Identification of a glycoprotein ligand for E-selectin on mouse myeloid cells

A. Levinovitz, J. Muhlhoff, S. Isenmann, D. Vestweber

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E-selectin is an inducible endothelial cell adhesion molecule for neutrophils which functions as a Ca2+-dependent lectin. Using a recombinant, antibody-like form of mouse E-selectin, we have searched for glycoprotein ligands on mouse neutrophils and the neutrophil progenitor cell line 32D cl 3. We have identified a 150-kD glycoprotein as the only protein which could be affinity-isolated with soluble E-selectin from [35S]methionine/[35S]cysteine-labeled 32D cl 3 cells. Binding of this protein was strictly Ca2+-dependent, was blocked by a cell adhesion- blocking mAb against mouse E-selectin, and required the presence of sialic acid on the 150-kD ligand. This glycoprotein was also affinity-isolated from mature neutrophils, in addition to a minor component at 250 kD, but could not be isolated from several other non-myeloid cell lines. The 150-kD glycoprotein was the only protein from 32D cl 3 cells, which was detectable by silverstaining after a one-step affinity-isolation.

Original languageEnglish
Pages (from-to)449-459
Number of pages11
JournalJournal of Cell Biology
Issue number2
Publication statusPublished or Issued - 1993
Externally publishedYes

ASJC Scopus subject areas

  • Cell Biology

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