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Prepublished online as a Blood First Edition Paper on July 25, 2002; DOI 10.1182/blood-2002-04-1007.
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Blood, 15 November 2002, Vol. 100, No. 10, pp. 3618-3625
HEMOSTASIS, THROMBOSIS, AND VASCULAR BIOLOGY
Sialyltransferase specificity in selectin ligand
formation
Lesley G. Ellies,
Markus Sperandio,
Gregory H. Underhill,
James Yousif,
Michael Smith,
John J. Priatel,
Geoffrey S. Kansas,
Klaus Ley, and
Jamey D. Marth
From the Department of Cellular and Molecular Medicine,
Glycobiology Research and Training Center, and Howard Hughes Medical
Institute, University of California, San Diego; Cardiovascular Research
Center and Department of Biomedical Engineering, University of Virginia
Health Sciences Center, Charlottesville, VA; Department of Biomedical
Engineering and Microbiology-Immunology, Northwestern University
Medical School, Chicago, IL.
Selectin ligands are glycan structures that participate in
leukocyte trafficking and inflammation. At least 6 ST3Gal
sialyltransferases (I-VI) have been identified that may contribute to
selectin ligand formation. However, it is not known which of these
sialyltransferases are involved in vivo and whether they may
differentially regulate selectin function. We have produced and
characterized mice genetically deficient in ST3Gal-I, ST3Gal-II,
ST3Gal-III, and ST3Gal-IV. Unlike mice bearing severe defects in
selectin ligand formation, there was no finding of leukocytosis with
these single ST3Gal deficiencies. Among neutrophils, only ST3Gal-IV was
found to play a role in the synthesis of selectin ligands. In vitro
rolling of marrow-derived neutrophils on E- or P-selectins presented by
Chinese hamster ovary cells was reduced in the absence of ST3Gal-IV.
However, in a tumor necrosis factor  (TNF-)-induced
inflammation model in vivo, no defect among P-selectin ligands
was observed. Nevertheless, the number of leukocytes rolling on
postcapillary venules in an E-selectin-dependent manner was decreased
while E-selectin-dependent rolling velocity was increased. We propose
that multiple ST3Gal sialyltransferases contribute to selectin ligand
formation, as none of these ST3Gal deficiencies recapitulated the
degree of E- and P-selectin ligand deficit observed on neuraminidase
treatment of intact neutrophils. Our findings indicate a high degree of functional specificity among sialyltransferases and a
substantial role for ST3Gal-IV in selectin ligand formation.
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