TY - JOUR
T1 - Expression cloning of a cDNA encoding a sulfotransferase involved in the biosynthesis of the HNK-1 carbohydrate epitope
AU - Bakker, Hans
AU - Friedmann, Igor
AU - Oka, Shogo
AU - Kawasaki, Toshisuke
AU - Nifant'Ev, Nikolay
AU - Schachnerfl, Melitta
AU - Mantei, Ned
PY - 1997/11/21
Y1 - 1997/11/21
N2 - 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-GlcAβ1→3Galβ1→4GlcNAc. 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.
AB - 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-GlcAβ1→3Galβ1→4GlcNAc. 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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U2 - 10.1074/jbc.272.47.29942
DO - 10.1074/jbc.272.47.29942
M3 - Article
C2 - 9368071
AN - SCOPUS:0030721537
SN - 0021-9258
VL - 272
SP - 29942
EP - 29946
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 47
ER -