A membrane-bound lectin responsive to monocytic maturation in the promyelocytic leukemia cell line HL-60.
A novel mammalian lectin activity responsive to monocytic differentiation is described in the human promyelocytic leukemia cell line HL-60. Glycoprotein binding indicates that the lectin recognizes both N-acetylneuraminic acid and galactose-terminating biantennary oligosaccharide structures. Lectin activity is independent of calcium and appears to reside in a Mr 17,000 intracellular membrane protein. Induction of wild-type HL-60 cells into their macrophage-like counterparts by 1,25-dihydroxyvitamin D3 markedly enhances lectin activity. Induction of granulocytic differentiation by retinoic acid does not affect expression of the lectin. HL-60 sublines which are resistant to granulocytic differentiation by retinoic acid, dimethylsulfoxide, or 6-thioguanine are largely deficient in orosomucoid-binding activity. Induction of monocyte/macrophage differentiation of these sublines upregulates lectin activity to the level seen in induced wild-type cells.
D001212:Asialoglycoproteins; D001665:Binding Sites; D002454:Cell Differentiation; D006801:Humans; D037102:Lectins / Q000032:analysis* / Q000302:isolation & purification / Q000378:metabolism; D015470:Leukemia, Myeloid, Acute / Q000378:metabolism / Q000473:pathology*; D008264:Macrophages / Q000473:pathology; D009000:Monocytes / Q000473:pathology*; D009844:Oligosaccharides / Q000032:analysis; D009961:Orosomucoid / Q000031:analogs & derivatives / Q000378:metabolism; D011961:Receptors, Fc / Q000032:analysis; D017452:Receptors, IgG; D013329:Structure-Activity Relationship; D014407:Tumor Cells, Cultured
D001212:Asialoglycoproteins; D037102:Lectins; D009844:Oligosaccharides; D009961:Orosomucoid; D011961:Receptors, Fc; D017452:Receptors, IgG; C017030:asialoorosomucoid