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J. Biol. Chem., Vol. 275, Issue 40, 31353-31360, October 6, 2000
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From the P-selectin glycoprotein ligand-1 (PSGL-1) and
E-selectin ligand-1 (ESL-1) are the two major selectin ligands on mouse
neutrophils. Transfection experiments demonstrate that each ligand
requires
P-selectin Glycoprotein Ligand-1 and E-selectin Ligand-1 Are
Differentially Modified by Fucosyltransferases Fuc-TIV and Fuc-TVII
in Mouse Neutrophils*
§,§,,
, and**
Institute of Cell Biology, ZMBE,
University of Münster and Max-Planck-Institute of
Physiological and Clinical Research, D-48149 Münster, Germany
and the ¶ Department of Pathology, Howard Hughes Medical
Institute, University of Michigan, Medical School,
Ann Arbor, Michigan 48109-0650
1,3-fucosylation for selectin-binding. However, the
relative contributions made by the two known myeloid
1,3-fucosyltransferases Fuc-TVII or Fuc-TIV to this
1,3-fucosylation are not yet clear. To address this issue, we have
used mice deficient in Fuc-TIV and/or Fuc-TVII to examine how these
enzymes generate selectin-binding glycoforms of PSGL-1 and ESL-1 in
mouse neutrophils. Selectin binding was analyzed by affinity isolation
experiments using recombinant, antibody-like forms of the respective
endothelial selectins. We observe essentially normal binding of E- or
P-selectin to PSGL-1 expressed by Fuc-TIV-deficient neutrophils but
find that PSGL-1 expressed by Fuc-TVII-deficient neutrophils is not
bound by E- or P-selectin. By contrast, E-selectin binds with normal
efficiency to ESL-1 on Fuc-TVII-deficient neutrophils but exhibits an
80% reduction in its ability to bind ESL-1 isolated from
Fuc-TIV-deficient neutrophils. The same specificity with which Fuc-TVII
and Fuc-TIV generate selectin-binding forms of PSGL-1 and ESL-1 was
found in transfection experiments with CHO-Pro
5
cells. In contrast, each fucosyltransferase alone could generate selectin-binding glycoforms of each of the two ligands in CHO-DUKX-B1 cells. Our data imply that in mouse neutrophils and their precursors, Fuc-TVII exclusively directs expression of PSGL-1 glycoforms bound with
high affinity by P-selectin. By contrast, Fuc-TIV preferentially directs expression of ESL-1 glycoforms that exhibit high affinity for
E-selectin. This substrate specificity can be mimicked in CHO-Pro5 cells.
*
This work was supported by the Max-Planck-Society and by
Deutsche Forschungsgemeinschaft Grant SFB 293 (to D. V.).The costs of publication of this
article were defrayed in part by the
payment of page charges. The article
must therefore be hereby marked
"advertisement" in
accordance with 18 U.S.C. Section
1734 solely to indicate this fact.
Investigator of the Howard Hughes Medical Institute. Supported
by National Institutes of Health Grant 1PO1CA-1932.
**
To whom correspondence should be addressed: Inst. of Cell Biology,
ZMBE, University of Münster, Von-Esmarch-Str. 56, D-48149 Münster, Germany. Tel.: 49-251-83-5-86-17; Fax:
49-251-83-5-86-16; E-mail: vestweb@uni-muenster.de.
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