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J Biol Chem, Vol. 273, Issue 7, 4021-4026, February 13, 1998
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From the The P-selectin counterreceptor PSGL-1 is
covalently modified by mono Institute of Biotechnology, P.O. Box 56 and
¶ Department of Bacteriology and Immunology, Haartman
Institute, P.O. Box 21, University of Helsinki, FIN-00014 Helsinki,
Finland and the Howard Hughes Medical Institute and Department
of Pathology, University of Michigan Medical School, Ann Arbor,
Michigan 48109-0650
2,3-sialylated, multiply
1,3-fucosylated polylactosamines. These glycans are required for the
adhesive interactions that allow this adhesion receptor-counterreceptor
pair to facilitate leukocyte extravasation. To begin to understand the
biosynthesis of these glycans, we have characterized the acceptor and
site specificities of the two granulocyte 1,3-fucosyltransferases, Fuc-TIV and Fuc-TVII, using recombinant forms of these two enzymes and
a panel of synthetic polylactosamine-based acceptors. We find that
Fuc-TIV can transfer fucose effectively to all N-acetyllactosamine (LN)
units in neutral polylactosamines, and to the "inner" LN units of
2,3-sialylated acceptors but is ineffective in transfer to the
distal 2,3-sialylated LN unit in 2,3-sialylated acceptors. Fuc-TVII, by contrast, effectively fucosylates only the distal 2,3-sialylated LN unit in 2,3-sialylated acceptors and thus exhibits an acceptor site-specificity that is complementary to Fuc-TIV.
Furthermore, the consecutive action of Fuc-TIV and Fuc-TVII, in
vitro, can convert the long chain sialoglycan
SA2-3'LN
1-3'LN1-3'LN (where SA is sialic acid) into the
trifucosylated molecule SA2-3'Lex1-3'Lex1-3'Lex (where Lex
is the trisaccharide Gal1-4(Fuc1-3)GlcNAc) known to decorate
PSGL-1. The complementary in vitro acceptor
site-specificities of Fuc-TIV and Fuc-TVII imply that these enzymes
cooperate in vivo in the biosynthesis of monosialylated,
multifucosylated polylactosamine components of selectin
counterreceptors on human leukocytes.
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