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Originally published In Press as doi:10.1074/jbc.M201999200 on March 20, 2002

J. Biol. Chem., Vol. 277, Issue 24, 21130-21139, June 14, 2002
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L-selectin Dimerization Enhances Tether Formation to Properly Spaced Ligand*

Oren DwirDagger , Douglas A. Steeber§, Ulrich S. Schwarz||, Raymond T. Camphausen**, Geoffrey S. KansasDagger Dagger §§, Thomas F. Tedder§, and Ronen AlonDagger ¶¶

From the Dagger  Department of Immunology, Weizmann Institute of Science, Rehovot, 76100 Israel, the § Department of Immunology, Duke University Medical Center, Durham, North Carolina 27710,  Max-Planck-Institute of Colloids and Interfaces, Potsdam, Germany 14424, ** Wyeth/Genetics Institute, Cambridge, Massachusetts 02140, and the Dagger Dagger  Department of Microbiology-Immunology, Northwestern Medical School, Chicago, Illinois 60611

Selectin counterreceptors are glycoprotein scaffolds bearing multiple carbohydrate ligands with exceptional ability to tether flowing cells under disruptive shear forces. Bond clusters may facilitate formation and stabilization of selectin tethers. L-selectin ligation has been shown to enhance L-selectin rolling on endothelial surfaces. We now report that monoclonal antibodies-induced L-selectin dimerization enhances L-selectin leukocyte tethering to purified physiological L-selectin ligands and glycopeptides. Microkinetic analysis of individual tethers suggests that leukocyte rolling is enhanced through the dimerization-induced increase in tether formation, rather than by tether stabilization. Notably, L-selectin dimerization failed to augment L-selectin-mediated adhesion below a threshold ligand density, suggesting that L-selectin dimerization enhanced adhesiveness only to properly clustered ligand. In contrast, an epidermal growth factor domain substitution of L-selectin enhanced tether formation to L-selectin ligands irrespective of ligand density, suggesting that this domain controls intrinsic ligand binding properties of L-selectin without inducing L-selectin dimerization. Strikingly, at low ligand densities, where L-selectin tethering was not responsive to dimerization, elevated shear stress restored sensitivity of tethering to selectin dimerization. This is the first indication that shear stress augments effective selectin ligand density at local contact sites by promoting L-selectin encounter of immobilized ligand.

* This work was supported in part by the United States Israel Binational Science Foundation (to R. A. and G. S. K) and by the Israel Science Foundation founded by the Israel Academy of Sciences and Humanities (to R. A.).The costs of publication of this article were defrayed in part by the payment of page charges. The article must therefore be hereby marked "advertisement" in accordance with 18 U.S.C. Section 1734 solely to indicate this fact.

|| Supported by the Emmy-Noether-Programme of the German Science Foundation.

§§ Recipient of National Institutes of Health Grant 1R24HL64381.

¶¶ Incumbent of The Tauro Career Development Chair in Biomedical Research. To whom correspondence should be addressed: Dept. of Immunology, Weizmann Inst. of Science, Rehovot, 76100 Israel; Tel.: 972-8-9342482; Fax: 972-8-9344141; Email: ronalon@wicc.weizmann.ac.il.

Copyright © 2002 by The American Society for Biochemistry and Molecular Biology, Inc.
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