The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor

Martin Steegmaler, Agneta Levinovitz, Sandra Isenmann, Eric Borges, Martin Lenter, Hans P. Kocher, Beate Kleuser, Dletmar Vestweber

Research output: Contribution to journalArticle

312 Citations (Scopus)


E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca2+-dependent lectin1–3. We have recently identified a 150K glycoprotein as the major ligand for E-selectin on myeloid cells, using a recombinant antibody-like form of mouse E-selectin as an affinity probe4, 5. Here we report the isolation of a mouse complementary DNA for this E-selectin ligand (ESL-1). The predicted amino-acid sequence of ESL-1 is 94% identical (over 1, 078 amino acids) to the recently identified chicken cysteine-rich fibroblast growth-factor receptor6, except for a unique 70-amino-acid amino-terminal domain of mature ESL-1. Fucosylation of ESL-1 is imperative for affinity isolation with E-selectin-IgG. A fucosylated, recombinant antibody-like form of ESL-1, but not of L-selectin, supports adhesion of E-selectin-transfected Chinese hamster ovary cells. Antibodies against ESL-1 block the binding of mouse myeloid cells to E-selectin. ESL-1, with a structure essentially identical to that of a receptor, thus functions as a cell adhesion ligand of E-selectin.

Original languageEnglish
Pages (from-to)615-620
Number of pages6
Issue number6515
Publication statusPublished - 16 Feb 1995

ASJC Scopus subject areas

  • General

Cite this

Steegmaler, M., Levinovitz, A., Isenmann, S., Borges, E., Lenter, M., Kocher, H. P., ... Vestweber, D. (1995). The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor. Nature, 373(6515), 615-620.