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Research Article Free access | 10.1172/JCI118888

Neutrophil-neutrophil interactions under hydrodynamic shear stress involve L-selectin and PSGL-1. A mechanism that amplifies initial leukocyte accumulation of P-selectin in vitro.

B Walcheck, K L Moore, R P McEver, and T K Kishimoto

Department of Immunology, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, Connecticut 06877, USA.

Find articles by Walcheck, B. in: PubMed | Google Scholar

Department of Immunology, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, Connecticut 06877, USA.

Find articles by Moore, K. in: PubMed | Google Scholar

Department of Immunology, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, Connecticut 06877, USA.

Find articles by McEver, R. in: PubMed | Google Scholar

Department of Immunology, Boehringer Ingelheim Pharmaceuticals, Inc., Ridgefield, Connecticut 06877, USA.

Find articles by Kishimoto, T. in: PubMed | Google Scholar

Published September 1, 1996 - More info

Published in Volume 98, Issue 5 on September 1, 1996
J Clin Invest. 1996;98(5):1081–1087. https://doi.org/10.1172/JCI118888.
© 1996 The American Society for Clinical Investigation
Published September 1, 1996 - Version history
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Abstract

Leukocytes attach to and roll on inflamed endothelium and on leukocyte monolayers that form on the endothelial cells. Leukocyte-leukocyte interactions occurring under hydrodynamic shear stress are mediated by binding of L-selectin to unknown sialomucin-like glycoproteins. We show that purified neutrophil PSGL-1, a sialomucin glycoprotein that serves as a ligand for both P- and E-selectin, can also support the attachment and rolling of free flowing neutrophils in vitro. Neutrophil rolling on PSGL-1 was abolished by the anti-L-selectin mAb DREG200 and by the anti-PSGL-1 mAb PL1, indicating that L-selectin can interact directly with PSGL-1. Neutrophil rolling on neutrophil monolayers was also blocked by PL1 (60 +/- 9% SEM inhibition); however, DREG200 blocked more efficiently (93 +/- 7% SEM inhibition), suggesting that other L-selectin ligands may exist on the neutrophil surface. These studies demonstrate that PSGL-1 on the neutrophil surface is a major functional ligand for L-selectin. The avidity of this L-selectin-dependent adhesion event was sufficient to allow individual neutrophils rolling on P-selectin to capture free flowing neutrophils, which progressed to form linear strings and discrete foci of rolling neutrophils. Neutrophil accumulation on P-selectin accelerated with time as a result of neutrophil-assisted capture of free flowing neutrophils. When neutrophil-neutrophil interactions were blocked by DREG200, neutrophils accumulated on P-selectin in a random pattern and at a uniform rate. Thus, leukocyte-assisted capture of flowing leukocytes may play an important role in amplifying the rate of initial leukocyte recruitment at sites of inflammation.

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