The sulphation pattern of glycosaminoglycan (GAG) plays a critical role in biological functions of proteoglycans. In this study, we showed that decorins from different bovine tissues present specific sulphation pattern coupled with peculiar biological activity. In order to elucidate chemical structure of decorin glycosaminoglycan chains, we improved an electrophoretic method to analyse fluorescent disaccharides from dermatan/chondroitin sulphate GAG chains. The disaccharide separation is based on minigels, and this technique was able to define the polysaccharide chain composition in terms of sulphated and not sulphated disaccharides. This approach allowed not only the measurement of few picomoles of material, but it also permits a rapid qualitative analysis of the GAG chains. Data obtained by PAGEFS indicate that the sulphation pattern of GAG is tissue specific and this finding may explain the different binding properties to von Willebrand factor of decorins.
Decorin from different bovine tissues: study of glycosaminoglycan chain by PAGEFS
VIOLA, MANUELA;KAROUSOU, EVGENIA;VIGETTI, DAVIDE;PALLOTTI, FRANCESCO;DE LUCA, GIANCARLO;PASSI, ALBERTO
2006-01-01
Abstract
The sulphation pattern of glycosaminoglycan (GAG) plays a critical role in biological functions of proteoglycans. In this study, we showed that decorins from different bovine tissues present specific sulphation pattern coupled with peculiar biological activity. In order to elucidate chemical structure of decorin glycosaminoglycan chains, we improved an electrophoretic method to analyse fluorescent disaccharides from dermatan/chondroitin sulphate GAG chains. The disaccharide separation is based on minigels, and this technique was able to define the polysaccharide chain composition in terms of sulphated and not sulphated disaccharides. This approach allowed not only the measurement of few picomoles of material, but it also permits a rapid qualitative analysis of the GAG chains. Data obtained by PAGEFS indicate that the sulphation pattern of GAG is tissue specific and this finding may explain the different binding properties to von Willebrand factor of decorins.File | Dimensione | Formato | |
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19 Decorin GAG by PAGEFS_ J PHARMAC BIOMED ANAL 2006.pdf
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