An tibodies Against Human Neutrophil LECAM - 1 ( LAM - l / Leu - 8 / DREG - 56 antigen ) and Endothelial Cell ELAM - 1 Inhibit a Common CD 18 - Independent Adhesion Pathway In Vitro

نویسندگان

  • Takashi Kei Kishimoto
  • Aaron Warnock
  • Mark A. Jutila
چکیده

Neutrophil adhesion to interleukin-1 (IL-1)-stimulated human umbilical vein endothelial cells (HUVEC) involves the CD18 family of leukocyte integrins (lymphocyte function-associated antigen-1 [LFA-11, Mac-1, and ~150.95) and LECAM-1 (DREG-56/LEU-8/LAM-l antigen) on neutrophils and intercellular adhesion molecule-l (ICAM-l) and endothelial leukocyte adhesion molecule-1 (ELAM-1) on the endothelium. In this study, we compare CD18-independent adhesion pathways mediated by neutrophil LECAM-1 and endothelial ELAM-1 and find that these two pathways overlap in a variety of assays: (1) anti-LECAM-1 and anti-ELAM-I monoclonal antibody (MoAb) inhibit neutrophil binding to HUVEC, and the inhibitory effect is not additive; (2) anti-LECAM-1 MoAb, like anti-ELAM-1 MoAb, inhibits neutrophil binding to HUVEC stimulated for 3 hours with IL-1, but not to HUVEC

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Antibodies against human neutrophil LECAM-1 (LAM-1/Leu-8/DREG-56 antigen) and endothelial cell ELAM-1 inhibit a common CD18-independent adhesion pathway in vitro.

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تاریخ انتشار 2003