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Oren Dwir¹, Ariel Solomon¹, Shmuel Mangan¹, Geoffrey S. Kansas², Ulrich S. Schwarz³ and Ronen Alon¹

¹ Department of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel
² Department of Microbiology-Immunology, Feinberg School of Medicine, Northwestern University, Chicago, IL 60611
³ Max Planck Institute of Colloids and Interfaces, 14424 Potsdam, Germany

Address correspondence to Ronen Alon, Dept. of Immunology, Weizmann Institute of Science, Rehovot 76100, Israel. Tel.: 972-8-9342482. Fax: 972-8-9344141. email: ronalon{at}wicc.weizmann.ac.il

L-selectin is a key lectin essential for leukocyte capture and rolling on vessel walls. Functional adhesion of L-selectin requires a minimal threshold of hydrodynamic shear. Using high temporal resolution videomicroscopy, we now report that L-selectin engages its ligands through exceptionally labile adhesive bonds (tethers) even below this shear threshold. These tethers share a lifetime of 4 ms on distinct physiological ligands, two orders of magnitude shorter than the lifetime of the P-selectin–PSGL-1 bond. Below threshold shear, tether duration is not shortened by elevated shear stresses. However, above the shear threshold, selectin tethers undergo 14-fold stabilization by shear-driven leukocyte transport. Notably, the cytoplasmic tail of L-selectin contributes to this stabilization only above the shear threshold. These properties are not shared by P-selectin– or VLA-4–mediated tethers. L-selectin tethers appear adapted to undergo rapid avidity enhancement by cellular transport, a specialized mechanism not used by any other known adhesion receptor.

Key Words: selectin; rolling; lymph nodes; aggregation; shear flow

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