Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model.
Fiche publication
Date publication
février 2016
Journal
Oncotarget
Auteurs
Membres identifiés du Cancéropôle Est :
Pr PIOT Olivier, Pr SOCKALINGUM Ganesh, Dr TERRYN Christine
Tous les auteurs :
Guilbert M, Roig B, Terryn C, Garnotel R, Jeannesson P, Sockalingum GD, Manfait M, Perraut F, Dinten JM, Koenig A, Piot O
Lien Pubmed
Résumé
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.
Mots clés
Aging, physiology, Animals, Collagen Type I, metabolism, Extracellular Matrix, chemistry, Imaging, Three-Dimensional, methods, Male, Microscopy, Confocal, methods, Microscopy, Interference, methods, Rats, Rats, Sprague-Dawley, Spectroscopy, Fourier Transform Infrared
Référence
Oncotarget. 2016 Feb;7(8):8546-55