J. Cell Biol.
© The Rockefeller University Press
0021-9525/97/04/509/11 $2.00
Volume 137, Number 2, April 21, 1997 509-519

Isolated P-selectin Glycoprotein Ligand-1 Dynamic Adhesion to P- and E-selectin

Douglas J. Goetz,^* Daniel M. Greif,^* Han Ding,^* Raymond T. Camphausen, Steven Howes, Kenneth M. Comess, Karen R. Snapp,^§ Geoffrey S. Kansas,^§ and Francis W. Luscinskas^*

^* Vascular Research Division, Department of Pathology, Brigham and Women's Hospital, Harvard Medical School, Boston, Massachusetts 02115;  Small Molecule Drug Discovery Group, Genetics Institute, Cambridge, Massachusetts 02140; and ^§ Department of Microbiology-Immunology, Northwestern University Medical School, Chicago, Illinois 60611

Leukocyte adhesion to vascular endothelium under flow involves an adhesion cascade consisting of multiple receptor pairs that may function in an overlapping fashion. P-selectin glycoprotein ligand-1 (PSGL-1) and L-selectin have been implicated in neutrophil adhesion to P- and E-selectin under flow conditions. To study, in isolation, the interaction of PSGL-1 with P-and E-selectin under flow, we developed an in vitro model in which various recombinant regions of extracellular PSGL-1 were coupled to 10-µm-diameter microspheres. In a parallel plate chamber with well defined flow conditions, live time video microscopy analyses revealed that microspheres coated with PSGL-1 attached and rolled on 4-h tumor necrosis factor--activated endothelial cell monolayers, which express high levels of E-selectin, and CHO monolayers stably expressing E-or P-selectin. Further studies using CHO-E and -P monolayers demonstrate that the first 19 amino acids of PSGL-1 are sufficient for attachment and rolling on both E- and P-selectin and suggest that a sialyl Lewis x-containing glycan at Threonine-16 is critical for this sequence of amino acids to mediate attachment to E- and P-selectin. The data also demonstrate that a sulfated, anionic polypeptide segment within the amino terminus of PSGL-1 is necessary for PSGL-1-mediated attachment to P- but not to E-selectin. In addition, the results suggest that PSGL-1 has more than one binding site for E-selectin: one site located within the first 19 amino acids of PSGL-1 and one or more sites located between amino acids 19 through 148.

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