6533b86dfe1ef96bd12caa01

RESEARCH PRODUCT

Infrared microspectroscopic determination of collagen cross-links in articular cartilage

Simo SaarakkalaK.a.m. KulmalaHarri T. KokkonenJuha TöyräsLassi RieppoVuokko KovanenMikko J. Lammi

subject

0301 basic medicineCartilage ArticularGlycation End Products AdvancedcollagenSpectrophotometry InfraredPROTEOGLYCAN01 natural sciencesHigh-performance liquid chromatographychemistry.chemical_compoundBiomedicinsk laboratorievetenskap/teknologiPartial least squares regressionBiomedical Laboratory Science/Technologyinfrared spectroscopyPyridinolineThreoseChemistryMedicinsk bildbehandlingSTIFFNESSinfrapunaspektroskopiata3141AnatomyAtomic and Molecular Physics and OpticsDIFFUSIONElectronic Optical and Magnetic Materialsmedicine.anatomical_structuremultivariate analysisGLYCATION END-PRODUCTSNONENZYMATIC GLYCATIONBiomedical EngineeringInfrared spectroscopyI COLLAGENFORMALIN FIXATIONcross-linksOrthopaedicsBiomaterials03 medical and health sciencesmedicineAnimalsarticular cartilageFourier transform infrared spectroscopyPentosidineLeast-Squares Analysista217ChromatographyCartilage010401 analytical chemistry3126 Surgery anesthesiology intensive care radiology0104 chemical sciencesMedical Image Processing030104 developmental biologyOrtopedi1182 Biochemistry cell and molecular biologyCattle

description

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

yearjournalcountryeditionlanguage
2017-01-01Journal of Biomedical Optics
10.1117/1.jbo.22.3.035007https://doi.org/10.1117/1.JBO.22.3.035007