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The P-Selectin Glycoprotein Ligand-1 Is Important for Recruitment of Neutrophils Into Inflamed Mouse Peritoneum
Eric Borges,
Ruth Eytner,
Thomas Moll,
Martin Steegmaier,
Matthew A. Campbell,
Klaus Ley,
Horst Mossmann, and
Dietmar Vestweber
From the Institute of Cell Biology, Zentrum für Molekularbiologie der Entzündung (ZMBE), University of Münster, Münster, Germany; Max Planck Institute of Immunobiology, Freiburg, Germany; and Department of Biomedical Engineering, University of Virginia Health Sciences Center, Charlottesville, VA.
The P-selectin glycoprotein ligand-1 (PSGL-1) is a high-affinity ligand of P-selectin on myeloid cells and certain subsets of lymphoid cells. We generated the rat monoclonal antibody (MoAb) 2PH1 that recognizes an epitope within the first 19 amino acids at the N-terminus of the processed form of mouse PSGL-1. This antibody blocks attachment of mouse myeloid cells to P-selectin under both static and flow conditions. Intravenous administration of saturating amounts of 2PH1 reduced the number of rolling leukocytes in venules of the acutely exposed mouse cremaster muscle by 79% (±5.7%), whereas an anti-P-selectin MoAb reduced it completely. Examining the effect of the MoAb 2PH1 on the recruitment of neutrophils into chemically inflamed mouse peritoneum showed that blocking PSGL-1 inhibited neutrophil accumulation in the peritoneum by 82% (±7%) at 2 hours and by 59% (±7.9%) at 4 hours after stimulation. A similar effect was seen with the MoAb against P-selectin. Simultaneous administration of both antibodies at the 4-hour time point blocked neutrophil accumulation by 86% (±4.2%), arguing for an additional partner molecule for PSGL-1 besides P-selectin. This is the first demonstration of the importance of PSGL-1 in the recruitment of mouse neutrophils into inflamed tissue.
Blood, Vol. 90 No. 5 (September 1), 1997:
pp. 1934-1942
© 1997 by The American Society of Hematology.
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