Fucosyltransferase activities cells

Differences in fucolipid content as between normal and transformed cells, and changes on ontogenesis, have already been discussed, and these effects are presumably due to variations in fucosyltransferase activities, with possible specificity differences, namely, a-(l— 2) to Gal or (1— 3 or 4) to GlcNAc. However, the enzymes involved in these cells have not yet been separated and purified, and information on the separate enzyme-activities involved is almost nonexistent. 

Glycolipid Fucosyltransferase Activities in Mouse and Human Tumor Cells... 

Human a-l,3-fucosyltransferases are found in milk,51 53 saliva,54 and other specific cell lines.55-57 Through cloning studies, a role for an a-1,3-fucosyltransferase in cell adhesion was identified for the biosynthesis of sialyl Lewisxon neutrophils.58-59 As these studies link a-l,3-fucosyltransferase to cell adhesion and since the activated fucose species used by this enzyme is GDP-L-fucose, Luengo, et al.,eo prepared the C-glycoside analog of GDP-fucose shown in Figure 1.4.4. 

The a-2- and a-3-L-fucosyltransferase activities of human cells and plasma are inhibited by A -ethylmaleimide, but activities are restored by treatment with dithiothreitol, indicating the necessity of a free thiol group for activity. 

L-Fucosyltransferase activity has been demonstrated in rat ascites hepatoma cells and this enzyme catalyses the addition of L-fucose residues to asialo-G to form an L-fucolipid, in the presence of a detergent with the structure (26). The lipid co-chromatographed with authentic blood-group H-active L-fucolipid. The L-fucosyltransferase activity was highly specific for asialo-G i. ... 

Yamada N, Chung YS, Takatsuka S, Arimoto Y, Sawada T, Dohi T, Sowa M. Increased sialyl Lewis A expression and fucosyltransferase activity with acquisition of a high metastatic capacity in a colon cancer cell line. Br J Cancer 1994 76 582 587. 

The original nomenclature for the various isoforms of fucosyltransferases, based upon the order in which the genes were isolated, was established by Pamela Stanley [1] and further extended by John Lowe. FucT I and II were used to designate fucosyltransferases activities found in the lectin-resistant CHO cell lines LECH and LEC12 the next five fucosyltransferases identified were human a3,4-fucosyl-transferases whose genes have been cloned (FucT III to VII) [2-8]. 

After preparation of this review, an abstract by Godde A, Kragl U, Biselli M, Katapodis A, Bowen BR, Ernst B, Wandrey C, was published on the XVIIIth International Carbohydrate Symposium, July 21-26, 1996, Milano, Italy (BP 135, p 390). It reports the large-scale production of 1800 units of a recombinant human al-3 fucosyltransferase (FucT VI, EC. 2.4.1.152) in its soluble form with a CHO cell line in a continuous fermentation process in a fluidized bed reactor (34mUmg 1 in culture supernatant). After partial purification the specific activity yielded 220 mU mg ... 

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