Highlighting the impact of aging on type I collagen: label-free investigation using confocal reflectance microscopy and diffuse reflectance spectroscopy in 3D matrix model

Oncotarget
Marie GuilbertOlivier Piot

Abstract

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...Continue Reading

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Citations

Jul 3, 2016·Cardiovascular Research·Antonio CannatàFrancesco S Loffredo
Apr 23, 2020·Journal of Cosmetic Dermatology·Dong Hye SuhKye Young Song
Aug 28, 2020·Frontiers in Bioengineering and Biotechnology·Yuliia SednievaLaure-Lise Gras
Feb 14, 2021·Journal of Cosmetic Dermatology·Marie MeunierRomain Reynaud

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Methods Mentioned

BETA
confocal reflectance microscopy
infrared spectroscopy
electrophoresis

Software Mentioned

ImageJ
ZEN Imaging

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