Failure to detect IL-3-binding sites on human mast cells

P. Valent, J. Besemer, Ch Sillaber, J. H. Butterfield, R. Eher, O. Majdic, K. Kishi, W. Klepetko, F. Eckersberger, K. Lechner, P. Bettelheim

Research output: Contribution to journalArticlepeer-review

92 Scopus citations


IL-3, a pleiotropic lymphokine, has been termed mast cell growth factor because it promotes growth and differentiation of murine mast cells. Murine mast cells, in turn, express cell surface receptors for IL-3. Human rIL-3 has been shown to induce proliferation and differentiation of human basophils and to activate basophils via high affinity binding sites. To investigate whether human mast cells express IL-3R, binding studies with 125I-radiolabeled human rIL-3 were performed on HMC-1, a novel human mast cell line, and on pure populations (i.e., 93 to 99% purity) of human tissue mast cells obtained with mAb and C from dispersed lung (n = 2). Unexpectedly, neither enriched human lung mast cells nor HMC-1 cells bound radiolabeled human rIL-3 specifically. Moreover, human rIL-3 failed to promote uptake of [3H]thymidine, synthesis of histamine, histamine releasability, or changes in expression of mast cell differentiation Ag (YB5B8, CD54/ ICAM-1, CD9/p24, CD33/gp67) on either human lung mast cells or HMC-1 cells. It is hypothesized that the fundamental difference in the biologic response to IL-3 between human and murine mast cells is due to a loss during evolution of mast cell high affinity IL-3 binding sites.

Original languageEnglish (US)
Pages (from-to)3432-3437
Number of pages6
JournalJournal of Immunology
Issue number10
StatePublished - Nov 15 1990

ASJC Scopus subject areas

  • Immunology and Allergy
  • Immunology


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