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Originally published In Press as doi:10.1074/jbc.M204360200 on October 25, 2002

J. Biol. Chem., Vol. 278, Issue 1, 37-47, January 3, 2003
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Molecular Basis of Leukocyte Rolling on PSGL-1
PREDOMINANT ROLE OF CORE-2 O-GLYCANS AND OF TYROSINE SULFATE RESIDUE 51*

Michael Pierre BernimoulinDagger , Xian-Lu ZengDagger , Claire AbbalDagger , Sylvain GiraudDagger , Manuel MartinezDagger , Olivier Michielin§, Marc SchapiraDagger , and Olivier SpertiniDagger ||

From the Dagger  Division and Central Laboratory of Hematology, Centre Hospitalier Universitaire Vaudois, Bugnon 46, 1011 Lausanne, Switzerland, the § Ludwig Institute for Cancer Research, Lausanne Branch, chemin des Boveresses 155, Epalinges, and the  Swiss Institute for Bioinformatics, chemin des Boveresses 155, Epalinges, Switzerland

Interactions between the leukocyte adhesion receptor L-selectin and P-selectin glycoprotein ligand-1 play an important role in regulating the inflammatory response by mediating leukocyte tethering and rolling on adherent leukocytes. In this study, we have examined the effect of post-translational modifications of PSGL-1 including Tyr sulfation and presentation of sialylated and fucosylated O-glycans for L-selectin binding. The functional importance of these modifications was determined by analyzing soluble L-selectin binding and leukocyte rolling on CHO cells expressing various glycoforms of PSGL-1 or mutant PSGL-1 targeted at N-terminal Thr or Tyr residues. Simultaneous expression of core-2 beta 1,6-N-acetylglucosaminyltransferase and fucosyltransferase VII was required for optimal L-selectin binding to PSGL-1. Substitution of Thr-57 by Ala but not of Thr-44, strongly decreased L-selectin binding and leukocyte rolling on PSGL-1. Substitution of Tyr by Phe revealed that PSGL-1 Tyr-51 plays a predominant role in mediating L-selectin binding and leukocyte rolling whereas Tyr-48 has a minor role, an observation that contrasts with the pattern seen for the interactions between PSGL-1 and P-selectin where Tyr-48 plays a key role. Molecular modeling analysis of L-selectin and P-selectin interactions with PSGL-1 further supported these observations. Additional experiments showed that core-2 O-glycans attached to Thr-57 were also of critical importance in regulating the velocity and stability of leukocyte rolling. These observations pinpoint the structural characteristics of PSGL-1 that are required for optimal interactions with L-selectin and may be responsible for the specific kinetic and mechanical bond properties of the L-selectin-PSGL-1 adhesion receptor-counterreceptor pair.

* This work was supported by Grant 32-065177.01 from the Swiss National Foundation for Scientific Research.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.

|| To whom correspondence should be addressed: Division of Hematology, University of Lausanne, BH 18-544, 1011-CHUV Lausanne, Switzerland. Tel.: 41-21-314-42-26; Fax: 41-21-314-41-80; E-mail: Olivier.Spertini@chuv.hospvd.ch.

Copyright © 2003 by The American Society for Biochemistry and Molecular Biology, Inc.
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