Research Papers: Gerotarget (Focus on Aging):
Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model
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Marie Guilbert1,*, Blandine Roig2,*, Christine Terryn3, Roselyne Garnotel1, Pierre Jeannesson1, Ganesh D. Sockalingum1,3, Michel Manfait1, François Perraut2, Jean-Marc Dinten2, Anne Koenig2 and Olivier Piot1,3
1 MéDIAN-Biophotonique et Technologies pour la Santé, Université de Reims Champagne-Ardenne, CNRS UMR 7369 MEDyC, UFR de Pharmacie, SFR CAP Santé, Reims, France
2 CEA, LETI, Minatec campus, Grenoble, France
3 Plate-forme Imagerie Cellulaire et Tissulaire, Université de Reims Champagne-Ardenne, Reims, France
* These authors have contributed equally to this work
Olivier Piot, email:
Keywords: Type I collagen aging, 3D matrix, confocal reflectance microscopy, diffuse reflectance spectroscopy, ATR infrared imaging, Gerotarget
Received: September 07, 2015 Accepted: January 30, 2016 Published: February 14, 2016
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.
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