Changes of Noncollagenous Extracellular Matrix in Turkey Leg Tendon During Calcification
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概要
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Calcified and uncalcified portions of turkey leg tendon were analyzed for their soluble and insoluble components. The yield of the soluble fraction in 0.5 M EDTA and 4 M guanidine hydroehloride was 1.8 times higher in the uncalcified tendon than in the calcified tendon, when they were compared in total dry weight percentage of organic matrix. The contents of protein in the soluble and insoluble fraction were very similar, with about 85% (w/w) in both calcified and uncalcified tendon. However, the content of uronic acid in the soluble fraction was 3 times higher in the uncalcified tendon than in the calcified tendon, indicating that the major compositional change of the tendon during calcification was a decrease in the content of uronic acid containing proteoglycan. SDS-polyacrylamide electrophoresis of the soluble fraction from both calcified and uncalcified tendon revealed that the a and β chain of collagens from the uncalcified tendon were staincd strongly by periodic acid Schiff (PAS) staining, while the those from the calcified tendon were not. Also alcian blue staining in the SDS-PAGE and histological section both showed the presence of high molecular weight proteoglycan almost exclusively in the soluble fraction of the uncalcified turkey leg tendon. The above results indicate that during calcification ofturkey tendon, the PAS rcactive glycoprotein and high molecular weight proteoglycan are removed from the collagenous matrix, thereby a calcifiable matrix is created, on which calcium and phosphate ions from the extracellular fluid deposit to form calcified tendon.
- 硬組織再生生物学会の論文
著者
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Liu An-jun
Department Of Biochemistry School Of Dentistry Hokkaido University:sangi Co. Sapporo Laboratory
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KUBOKI Yoshinori
Department of Oral Biochemistry, School of Dentistry, Hokkaido University
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Kuboki Yoshinori
Department Of Biochemistry Hokkaido University Dental School
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