Regulation of leukocyte rolling and adhesion to high endothelial venules through the cytoplasmic domain of L-selectin.

Journal Article

L-selectin (leukocyte adhesion molecule 1/MEL-14), a member of the selectin family of cell adhesion molecules, mediates leukocyte rolling and leukocyte adhesion to endothelium at sites of inflammation. In addition, L-selectin mediates the binding of lymphocytes to high endothelial venules (HEV) of peripheral lymph nodes. The strong amino acid sequence conservation of the cytoplasmic domain of L-selectin between humans and mice suggests an important role for this region. Deletion of the COOH-terminal 11 amino acids from the approximately 17 amino acid cytoplasmic domain of L-selectin eliminated binding of lymphocytes to HEV in the in vitro frozen section assay, and also abolished leukocyte rolling in vivo in exteriorized rat mesenteric venules, but did not alter the lectin activity of L-selectin. Pretreatment of cells with cytochalasin B, which disrupts actin microfilaments, also abolished adhesion without affecting carbohydrate recognition. Therefore, the cytoplasmic domain of L-selectin regulates leukocyte adhesion to endothelium independent of ligand recognition, by controlling cytoskeletal interactions and/or receptor avidity.

Full Text

Duke Authors

Cited Authors

  • Kansas, GS; Ley, K; Munro, JM; Tedder, TF

Published Date

  • March 1, 1993

Published In

Volume / Issue

  • 177 / 3

Start / End Page

  • 833 - 838

PubMed ID

  • 7679710

International Standard Serial Number (ISSN)

  • 0022-1007

Language

  • eng

Conference Location

  • United States