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(Received for publication, September 12, 1997)
,
,
and
From the The HNK-1 carbohydrate epitope is expressed on
several neural adhesion glycoproteins and as a glycolipid, and is
involved in cell interactions. The structural element of the epitope
common to glycoproteins and glycolipids has been determined to be
sulfate-3-GlcA
Department of Neurobiology, Swiss Federal
Institute of Technology, Hönggerberg, 8093 Zürich,
Switzerland, the § Department of Biological Chemistry,
Faculty of Pharmaceutical Sciences, Kyoto University, Sakyo-ku, Kyoto
606-01, Japan, the ¶ Zelinsky Institute of Organic Chemistry,
Russian Academy of Sciences, Leninsky Prospect 47, Moscow B-334, 117913 Russia, and the 
Zentrum für Molekulare Neurobiologie,
Universität Hamburg, Martinistraße 52, D-20246 Hamburg,
Germany
1
3Gal14GlcNAc. The glucuronyltransferase
and sulfotransferase are considered to be the key enzymes in the
biosynthesis of this epitope because the rest of the structure occurs
often in glycoconjugates. Here we describe the isolation of the rat
sulfotransferase cDNA via an expression cloning
strategy. The clone finally isolated predicts a protein of 356 amino
acids, with characteristics of a type II transmembrane protein and with
no sequence similarity to other known sulfotransferases. Both the
enzyme expressed as a soluble fusion protein and homogenates of cells
transfected with the full-length cDNA could transfer sulfate from a
sulfate donor to acceptor substrates containing terminal glucuronic
acid.
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