Mapping by monoclonal antibody detection of glycosaminoglycans in connective tissues.

Research output: Contribution to journalJournal articleResearchpeer-review

Chondroitin sulphate proteoglycans are widespread connective tissue components and chemical analysis of cartilage and other proteoglycans has demonstrated molecular speciation involving the degree and position of sulphation of the carbohydrate chains. This may, in turn, affect the properties of the glycosaminoglycan (GAG), particularly with respect to self-association and interactions with other extracellular matrix components. Interactions with specific molecules from different connective tissue types, such as the collagens and their associated glycoproteins, 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.
Original languageEnglish
Issue number5952
Pages (from-to)650-2
Number of pages2
Publication statusPublished - 1984

Bibliographical note

Keywords: Animals; Antibodies, Monoclonal; Antibody Specificity; Chondroitin; Chondroitin Sulfates; Connective Tissue; Glycosaminoglycans; Proteoglycans; Rats; Tissue Distribution

ID: 5167735