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J Biol Chem, Vol. 273, Issue 9, 5190-5195, February 27, 1998
From the Glycobiology Program, La Jolla Cancer Research Center, The
Burnham Institute, La Jolla, California 92037
The HNK-1 carbohydrate is expressed on various
adhesion molecules in the nervous system and is suggested to play a
role in cell-cell and cell-substratum interactions. Here we describe
the isolation and functional expression of a cDNA encoding a human sulfotransferase that synthesizes the HNK-1 carbohydrate epitope. A
mutant Chinese hamster ovary cell line, Lec2, which stably
expresses human neural cell adhesion molecule (N-CAM)
(Lec2-NCAM), was first established. Lec2-NCAM was co-transfected with a
human fetal brain cDNA library, a cDNA encoding the rat
glucuronyltransferase that forms a precursor of the HNK-1 carbohydrate,
and a vector encoding the polyoma large T antigen. The transfected
Lec2-NCAM cells expressing the HNK-1 glycan were enriched by
fluorescence-activated cell sorting. Sibling selection of recovered
plasmids resulted in a cDNA encoding a sulfotransferase, HNK-1ST,
that directs the expression of the HNK-1 carbohydrate epitope on the
cell surface. The deduced amino acid sequence indicates that the enzyme
is a type II membrane protein. Sequence analysis revealed that there is
a short amino acid sequence in the presumed catalytic domain, which is
highly homologous to the corresponding sequence in other
Golgi-associated sulfotransferases so far cloned. The amount of HNK-1ST
transcript is high in fetal brain compared with fetal lung, kidney, and
liver. Expression of HNK-1ST resulted in the formation of the HNK-1
epitope on N-CAM and a soluble chimeric form of HNK-1ST was shown to
add a sulfate group to a precursor,
GlcA
Expression Cloning of a Human Sulfotransferase That Directs the
Synthesis of the HNK-1 Glycan on the Neural Cell Adhesion Molecule and
Glycolipids
1
3Gal14GlcNAc1R, forming sulfo3GlcA13Gal14GlcNAc1R. The results combined
together indicate that the cloned HNK-1ST directs the synthesis of the HNK-1 carbohydrate epitope on both glycoproteins and glycolipids in the
nervous tissues.
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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