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A Membrane-bound Lectin Responsive to Monocytic Maturation in the Promyelocytic Leukemia Cell Line HL-60¹

The Department of Oncology, Montefiore Medical Center [E. P., R. G., P. H. W.], the Divisions of Medical Oncology [E. P., R. G., P. H. W.], and Genetic Medicine [R. J. S.], and the Liver Research Center [R. J. S.], Departments of Medicine [E. P., R. G., P. H. W., R. J. S.], and Biochemistry [R. J. S.], Albert Einstein College of Medicine, Bronx, New York

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 M_r 17,000 intracellular membrane protein. Induction of wild-type HL-60 cells into their macrophage-like counterparts by 1,25-dihydroxy-vitamin 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.

¹ This work was supported in part by Grant P30CA13330 awarded by the National Cancer Institute, Department of Health and Human Services, by a grant from the Chemotherapy Research Foundation, and by NIH Grants DK-32972, DK-34668, DK-32972, and CA42047.

² To whom requests for reprints should be addressed, at Department of Oncology, Montefiore Medical Center, 111 East 210th Street, Bronx, New York 10467.

Received 4/23/87. Revised 7/29/87. Revised 10/16/87. Accepted 10/19/87.

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