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Blood, 15 July 2002, Vol. 100, No. 2, pp. 531-538
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
The N-terminal peptide of PSGL-1 can mediate adhesion to
trauma-activated endothelium via P-selectin in vivo
Erin E. Burch,
Vivek R. Shinde Patil,
Raymond T. Camphausen,
Mohammad F. Kiani, and
Douglas J. Goetz
From the Department of Chemical Engineering, Ohio
University, Athens; Department of Biomedical Engineering, University of
Memphis, TN; Wyeth Research, Cambridge, MA; and School of Biomedical
Engineering, University of Tennessee Health Science Center, Memphis.
P-selectin glycoprotein ligand-1 (PSGL-1) is present on leukocytes
and is the major ligand for endothelial expressed P-selectin. A variety
of studies strongly suggests that the N-terminal region of PSGL-1
contains the binding site for P-selectin. We hypothesized that this
relatively small N-terminal peptide of PSGL-1 is sufficient to support
adhesion to P-selectin in vivo. To test this hypothesis, we coated 2 µm-diameter microspheres with a recombinant PSGL-1 construct, termed
19.ek.Fc. The 19.ek.Fc construct consists of the first 19 N-terminal
amino acids of mature PSGL-1 linked to an enterokinase cleavage site
that, in turn, is linked to human immunoglobulin G Fc. The
19.ek.Fc-coated microspheres were injected into the jugular vein of
mice. Intravital microscopy of postcapillary venules within the
cremaster muscle of mice revealed that a significantly greater number
of 19.ek.Fc microspheres rolled compared with control microspheres. The
number of rolling 19.ek.Fc microspheres was significantly diminished by
pretreatment of the mice with a monoclonal antibody to P-selectin or by
pretreatment of the 19.ek.Fc microspheres with a monoclonal antibody to
PSGL-1. Combined, the results indicate that the N-terminal peptide of
PSGL-1 can mediate adhesion to trauma-activated microvascular
endothelium via P-selectin in vivo.
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