Structural characterization of chick embryonic skeletal muscle chondroitin sulfate proteoglycan

Embryonic chick skeletal muscle has been shown to synthesize a distinct proteoglycan of large size with relatively large, highly 6-sulfated chondroitin sulfate glycosaminoglycans. Further analysis of these proteoglycans indicates that tryptic digestion gives rise to fragments with an average of two chondroitin sulfate chains per peptide. The skeletal muscle chondroitin sulfate proteoglycan also contains oligosaccharides whose characteristics suggest the presence of both O-linked and N-linked oligosaccharides. These characteristics include the average hydrodynamic size of the oligosaccharides as well as their localization. Approximately 10% of the putative O-linked oligosaccharides reside on the same tryptic fragments which contain the chondroitin sulfate chains, while the presumptive N-linked oligosaccharides appear to be present at sites distant from the chondroitin sulfate. Further support for this identification comes from radioisotopic labeling with [3H]mannose, which is incorporated exclusively into the putative N-linked oligosaccharides. Some of the O-linked oligosaccharides which are not in close apposition to the chondroitin sulfate seem to occur in clusters. The skeletal muscle chondroitin sulfate proteoglycan has the ability to interact in a link protein-stabilized fashion with hyaluronic acid. This ability as well as the estimated number of chondroitin sulfate chains per cluster and the estimated number of oligosaccharides per chondroitin sulfate chain have implications about the structure of the core protein of the skeletal muscle proteoglycan. The information presented is used to construct a model of these molecules; with this detailed model, attention can now be directed at other aspects of the skeletal muscle chondroitin sulfate proteoglycan, such as its role in myogenesis.