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dc.contributor.authorRieppo L
dc.contributor.authorKokkonen HT
dc.contributor.authorKulmala KAM
dc.contributor.authorKovanen V
dc.contributor.authorLammi MJ
dc.contributor.authorTöyräs J
dc.contributor.authorSaarakkala S
dc.date.accessioned2017-10-30T12:06:39Z
dc.date.available2017-10-30T12:06:39Z
dc.date.issued2017
dc.identifier.urihttps://erepo.uef.fi/handle/123456789/4427
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 = 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 cartilageen
dc.language.isoENen
dc.publisherSPIE Intl Soc Optical Engen
dc.relation.ispartofseriesJournal of Biomedical Opticsen
dc.relation.urihttp://dx.doi.org/10.1117/1.JBO.22.3.035007en
dc.rightsCC BY http://creativecommons.org/licenses/by/3.0/en
dc.subjectarticular cartilageen
dc.subjectcollagenen
dc.subjectcross-linksen
dc.subjectinfrared spectroscopyen
dc.subjectmultivariate analysisen
dc.titleInfrared microspectroscopic determination of collagen cross-links in articular cartilageen
dc.description.versionpublished versionen
dc.contributor.departmentDepartment of Applied Physics, activitiesen
uef.solecris.id46985795en
dc.type.publicationinfo:eu-repo/semantics/articleen
dc.rights.accessrights© Authorsen
dc.relation.doi10.1117/1.JBO.22.3.035007en
dc.description.reviewstatuspeerRevieweden
dc.relation.articlenumber035007
dc.relation.issn1083-3668en
dc.relation.issue3en
dc.relation.volume22en
dc.rights.accesslevelopenAccessen
dc.type.okmA1en
dc.type.versioninfo:eu-repo/semantics/publishedVersionen


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