Lectins are known to be sugar-binding proteins found in plant extracts. Thirteen types of fluorescence isothiocyanate-conjugated lectins, Urex europaeus 1 (UEA-1), Arachis hypogaea (PNA), Griffonia simplicifolia 1 (GS-1), Dolichos biflorus (DBA, Glycine max (SBA), Ricinus communis 1 (RCA-1), Maclura pomifera (MPA), Canavalia ensiformis (Con-A), Griffonia simplicifolia 2 (GS-1), Triticum vulgalis (WGA), Lens culinaris (LCH), Limulus polyphemus (LPA) and Helix pomatia (HP) were used for revealing histochemical lectin bindings on the osteoarthritic articular cartilage.
Cartilage tissues on loaded areas were fixed with 95% cooled alcohol, and paraffin-embedded. methods were used. In the results WGA, LCH and Con-A were positively stained in the cytoplasm and pericellular matrix of the cartilage. In the glucose-specific lectins, no differences were found between osteoarthritic (OA) cartilage and normal control (NC), while in the galactose-specific lectins, MPA, RCA-1 and GS-1 were stained positively and DBA slightly on the OA cartilage, but not on the NC.
Cartilage matrices were thus shown to bind specifically with WGA, LCH, Con-A and GS-2. In the glucose-specific lectins, OA cartilage matrices were bound more specifically than those of normal control. In the galactose-specific lectins, osteoarthritic cartilage matrices were bound RCA-1 partially, but there were no differences between OA cartilage matrices and NC.
This study suggests that since varied lectin binding was seen on the articular cartilage, OA cartilage is bound with lectins stronger than with normals, and, the contents of the carbohydrate component are higher than in the normal control.
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