm.nih.gov/pubmed/26885896 http://dx.doi.org/10.18632/oncotarget.7385 |
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author | Guilbert, Marie Roig, Blandine Terryn, Christine Garnotel, Roselyne Jeannesson, Pierre Sockalingum, Ganesh D. Manfait, Michel Perraut, François Dinten, Jean-Marc Koenig, Anne Piot, Olivier |
author_facet | Guilbert, Marie Roig, Blandine Terryn, Christine Garnotel, Roselyne Jeannesson, Pierre Sockalingum, Ganesh D. Manfait, Michel Perraut, François Dinten, Jean-Marc Koenig, Anne Piot, Olivier |
author_sort | Guilbert, Marie |
collection | PubMed |
description | During aging, alterations of extracellular matrix proteins contribute to various pathological phenotypes. Among these alterations, type I collagen cross-linking and associated glycation products accumulation over time detrimentally affects its physico-chemical properties, leading to alterations of tissue biomechanical stability. Here, different-age collagen 3D matrices using non-destructive and label-free biophotonic techniques were analysed to highlight the impact of collagen I aging on 3D constructs, at macroscopic and microscopic levels. Matrices were prepared with collagens extracted from tail tendons of rats (newborns, young and old adults) to be within the physiological aging process. The data of diffuse reflectance spectroscopy reveal that aging leads to an inhibition of fibril assembly and a resulting decrease of gel density. Investigations by confocal reflectance microscopy highlight poor-fibrillar structures in oldest collagen networks most likely related to the glycation products accumulation. Complementarily, an infrared analysis brings out marked spectral variations in the Amide I profile, specific of the peptidic bond conformation and for carbohydrates vibrations as function of collagen-age. Interestingly, we also highlight an unexpected behavior for newborn collagen, exhibiting poorly-organized networks and microscopic features close to the oldest collagen. These results demonstrate that changes in collagen optical properties are relevant for investigating the incidence of aging in 3D matrix models. |
format | Online Article Text |
id | pubmed-4890986 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Impact Journals LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-48909862016-06-20 Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model Guilbert, Marie Roig, Blandine Terryn, Christine Garnotel, Roselyne Jeannesson, Pierre Sockalingum, Ganesh D. Manfait, Michel Perraut, François Dinten, Jean-Marc Koenig, Anne Piot, Olivier Oncotarget Research Paper: Gerotarget (Focus on Aging) During aging, alterations of extracellular matrix proteins contribute to various pathological phenotypes. Among these alterations, type I collagen cross-linking and associated glycation products accumulation over time detrimentally affects its physico-chemical properties, leading to alterations of tissue biomechanical stability. Here, different-age collagen 3D matrices using non-destructive and label-free biophotonic techniques were analysed to highlight the impact of collagen I aging on 3D constructs, at macroscopic and microscopic levels. Matrices were prepared with collagens extracted from tail tendons of rats (newborns, young and old adults) to be within the physiological aging process. The data of diffuse reflectance spectroscopy reveal that aging leads to an inhibition of fibril assembly and a resulting decrease of gel density. Investigations by confocal reflectance microscopy highlight poor-fibrillar structures in oldest collagen networks most likely related to the glycation products accumulation. Complementarily, an infrared analysis brings out marked spectral variations in the Amide I profile, specific of the peptidic bond conformation and for carbohydrates vibrations as function of collagen-age. Interestingly, we also highlight an unexpected behavior for newborn collagen, exhibiting poorly-organized networks and microscopic features close to the oldest collagen. These results demonstrate that changes in collagen optical properties are relevant for investigating the incidence of aging in 3D matrix models. Impact Journals LLC 2016-02-14 /pmc/articles/PMC4890986/ /pubmed/26885896 http://dx.doi.org/10.18632/oncotarget.7385 Text en Copyright: © 2016 Guilbert et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Research Paper: Gerotarget (Focus on Aging) Guilbert, Marie Roig, Blandine Terryn, Christine Garnotel, Roselyne Jeannesson, Pierre Sockalingum, Ganesh D. Manfait, Michel Perraut, François Dinten, Jean-Marc Koenig, Anne Piot, Olivier Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model |
title | Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model |
title_full | Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model |
title_fullStr | Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model |
title_full_unstemmed | Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model |
title_short | Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model |
title_sort | highlighting the impact of aging on type i collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3d matrix model |
topic | Research Paper: Gerotarget (Focus on Aging) |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC4890986/ https://www.ncbi.nlm.nih.gov/pubmed/26885896 http://dx.doi.org/10.18632/oncotarget.7385 |
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