Nature 373, 615 - 620 (16 February 1995); doi:10.1038/373615a0

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^*§

^*Hans-Spemann-Laboratory at the Max-Planek-Institute for Immunobiology, D-79108 Freiburg, Germany
^‡Sandoz Pharma Ltd, CH-4002 Basel, Switzerland
^†Present address: Department of Pathology, Huddinge University Hospital, S-14186 Huddinge, Sweden.
^§To whom correspondence should be addressed.

E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca²⁺-dependent lectin^1–3. 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 probe^4,5. 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.

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