Membrane differentiation in human myeloid cells: expression of unique profiles of cell surface glycoproteins in myeloid leukemic cell lines blocked at different stages of differentiation and maturation.

Cell surface glycoprotein structures of human leukemic cell lines blocked at various stages of myeloid (granulocyte--monocyte) differentiation and maturation were characterized. Cell lines representing early stages of differentiation and maturation such as KG1a, KG1 and those representing later stages such as ML-1-3 and HL-60 were found to express discretely different sets of cell surface glycoproteins. The proteins (such as Gp130) present on mature granulocytes appear only in cell lines representing later stages of maturation. The quantity and structure of the carbohydrate chains susceptible to endo-beta-galactosidase ("lactosaminoglycan") are also significantly different among cell lines. A small quantity of essentially unbranched lactosaminoglycan is present on KG1a and KG1 cells, whereas a significant quantity of branched lactosaminoglycan is present on the more mature ML-1-3 and HL-60 cells. The process of myeloid maturation from promyeloblast to granulocyte is accompanied by the disappearance of the 105- and 95-kilodalton glycoproteins, the appearance of Gp130, and a great increase in the quantity and branching structure of lactosaminoglycan. These results are discussed together with our previous findings on erythroid differentiation and maturation.