University of Oulu

Rieppo L, Kokkonen HT, Kulmala KM, et al; Infrared microspectroscopic determination of collagen cross-links in articular cartilage. J. Biomed. Opt. 0001;22(3):035007. doi:10.1117/1.JBO.22.3.035007.

Infrared microspectroscopic determination of collagen cross-links in articular cartilage

Saved in:
Author: Rieppo, Lassi1,2; Kokkonen, Harri T.3; Kulmala, Katariina A. M.2;
Organizations: 1University of Oulu, Research Unit of Medical Imaging, Physics and Technology, Faculty of Medicine, Oulu, Finland
2University of Eastern Finland, Department of Applied Physics, Kuopio, Finland
3South Karelia Central Hospital, Department of Radiology, Lappeenranta, Finland
4University of Jyväskylä, Department of Health Sciences, Jyväskylä, Finland
5Umeå University, Department of Integrative Medical Biology, Umeå, Sweden
6Health Science Center of Xi’an Jiaotong University, School of Public Health, Key Laboratory of Trace Elements and Endemic Diseases, National Health and Family Planning Commission, Xi’an, China
7Kuopio University Hospital, Diagnostic Imaging Center, Kuopio, Finland
8Oulu University Hospital, Department of Diagnostic Radiology, Oulu, Finland
9University of Oulu and Oulu University Hospital, Medical Research Center Oulu, Oulu, Finland
Format: article
Version: published version
Access: open
Online Access: PDF Full Text (PDF, 1.2 MB)
Persistent link:
Language: English
Published: SPIE, 2017
Publish Date: 2017-05-22


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.

see all

Series: Journal of biomedical optics
ISSN: 1083-3668
ISSN-E: 1560-2281
ISSN-L: 1083-3668
Volume: 22
Issue: 3
Article number: 035007
DOI: 10.1117/1.JBO.22.3.035007
Type of Publication: A1 Journal article – refereed
Field of Science: 217 Medical engineering
Funding: The financial support from the Academy of Finland (Grant Nos. 268378 and 273571); Sigrid Juselius Foundation; European Research Council under the European Union’s Seventh Framework Programme (FP/2007-2013)/ERC Grant Agreement no. 336267; the strategic funding of the University of Oulu; and the strategic funding of the University of Eastern Finland is acknowledged. The funding bodies had no role in the study design, implementation, or writing of the manuscript.
EU Grant Number: (336267) 3D-OA-HISTO - Development of 3D Histopathological Grading of Osteoarthritis
Academy of Finland Grant Number: 268378
Detailed Information: 268378 (Academy of Finland Funding decision)
273571 (Academy of Finland Funding decision)
Copyright information: © 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.