The cell-surface proteins of HL-60 human promyelocytic leukemia cells have been compared to those of normal human neutrophils. Proteins of HL-60 cells surface labeled with 125I differed markedly from those of normal neutrophils, as shown by immunoprecipitation and polyacrylamide electrophoresis. Differentiation of HL-60 cells by treatment with dimethylformamide, trans-retinoic acid, or 12-O-tetradecanoylphorbol acetate did not modify the predominant surface-labeled proteins of HL-60 cells to produce a pattern similar to that of normal, mature neutrophils. However, the agents did induce greater quantities of minor cell-surface proteins immunoprecipitated by hyperimmune anti-human neutrophil serum. These immunoprecipitated proteins resembled several of the surface-labeled polypeptides of normal human neutrophils.
Bibliographical noteFunding Information:
We thank Dr. H. S. Shin for the use of the cyto-centrifuge and Dr. M. Strand and Dr. E. Schmell for their review of this manuscript. The expert assistance of Mrs. Linda Poole and Mrs. Mimi Pudelko in the preparation of the manuscript is also acknowledged. The research was supported by National Institute of Health Grants ROlCA19471 and ROl GM31163 Keith M. Skubitz is a Postdoctoral Fellow supported by Training Grant 5 T32 CA09243.