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Prepublished online as a Blood First Edition Paper on August 29, 2002; DOI 10.1182/blood-2001-11-0036.
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Blood, 15 January 2003, Vol. 101, No. 2, pp. 552-559
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
N-terminal residues in murine P-selectin glycoprotein ligand-1
required for binding to murine P-selectin
Lijun Xia,
Vishwanath Ramachandran,
J. Michael McDaniel,
Kiem N. Nguyen,
Richard D. Cummings, and
Rodger P. McEver
From the Cardiovascular Biology Research Program,
Oklahoma Medical Research Foundation, and Department of Biochemistry
and Molecular Biology, Oklahoma Center for Medical Glycobiology,
University of Oklahoma Health Sciences Center, Oklahoma City.
P-selectin binds to the N-terminal region of human P-selectin
glycoprotein ligand-1 (PSGL-1). For optimal binding, this region requires sulfation on 3 tyrosines and specific core-2
O-glycosylation on a threonine. P-selectin is also thought
to bind to the N terminus of murine PSGL-1, although it has a very
different amino acid sequence than human PSGL-1. Murine PSGL-1 has
potential sites for sulfation at Tyr13 and
Tyr15 and for O-glycosylation at Thr14 and
Thr17. We expressed murine PSGL-1 or constructs with substitutions of
these residues in transfected Chinese hamster ovary cells that coexpressed the glycosyltransferases required for binding to
P-selectin. The cells were assayed for binding to fluid-phase
P-selectin and for tethering and rolling on P-selectin under flow. In
both assays, substitution of Tyr13 or Thr17 markedly diminished, but
did not eliminate, binding to P-selectin. In contrast, substitution of Tyr15 or Thr14 did not affect binding. Substitution of all 4 residues eliminated binding. Treatment of cells with chlorate, an inhibitor of
sulfation, markedly reduced binding of wild-type PSGL-1 to P-selectin
but did not further decrease binding of PSGL-1 with substitutions of
both tyrosines. These data suggest that sulfation of Tyr13 and
O-glycosylation of Thr17 are necessary for murine PSGL-1 to
bind optimally to P-selectin. Because it uses only one tyrosine, murine
PSGL-1 may rely more on other peptide components and
O-glycosylation to bind to P-selectin than does human
PSGL-1.
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