title: The E-selectin-ligand ESL-1 is a variant of a receptor for fibroblast growth factor.
abstract: 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.
authors.affiliation: Hans-Spemann-Laboratory, Max-Planck-Institute for Immunobiology, Freiburg, Germany.
authors.forename: M
authors.initials: M
authors.lastname: Steegmaier
authors.forename: A
authors.initials: A
authors.lastname: Levinovitz
authors.forename: S
authors.initials: S
authors.lastname: Isenmann
authors.forename: E
authors.initials: E
authors.lastname: Borges
authors.forename: M
authors.initials: M
authors.lastname: Lenter
authors.forename: H P
authors.initials: HP
authors.lastname: Kocher
authors.forename: B
authors.initials: B
authors.lastname: Kleuser
authors.forename: D
authors.initials: D
authors.lastname: Vestweber
mesh_terms: D000595:Amino Acid Sequence; D000818:Animals; D001483:Base Sequence; D016466:CHO Cells; D015815:Cell Adhesion Molecules / Q000378:metabolism*; D002645:Chickens; D003001:Cloning, Molecular; D006224:Cricetinae; D018076:DNA, Complementary; D019040:E-Selectin; D005643:Fucose / Q000378:metabolism; D006023:Glycoproteins / Q000737:chemistry / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D006801:Humans; D007074:Immunoglobulin G / Q000235:genetics / Q000378:metabolism; D008024:Ligands; D008562:Membrane Glycoproteins / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D051379:Mice; D008969:Molecular Sequence Data; D009504:Neutrophils / Q000378:metabolism; D011233:Precipitin Tests; D011485:Protein Binding; D017468:Receptors, Fibroblast Growth Factor / Q000737:chemistry* / Q000235:genetics / Q000302:isolation & purification* / Q000378:metabolism; D011971:Receptors, Immunologic / Q000235:genetics / Q000302:isolation & purification / Q000378:metabolism; D011993:Recombinant Fusion Proteins / Q000235:genetics / Q000378:metabolism; D017386:Sequence Homology, Amino Acid; D012795:Sialoglycoproteins; D014162:Transfection
chemical_list: D015815:Cell Adhesion Molecules; D018076:DNA, Complementary; D019040:E-Selectin; D006023:Glycoproteins; D007074:Immunoglobulin G; D008024:Ligands; D008562:Membrane Glycoproteins; D017468:Receptors, Fibroblast Growth Factor; D011971:Receptors, Immunologic; D011993:Recombinant Fusion Proteins; D012795:Sialoglycoproteins; C086711:cysteine-rich fibroblast growth factor receptor; D005643:Fucose