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Infrared microspectroscopic determination of collagen cross-links in articular cartilage

Rieppo, Lassi (författare)
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
Kokkonen, Harri T. (författare)
South Karelia Central Hospital, Department of Radiology, Lappeenranta, Finland
Kulmala, Katariina A. M. (författare)
University of Eastern Finland, Department of Applied Physics, Kuopio, Finland
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Kovanen, Vuokko (författare)
University of Jyväskylä, Department of Health Sciences, Jyväskylä, Finland
Lammi, Mikko J., 1961- (författare)
Umeå universitet,Institutionen för integrativ medicinsk biologi (IMB),Health Science Center of Xi’an Jiaotong University, School of Public Health, Key Laboratory of Trace Elements and Endemic Diseases, National Health and Family Planning Commission, Xi’an, China,Chondrogenic and Osteogenic Differentiation Group
Töyräs, Juha (författare)
University of Eastern Finland, Department of Applied Physics, Kuopio, Finland; Kuopio University Hospital, Diagnostic Imaging Center, Kuopio, Finland
Saarakkala, Simo (författare)
University of Oulu, Research Unit of Medical Imaging, Physics and Technology, Faculty of Medicine, Oulu, Finland; Oulu University Hospital, Department of Diagnostic Radiology, Oulu, Finland; University of Oulu and Oulu University Hospital, Medical Research Center Oulu, Oulu, Finland
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 (creator_code:org_t)
SPIE - International Society for Optical Engineering, 2017
2017
Engelska.
Ingår i: Journal of Biomedical Optics. - : SPIE - International Society for Optical Engineering. - 1083-3668 .- 1560-2281. ; 22:3
  • Tidskriftsartikel (refereegranskat)
Abstract Ämnesord
Stäng  
  • 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.

Ämnesord

MEDICIN OCH HÄLSOVETENSKAP  -- Medicinsk bioteknologi -- Biomedicinsk laboratorievetenskap/teknologi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Medical Biotechnology -- Biomedical Laboratory Science/Technology (hsv//eng)
MEDICIN OCH HÄLSOVETENSKAP  -- Klinisk medicin -- Ortopedi (hsv//swe)
MEDICAL AND HEALTH SCIENCES  -- Clinical Medicine -- Orthopaedics (hsv//eng)
TEKNIK OCH TEKNOLOGIER  -- Medicinteknik -- Medicinsk bildbehandling (hsv//swe)
ENGINEERING AND TECHNOLOGY  -- Medical Engineering -- Medical Image Processing (hsv//eng)

Nyckelord

articular cartilage
collagen
cross-links
infrared spectroscopy
multivariate analysis
Computerized Image Analysis
datoriserad bildanalys
Orthopaedics
ortopedi

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