dc.contributor.author | Rieppo L | |
dc.contributor.author | Kokkonen HT | |
dc.contributor.author | Kulmala KAM | |
dc.contributor.author | Kovanen V | |
dc.contributor.author | Lammi MJ | |
dc.contributor.author | Töyräs J | |
dc.contributor.author | Saarakkala S | |
dc.date.accessioned | 2017-10-30T12:06:39Z | |
dc.date.available | 2017-10-30T12:06:39Z | |
dc.date.issued | 2017 | |
dc.identifier.uri | https://erepo.uef.fi/handle/123456789/4427 | |
dc.description.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 | en |
dc.language.iso | EN | en |
dc.publisher | SPIE Intl Soc Optical Eng | en |
dc.relation.ispartofseries | Journal of Biomedical Optics | en |
dc.relation.uri | http://dx.doi.org/10.1117/1.JBO.22.3.035007 | en |
dc.rights | CC BY 3.0 | |
dc.subject | articular cartilage | en |
dc.subject | collagen | en |
dc.subject | cross-links | en |
dc.subject | infrared spectroscopy | en |
dc.subject | multivariate analysis | en |
dc.title | Infrared microspectroscopic determination of collagen cross-links in articular cartilage | en |
dc.description.version | published version | en |
dc.contributor.department | Department of Applied Physics, activities | en |
uef.solecris.id | 46985795 | en |
dc.type.publication | info:eu-repo/semantics/article | en |
dc.relation.doi | 10.1117/1.JBO.22.3.035007 | en |
dc.description.reviewstatus | peerReviewed | en |
dc.relation.articlenumber | 035007 | |
dc.relation.issn | 1083-3668 | en |
dc.relation.issue | 3 | en |
dc.relation.volume | 22 | en |
dc.rights.accesslevel | openAccess | en |
dc.type.okm | A1 | en |
dc.type.version | info:eu-repo/semantics/publishedVersion | en |
dc.rights.copyright | © Authors | |
dc.type.displayType | article | en |
dc.type.displayType | artikkeli | fi |
dc.rights.url | https://creativecommons.org/licenses/by/3.0/ | |