The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140

Louis Picker, R. Aaron Warnock, Alan R. Burns, Claire M. Doerschuk, Ellen L. Berg, Eugene C. Butchert

Research output: Contribution to journalArticle

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Abstract

LECAM-1 (leukocyte-endothelial cell adhesion molecule 1), the lymphocyte lectin ("selectin") homing receptor for peripheral lymph nodes (PLNs), participates in the earliest interactions of polymorphonuclear neutrophilic leukocytes (PMNs) with inflamed venuies. Here, we present evidence that LECAM-1 mediates this function through a novel mechanism-presentation of oligosaccharide ligands to the inducible vascular selectins endothelial-leukocyte adhesion molecule (ELAM-1) and granule membrane protein 140 (GMP-140). PMN, but not lymphocyte, LECAM-1 is modified with the vascular selectin ligand sialyl Lewis x (sLex) and specifically binds ELAM-1-transfected cells. Although only a small fraction of total cell surface sLex, LECAM-1-associated sLex appears to play a prominent role in PMN interactions with cell-associated ELAM-1 and GMP-140, as anti-LECAM-1 monoclonal antibodies or selective removal of cell surface LECAM-1 inhibits PMN binding to vascular selectin transfectants by up to 70%. The enhanced function of LECAM-1-associated sLex may reflect the striking concentration, shown here, of LECAM-1 on PMN surface microvilli, the site of initial cellular contact.

Original languageEnglish (US)
Pages (from-to)921-933
Number of pages13
JournalCell
Volume66
Issue number5
DOIs
StatePublished - Sep 6 1991
Externally publishedYes

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Selectins
E-Selectin
Endothelial cells
Cell Adhesion Molecules
Blood Vessels
Membrane Proteins
Neutrophils
Leukocytes
Endothelial Cells
Carbohydrates
Ligands
Lymphocytes
Lymphocyte Homing Receptors
Microvilli
Oligosaccharides
Lectins
Cell Communication
Monoclonal Antibodies
5-acetylneuraminyl-(2-3)-galactosyl-(1-4)-(fucopyranosyl-(1-3))-N-acetylglucosamine

ASJC Scopus subject areas

  • Cell Biology
  • Molecular Biology

Cite this

The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140. / Picker, Louis; Warnock, R. Aaron; Burns, Alan R.; Doerschuk, Claire M.; Berg, Ellen L.; Butchert, Eugene C.

In: Cell, Vol. 66, No. 5, 06.09.1991, p. 921-933.

Research output: Contribution to journalArticle

Picker, Louis ; Warnock, R. Aaron ; Burns, Alan R. ; Doerschuk, Claire M. ; Berg, Ellen L. ; Butchert, Eugene C. / The neutrophil selectin LECAM-1 presents carbohydrate ligands to the vascular selectins ELAM-1 and GMP-140. In: Cell. 1991 ; Vol. 66, No. 5. pp. 921-933.
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AB - LECAM-1 (leukocyte-endothelial cell adhesion molecule 1), the lymphocyte lectin ("selectin") homing receptor for peripheral lymph nodes (PLNs), participates in the earliest interactions of polymorphonuclear neutrophilic leukocytes (PMNs) with inflamed venuies. Here, we present evidence that LECAM-1 mediates this function through a novel mechanism-presentation of oligosaccharide ligands to the inducible vascular selectins endothelial-leukocyte adhesion molecule (ELAM-1) and granule membrane protein 140 (GMP-140). PMN, but not lymphocyte, LECAM-1 is modified with the vascular selectin ligand sialyl Lewis x (sLex) and specifically binds ELAM-1-transfected cells. Although only a small fraction of total cell surface sLex, LECAM-1-associated sLex appears to play a prominent role in PMN interactions with cell-associated ELAM-1 and GMP-140, as anti-LECAM-1 monoclonal antibodies or selective removal of cell surface LECAM-1 inhibits PMN binding to vascular selectin transfectants by up to 70%. The enhanced function of LECAM-1-associated sLex may reflect the striking concentration, shown here, of LECAM-1 on PMN surface microvilli, the site of initial cellular contact.

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