Infrared microspectroscopic determination of collagen cross-links in articular cartilage

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Rieppo , L , Kokkonen , H T , Kulmala , K A M , Kovanen , V , Lammi , M J , Töyräs , J & Saarakkala , S 2017 , ' Infrared microspectroscopic determination of collagen cross-links in articular cartilage ' , Journal of Biomedical Optics , vol. 22 , no. 3 , 035007 . https://doi.org/10.1117/1.JBO.22.3.035007

Title: Infrared microspectroscopic determination of collagen cross-links in articular cartilage
Author: Rieppo, Lassi; Kokkonen, Harri T.; Kulmala, Katariina A. M.; Kovanen, Vuokko; Lammi, Mikko J.; Töyräs, Juha; Saarakkala, Simo
Contributor organization: HYKS erva
Date: 2017-03
Language: eng
Number of pages: 9
Belongs to series: Journal of Biomedical Optics
ISSN: 1083-3668
DOI: https://doi.org/10.1117/1.JBO.22.3.035007
URI: http://hdl.handle.net/10138/298794
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. (C) The Authors. Published by SPIE under a Creative Commons Attribution 3.0 Unported License. Distribution or reproduction of this work in whole or in part requires full attribution of the original publication, including its DOI.
Subject: articular cartilage
collagen
cross-links
infrared spectroscopy
multivariate analysis
GLYCATION END-PRODUCTS
NONENZYMATIC GLYCATION
FORMALIN FIXATION
I COLLAGEN
PROTEOGLYCAN
DIFFUSION
STIFFNESS
1182 Biochemistry, cell and molecular biology
3126 Surgery, anesthesiology, intensive care, radiology
Peer reviewed: Yes
Usage restriction: openAccess
Self-archived version: publishedVersion


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