A membrane-bound lectin responsive to monocytic maturation in the promyelocytic leukemia cell line hl-60

Elisabeth Paietta, Robert Gallagher, Peter H. Wiernik, Richard J. Stockert

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6 Scopus citations


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-acetylnenraminic 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 and 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 orosomncoid-binding activity. Induction of monocyte/macrophage differentiation of these sublines upregulates lectin activity to the level seen in induced wild-type cells.

Original languageEnglish (US)
Pages (from-to)280-287
Number of pages8
JournalCancer Research
Issue number2
StatePublished - Jan 1 1988
Externally publishedYes


ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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