Sulfatase‐mediated manipulation of the astrocyte‐Schwann cell interface
Quantitative biosynthetic studies with cultures highly enriched for glial fibrillary acidic protein (GFAP+) cells of neonatal mammalian brain demonstrated production of four proteoglycans: hyaluronate (HA), heparan sulphate (HS), chondroitin sulphate (CS), and dermatan sulphate (DS). The glycosaminoglycans were present in cell conditioned medium and in the cellular compartment. There were qualitative differences in the subcellular disposition of the various proteoglycans. The ratio of HS to CS/DS in cell extracts was 1:1, while in medium this ratio was 1:6. All of the glycosaminoglycans were associated with core proteins that were integral to the cell membrane and associated with the cell surface by non-covalent interactions involving glycosaminoglycans. Less than 20% of the HS was non-covalently associated with the astrocyte cell surface reflecting in part the proportionately smaller amounts of this proteoglycan released to astrocyte conditioned medium. HS released to medium was undersulphated relative to that associated with cells. The astrocyte can contribute proteoglycans to the extracellular milieu and displays cell surface proteoglycans that have the potential to provide appropriate substrates for neuron adhesion, process extension, and other cell-cell interactions.