Changes in collagen cross-linking of articular cartilage are revealed by spectral reflectance imaging

Excessive cross-linking of collagen during aging may contribute to degeneration of articular cartilage. Traditionally, the amount of cross-links is derived by using destructive high-performance liquid chromatography (HPLC). However, a sensitive, nondestructive method could help to evaluate tissue in...

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Published in2012 25th IEEE International Symposium on Computer-Based Medical Systems (CBMS) pp. 1 - 4
Main Authors Kinnunen, Jussi, Kokkonen, Harri T., Kovanen, Vuokko, Hauta-Kasari, Markku, Vahimaa, Pasi, Jurvelin, Jukka S.
Format Conference Proceeding
LanguageEnglish
Published IEEE 01.06.2012
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Summary:Excessive cross-linking of collagen during aging may contribute to degeneration of articular cartilage. Traditionally, the amount of cross-links is derived by using destructive high-performance liquid chromatography (HPLC). However, a sensitive, nondestructive method could help to evaluate tissue integrity, including cross-links. We increased collagen cross-linking in bovine articular cartilage by controlled threose incubation. During the incubation, optical spectral reflectance images of the samples were captured and related to HPLC results using regression analysis. Significant correlations with reflectance and cross-links were observed. When further developed the optical method may enable nondestructive evaluation of cross-links in vivo through a clinical arthroscope.
ISBN:9781467320498
1467320498
ISSN:1063-7125
DOI:10.1109/CBMS.2012.6266357