Abstract
Chondroitin sulphate proteoglycans are widespread connective tissue components1–4 and chemical analysis of cartilage and other proteoglycans has demonstrated molecular speciation involving the degree and position of sulphation of the carbohydrate chains5,6. This may, in turn, affect the properties of the glycpsaminoglycan (GAG), particularly with respect to self-association and interactions with other extracellular matrix components6,7. Interactions with specific molecules from different connective tissue types, such as the collagens8,9 and their associated glycoproteins10,11, could be favoured by particular charge organizations on the GAG molecule endowed by the sulphate groups. So far, it has not been possible to identify and map chondroitins of differing sulphation in tissues, but we have now raised three monoclonal antibodies which specifically recognize unsulphated, 4-sulphated and 6-sulphated chondroitin and dermatan sulphate. These provide novel opportunities to study the in vivo distribution of chondroitin sulphate proteoglycans. We demonstrate that chondroitin sulphates exhibit remarkable connective tissue specificity and furthermore provide evidence that some proteoglycans may predominantly carry only one type of chondroitin sulphate chain.
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Couchman, J., Caterson, B., Christner, J. et al. Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues. Nature 307, 650–652 (1984). https://doi.org/10.1038/307650a0
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DOI: https://doi.org/10.1038/307650a0
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