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Infrared microspectroscopic determination of collagen cross-links in articular cartilage

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Article (1.215Mb)
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published version
Date
2017
Author(s)
Rieppo L
Kokkonen HT
Kulmala KAM
Kovanen V
Lammi MJ
Töyräs J
Saarakkala S
Unique identifier
10.1117/1.JBO.22.3.035007
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Citation
Rieppo L. Kokkonen HT. Kulmala KAM. Kovanen V. Lammi MJ. Töyräs J. Saarakkala S. (2017). Infrared microspectroscopic determination of collagen cross-links in articular cartilage.  Journal of Biomedical Optics, 22 (3) , 035007. 10.1117/1.JBO.22.3.035007.
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CC BY http://creativecommons.org/licenses/by/3.0/
Abstract

Collagen forms an organized network in articular cartilage to give tensile stiffness to the tissue. Due to its long half-life, collagen is susceptible to cross-links caused by advanced glycation end-products. The current standard method for determination of cross-link concentrations in tissues is the destructive high-performance liquid chromatography (HPLC). The aim of this study was to analyze the cross-link concentrations nondestructively from standard unstained histological articular cartilage sections by using Fourier transform infrared (FTIR) microspectroscopy. Half of the bovine articular cartilage samples ( n = 27 ) were treated with threose to increase the collagen cross-linking while the other half ( n = 27 ) served as a control group. Partial least squares (PLS) regression with variable selection algorithms was used to predict the cross-link concentrations from the measured average FTIR spectra of the samples, and HPLC was used as the reference method for cross-link concentrations. The correlation coefficients between the PLS regression models and the biochemical reference values were r = 0.84 ( p < 0.001 ), r = 0.87 ( p < 0.001 ) and r = 0.92 ( p < 0.001 ) for hydroxylysyl pyridinoline (HP), lysyl pyridinoline (LP), and pentosidine (Pent) cross-links, respectively. The study demonstrated that FTIR microspectroscopy is a feasible method for investigating cross-link concentrations in articular cartilage

Subjects
articular cartilage   collagen   cross-links   infrared spectroscopy   multivariate analysis   
URI
https://erepo.uef.fi/handle/123456789/4427
Link to the original item
http://dx.doi.org/10.1117/1.JBO.22.3.035007
Publisher
SPIE Intl Soc Optical Eng
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  • Luonnontieteiden ja metsätieteiden tiedekunta [1109]
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