| Abstract: | The H-2K and H-2D proteins encoded by the K and D region of the major histocompatibility complex of the mouse were isolated by immunoprecipitation with specific antisera and resolved by two-dimensional gel electrophoresis. Of these two polypeptides, the H-2Dk glycoproteins isolated from macrophages of C3H/HeHa mice exhibit distinct cell surface and cytoplasmic forms although they share a strong degree of homology in the polypeptide backbone. Structurally they differ in their oligosaccharide structures. The structure of the oligosaccharides on the intracellular forms is of the high mannose type while the same structures on the cell surface forms are of the complex type. In the absence of all three oligosaccharide side chains, the unglycosylated polypeptides are expressed on the cell surface. In contrast, polypeptides containing one, two, or all three oligosaccharide side chains of the high mannose type are not transported to the cell surface. Cell surface expression of these glycoproteins requires processing of the oligosaccharide side chains from the high mannose form to the complex type. However, not all oligosaccharide antennae have to be terminally modified since H-2Dk glycoproteins synthesized in the presence of oligosaccharide-processing enzyme inhibitors such as swainsonine or monensin are also transported to the cell surface. H-2Dk glycoproteins containing oligosaccharide structures of the complex type but lacking terminal sialic acids are found on the cell surface, suggesting that sialylation is not required for transport. These results indicate that the oligosaccharide structures of the H-2Dk glycoproteins act to influence their cellular distribution. |
