| First Author | Steegmaier M | Year | 1995 |
| Journal | Nature | Volume | 373 |
| Issue | 6515 | Pages | 615-20 |
| PubMed ID | 7531823 | Mgi Jnum | J:25676 |
| Mgi Id | MGI:73388 | Doi | 10.1038/373615a0 |
| Citation | Steegmaier M, et al. (1995) The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor. Nature 373(6515):615-20 |
| abstractText | E-SELECTIN is an inducible cell-adhesion molecule on endothelial cells, which mediates the binding of neutrophils and functions as a Ca(2+)-dependent lectin. 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. 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 receptor, except for a unique 70-amino-acid aminoterminal 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. |
