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Prepublished online as a Blood First Edition Paper on August 29, 2002; DOI 10.1182/blood-2002-06-1799.
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Blood, 15 December 2002, Vol. 100, No. 13, pp. 4485-4494
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Discordant expression of selectin ligands and sialyl Lewis
x-related epitopes on murine myeloid cells
Marcin M. A. Kobzdej,
Anne Leppänen,
Vishwanath Ramachandran,
Richard D. Cummings, and
Rodger P. McEver
From the Cardiovascular Biology Research Program,
Oklahoma Medical Research Foundation; and the Department of
Biochemistry and Molecular Biology, Oklahoma Center for Medical
Glycobiology, University of Oklahoma Health Sciences Center, Oklahoma
City, OK.
Murine leukocytes are thought to express  2-3-sialylated and
1-3-fucosylated selectin ligands such as sialyl Lewis x
(sLex), although monoclonal antibodies (mAbs) to
sLex or Lex reportedly do not bind to murine
leukocytes. We observed that P- and E-selectin bound to
pronase-sensitive ligands on murine monocytic WEHI-3 cells and murine
neutrophils, indicating that the ligands for both selectins are
glycoproteins. CSLEX-1, HECA-452, and other widely used mAbs to
sLex and Lex did not bind to WEHI-3 cells and
bound at very low levels to murine neutrophils. Only the
anti-sLex mAbs 2H5 and KM93, which also recognize
nonfucosylated glycans, bound to WEHI-3 cells. 2H5 and KM93 bound to
pronase-resistant structures, indicating that the mAbs did not identify
selectin ligands. Treatment of WEHI-3 cells with glycosidases or
chlorate demonstrated that sialic acid modifications,
1-3-galactosylation, or sulfation did not mask epitopes for mAbs to
sLex or Lex. Compared to human promyelocytic
HL-60 cells, WEHI-3 cells and murine neutrophils expressed low
1-3-fucosyltransferase activities. Consistent with very low
endogenous fucosylation, forced fucosylation of intact WEHI-3 cells or
murine neutrophils by exogenous 1-3-fucosyltransferase FTVI and
GDP-fucose created many new epitopes for anti-sLex
mAbs such as HECA-452 and CSLEX-1. Nevertheless, forced fucosylation of
intact cells did not significantly augment their ability to bind to
fluid-phase P- or E-selectin or to roll on immobilized P- or E-selectin
under flow. These data suggest that murine myeloid leukocytes
fucosylate only a few specific glycans, which interact preferentially
with P- and E-selectin.
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