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J. Exp. Med.,
Volume 188, Number 7, October 5, 1998 1385-1390
By
From the * Department of Immunology, Duke University Medical Center, Durham, North Carolina
27710; and L-selectin binding activity for its ligand expressed by vascular endothelium is rapidly and transiently increased after leukocyte activation. To identify mechanisms for upregulation and assess how this influences leukocyte/endothelial cell interactions, cell-surface dimers of L-selectin
were induced using the coumermycin-GyrB dimerization strategy for cross-linking L-selectin
cytoplasmic domains in L-selectin cDNA-transfected lymphoblastoid cells. Coumermycin-
induced L-selectin dimerization resulted in an approximately fourfold increase in binding of
phosphomanan monoester core complex (PPME), a natural mimic of an L-selectin ligand,
comparable to that observed after leukocyte activation. Moreover, L-selectin dimerization significantly increased (by ~700%) the number of lymphocytes rolling on vascular endothelium
under a broad range of physiological shear stresses, and significantly slowed their rolling velocities. Therefore, L-selectin dimerization may explain the rapid increase in ligand binding activity that occurs after leukocyte activation and may directly influence leukocyte migration to peripheral lymphoid tissues or to sites of inflammation. Inducible oligomerization may also be a
common mechanism for rapidly upregulating the adhesive or ligand-binding function of other
cell-surface receptors.
Merck Co., Inc., Rahway, New Jersey 07065
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