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Infrared microspectroscopic determination of collagen cross-links in articular cartilage
University of Oulu, Research Unit of Medical Imaging, Physics and Technology, Faculty of Medicine, Oulu, Finland; University of Eastern Finland, Department of Applied Physics, Kuopio, Finland.
South Karelia Central Hospital, Department of Radiology, Lappeenranta, Finland.
University of Eastern Finland, Department of Applied Physics, Kuopio, Finland.
University of Jyväskylä, Department of Health Sciences, Jyväskylä, Finland.
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2017 (English)In: Journal of Biomedical Optics, ISSN 1083-3668, E-ISSN 1560-2281, Vol. 22, no 3, 35007Article in journal (Refereed) Published
Abstract [en]

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.

Place, publisher, year, edition, pages
2017. Vol. 22, no 3, 35007
Keyword [en]
Fourier-transform infrared spectorscopy, articular cartilage, collagen, cross-links
National Category
Biomedical Laboratory Science/Technology Orthopedics Medical Image Processing
Research subject
Computerized Image Analysis; Orthopaedics
Identifiers
URN: urn:nbn:se:umu:diva-132612DOI: 10.1117/1.JBO.22.3.035007ISI: 000397944900012PubMedID: 28290599OAI: oai:DiVA.org:umu-132612DiVA: diva2:1082870
Available from: 2017-03-19 Created: 2017-03-19 Last updated: 2017-05-12Bibliographically approved

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