ABSTRACT
One type of large proteoglycan and three types of small proteoglycans (decorin, decorin-subtype, and biglycan) were purified by chromatography, and alpha-elastin was isolated by alkali treatment from human yellow ligaments taken at the time of operation. The interaction of the proteoglycans with immobilized alpha-elastin on a sensor was analyzed by surface plasmon resonance, and we confirmed that each of the small proteoglycans exhibited a specific binding to alpha-elastin. The binding sites of small proteoglycans were contained in the protein cores. In addition, the differences in the interaction of the small proteoglycans with alpha-elastin of normal and ossified ligaments were compared. The interactions of the small proteoglycans with alpha-elastin of the ossified ligaments were lower than those with alpha-elastin of the normal ligaments. In the ossified ligaments, neodesmosine, one of the cross-linking amino acids, was significantly less than in the normal ligaments (p < .05).
Subject(s)
Elastin/metabolism , Extracellular Matrix/physiology , Ligamentum Flavum/chemistry , Ligamentum Flavum/cytology , Proteoglycans/metabolism , Adolescent , Adult , Aged , Aged, 80 and over , Amino Acids/analysis , Biglycan , Binding Sites , Decorin , Electrophoresis, Polyacrylamide Gel , Extracellular Matrix Proteins , Humans , Middle Aged , Ossification, Heterotopic/physiopathology , Protein Binding , Spine , Surface Plasmon ResonanceABSTRACT
The glycosaminoglycan chain of decorin from human spinal ligaments was digested using the hydrolysis of bovine testicular hyaluronidase. As a result, decorin with hexasaccharide, octasaccharide, and decasaccharide including the linkage region, GlcA-Gal-Gal-Xyl, was obtained. The obtained decorin as an acceptor and hyaluronic acid as a donor were incubated with bovine testicular hyaluronidase under the condition of transglycosylation reaction. The transglycosylation reaction product had hexasaccharide to triacontasaccharide. Judging from the analysis of glycosaminoglycan chain in the transglycosylation reaction product, it was confirmed that hyaluronic acid chain as a donor was transferred to the retained glycosaminoglycan chain of decorin as an acceptor. Similarly, it was possible to reconstruct the glycosaminoglycan chain in decorin to chondroitin, chondroitin 4-sulfate or chondroitin 6-sulfate. Therefore, we succeeded in synthesizing an artificial family of decorins.
