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P-selectin glycoprotein ligand-1 (PSGL-1) is a ligand for L-selectin in
neutrophil aggregation
DA Guyer, KL Moore, EB Lynam, CM Schammel, S Rogelj, RP McEver and LA Sklar
Cytometry, Cancer Research and Treatment Center, University of New Mexico
School of Medicine, Albuquerque, USA.
In inflammation, activated neutrophils adhere to endothelial cells and
aggregate with one another. While beta 2-integrin and L-selectin are
essential for aggregation, their ligands remain to be identified. We have
previously shown that L-selectin mediates a carbohydrate-dependent
interaction in aggregation (Simon et al: J Immunol 149:2765, 1992; Rochon
et al: J Immunol 152:1385, 1994). We have suggested that the L- selectin
counter-structure is a mucinlike protein and proposed that aggregation
occurs through a two-step process involving L-selectin, beta 2-integrin,
and their distinct counter-structures (Bennett et al: J Leuk Biol 58:510,
1995). A candidate ligand for L-selectin is P- selectin glycoprotein
ligand-1 (PSGL-1), a mucinlike protein on neutrophils that binds P-and
E-selectin. Using flow cytometry we show that the number and size of
neutrophil aggregates is reduced with Fab fragments of PL1, an anti-PSGL-1
monoclonal antibody that blocks the interaction between P-selectin and
PSGL-1 (Moore et al: J Cell Biol 128:661, 1995). In addition, monoclonal
antibodies to L-selectin and PSGL-1 were used simultaneously to modulate
the availability of these adhesion molecules on individual cell
populations. The inhibition of aggregation by these antibodies is
consistent with L-selectin and PSGL- 1 being counter-structures. We suggest
that L-selectin and PSGL-1 support a collisional cell-cell interaction that
represents the first step in neutrophil aggregation.
Volume 88,
Issue 7,
pp. 2415-2421,
10/01/1996
Copyright © 1996 by The American Society of Hematology
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