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dc.contributor.authorRieppo, Lassi
dc.contributor.authorKokkonen, Harri T.
dc.contributor.authorKulmala, Katariina A. M.
dc.contributor.authorKovanen, Vuokko
dc.contributor.authorLammi, Mikko J.
dc.contributor.authorTöyräs, Juha
dc.contributor.authorSaarakkala, Simo
dc.date.accessioned2017-03-29T06:45:56Z
dc.date.available2017-03-29T06:45:56Z
dc.date.issued2017
dc.identifier.citationRieppo, 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. <i>Journal of Biomedical Optics</i>, <i>22</i>(3), Article 035007. <a href="https://doi.org/10.1117/1.JBO.22.3.035007" target="_blank">https://doi.org/10.1117/1.JBO.22.3.035007</a>
dc.identifier.otherCONVID_26918090
dc.identifier.otherTUTKAID_73316
dc.identifier.urihttps://jyx.jyu.fi/handle/123456789/53394
dc.description.abstractCollagen 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 ¼ 27) were treated with threose to increase the collagen cross-linking while the other half (n ¼ 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 ¼ 0.84 (p < 0.001), r ¼ 0.87 (p < 0.001) and r ¼ 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.
dc.language.isoeng
dc.publisherSPIE - International Society for Optical Engineering
dc.relation.ispartofseriesJournal of Biomedical Optics
dc.subject.otherarticular cartilage
dc.subject.othercollagen
dc.subject.othercross-links
dc.subject.othermultivariate analysis
dc.titleInfrared microspectroscopic determination of collagen cross-links in articular cartilage
dc.typearticle
dc.identifier.urnURN:NBN:fi:jyu-201703231739
dc.contributor.laitosLiikuntatieteellinen tiedekuntafi
dc.contributor.laitosFaculty of Sport and Health Sciencesen
dc.contributor.oppiaineGerontologia ja kansanterveysfi
dc.contributor.oppiaineGerontology and Public Healthen
dc.type.urihttp://purl.org/eprint/type/JournalArticle
dc.date.updated2017-03-23T16:15:07Z
dc.type.coarjournal article
dc.description.reviewstatuspeerReviewed
dc.relation.issn1083-3668
dc.relation.numberinseries3
dc.relation.volume22
dc.type.versionpublishedVersion
dc.rights.copyright© The Authors. Published by SPIE under a Creative Commons Attribution 3.0 Unported License.
dc.rights.accesslevelopenAccessfi
dc.subject.ysoinfrapunaspektroskopia
jyx.subject.urihttp://www.yso.fi/onto/yso/p38871
dc.rights.urlhttps://creativecommons.org/licenses/by/3.0/
dc.relation.doi10.1117/1.JBO.22.3.035007


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© The Authors. Published by SPIE under a Creative Commons Attribution 3.0 Unported License.
Except where otherwise noted, this item's license is described as © The Authors. Published by SPIE under a Creative Commons Attribution 3.0 Unported License.