Differences in the plasma membrane glycoproteins of cultured myeloblastoid and promyelocytic human leukemia (HL60) cells.
Since the mechanisms that control synthesis of surface and internal granule membranes are closely-related within the Golgi apparatus, we have compared the plasma membrane proteins and glycolipids of cells of the human promyelocytic line HL-60 with those of its agranular myeloblastoid variant (HL60-D), and of other human myeloid lines (KG-1a, KG-1 and ML-2). Proteolytic degradation by granule enzymes altered the protein profiles unless multiple inhibitors were included in the cell suspension before lysis and during subsequent handling of the extracts. Polyacrylamide gel electrophoretic profiles of the proteins accessible to lactoperoxidase-catalyzed 125I-labeling or to periodate [3H]-borohydride labeling, as well as those of the glycoproteins bound to and eluted from immobilized concanavalin A, showed distinct patterns. The apparent molecular weights of the two major sialylated glycoproteins were larger in cell lines with a greater content of azurophilic granules. Also, the blastic line incorporated less fucose into glycolipid and contained less complex gangliosides and neutral glycolipids than did the parent. These data demonstrate that, within the limits of this culture model, cells capable of cytoplasmic granule production express a different constellation of surface components.
D002460:Cell Line; D002462:Cell Membrane / Q000032:analysis*; D004591:Electrophoresis, Polyacrylamide Gel; D010450:Endopeptidases / Q000378:metabolism; D006017:Glycolipids / Q000032:analysis; D006023:Glycoproteins / Q000032:analysis*; D006801:Humans; D015470:Leukemia, Myeloid, Acute / Q000473:pathology*; D008970:Molecular Weight; D009195:Peroxidase / Q000378:metabolism
D006017:Glycolipids; D006023:Glycoproteins; D009195:Peroxidase; D010450:Endopeptidases