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Elam-1 mediates cell-adhesion by recognition of a carbohydrate ligand, sialyl-lex

Academic Article
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Overview

authors

  • Phillips, M. L.
  • Nudelman, E.
  • Gaeta, F. C. A.
  • Perez, M.
  • Singhal, A. K.
  • Hakomori, S. I.
  • Paulson, James

publication date

  • November 1990

journal

  • Science  Journal

abstract

  • Recruitment of neutrophils to sites of inflammation is mediated in part by endothelial leukocyte adhesion molecule-1 (ELAM-1), which is expressed on activated endothelial cells of the blood vessel walls. ELAM-1 is a member of the LEC-CAM or selectin family of adhesion molecules that contain a lectin motif thought to recognize carbohydrate ligands. In this report, cell adhesion by ELAM-1 is shown to be mediated by a carbohydrate ligand, sialyl-Lewis X (SLex; NeuAc alpha 2,3Gal beta 1,4(Fuc alpha 1,3)-GlcNAc-), a terminal structure found on cell-surface glycoprotein and glycolipid carbohydrate groups of neutrophils.

subject areas

  • Animals
  • Antibodies, Monoclonal
  • Antigens, CD15
  • Carbohydrate Conformation
  • Carbohydrate Sequence
  • Cell Adhesion
  • Cell Adhesion Molecules
  • Cell Line
  • Cricetinae
  • E-Selectin
  • Glycosylation
  • Humans
  • Ligands
  • Molecular Sequence Data
  • Neuraminidase
  • Neutrophils
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Identity

International Standard Serial Number (ISSN)

  • 0036-8075

Digital Object Identifier (DOI)

  • 10.1126/science.1701274

PubMed ID

  • 1701274
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Additional Document Info

start page

  • 1130

end page

  • 1132

volume

  • 250

issue

  • 4984

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