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M204360200v1
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Papers In Press, published online ahead of print October 25, 2002
J. Biol. Chem, 10.1074/jbc.M204360200
Submitted on May 3, 2002
Revised on October 25, 2002
Accepted on October 24, 2002

Molecular basis of leukocyte rolling on PSGL-1: predominant role of core-2 O-glycans and of tyrosine sulfate residue 51

Michael Pierre Bernimoulin, Xian-Lu Zeng, Claire Abbal, Sylvain Giraud, Manuel Martinez, Olivier Michielin, Marc Schapira, and Olivier Spertini

Hematology Dept., CHUV, Lausanne, VD 1011

Corresponding Author: Olivier.Spertini{at}chuv.hospvd.ch

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 b1-6, 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.


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