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Mouse P-selectin glycoprotein ligand-1: molecular cloning, chromosomal
localization, and expression of a functional P-selectin receptor
J Yang, J Galipeau, CA Kozak, BC Furie and B Furie
Center for Hemostasis and Thrombosis Research, Division of Hematology-
Oncology, New England Medical Center, Boston, MA, USA.
A mouse homolog of P-selectin glycoprotein ligand-1 (PSGL-1), a P- selectin
receptor on myeloid cells, has been cloned using the human cDNA sequence to
probe a cDNA library prepared from the mouse WEHI-3 monocytic cell line and
a genomic DNA library prepared from 129/SvJ mouse tissue. The gene flanking
the entire open reading frame of 397 amino acids is composed of a single
exon. Mouse and human PSGL-1 show an overall similarity of 67% and an
identity of 50% and contain a similar domain organization. However, there
are 10 threonine/serine- rich decameric repeats in mouse PSGL-1 as compared
with 15 threonine- rich repeats in human PSGL-1. When the mouse PSGL-1 cDNA
is coexpressed with an alpha 1,3/1,4 fucosyltransferase cDNA in COS cells,
a functional protein is expressed on the COS cell surface mediating binding
to human P-selectin. The mouse PSGL-1 gene, Selpl, was mapped to a position
on mouse chromosome 5 (Chr 5). Northern blot analyses of mouse tissues
showed moderate expression of a PSGL-1 mRNA species in most tissues
including heart, kidney, liver, muscle, ovary, and stomach and high levels
of expression in blood, bone marrow, brain, adipose tissue, spleen, and
thymus. Whereas certain mouse myeloid cell lines including PU5-1.8,
WEHI-3B, and 32DC13 express high levels of PSGL-1 mRNA, only WEHI-3B and
32DC13 bind to P-selectin; this interaction is blocked by anti-PSGL-1
antibody. WEHI-3B cells bind significantly better to P-selectin than to
E-selectin. Although comparable P-selectin binding is observed in 32DC13
cells, these cells bind better to E- selectin. Binding of 32DC13 cells to
E-selectin is not blocked by anti- PSGL-1 antibody. Treatment of WEHI-3B
cells with trypsin or neuraminidase abolished their ability to interact
with P-selectin. These results indicate that mouse PSGL-1 has structural
and functional homology to human PSGL-1 but is characterized by differences
in the composition and number of the decameric repeats. PSGL-1 on mouse
myeloid cells is critical for high-affinity binding to P-selectin but not
E-selectin.
Volume 87,
Issue 10,
pp. 4176-4186,
05/15/1996
Copyright © 1996 by The American Society of Hematology
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