Acceptor specificity and tissue distribution of three human alpha-3-fucosyltransferases.
Based on the capacity to transfer alpha-L-fucose onto type-1 and type-2 synthetic blood group H and sialylated acceptors, a comparison of the alpha-3-fucosyltransferase activities of different human tissues is shown. Three distinct acceptor specificity patterns are described: (I) myeloid alpha-3-fucosyltransferase pattern, in which leukocytes and brain enzymes transfer fucose actively onto H type-2 acceptor and poorly onto sialylated N-acetyllactosamine: (II) plasma alpha-3-fucosyltransferase (EC 2.4.1.152), in which plasma and hepatocyte enzymes transfer, in addition, onto the sialylated N-acetyllactosamine; (III) Lewis alpha-3 4-fucosyltransferase (EC 2.4.1.65), in which gall-bladder kidney and milk enzymes transfer, in addition, onto type-1 acceptors. The small amount (less than 10%) of alpha-3-fucosyltransferase activity found in the plasma of an alpha-3-fucosyltransferase-deficient individual had a myeloid-type acceptor pattern, suggesting that this small proportion of the plasma enzyme is derived from leukocytes. In addition to the three acceptor specificity patterns, these enzyme activities can be differentiated by their optimum pH: 8.0-8.7 for the enzymes from myeloid cells and brain. 7.2-8.0 for liver enzymes and 6.0-7.2 for gallbladder enzymes. Milk samples had two alpha-3-fucosyltransferase activities, the Lewis or alpha-3/4-fucosyltransferase under control of the Lewis gene and an alpha-3-fucosyltransferase with plasma acceptor pattern which was independent of the control of the Lewis gene. The apparent affinity for GDP-fucose of the myeloid-like enzyme was weaker than those of the plasma and Lewis-like enzymes. The apparent affinities for H type 2 and sialylated N-acetyllactosamine were stronger for exocrine secretions as compared to the plasma and myeloid enzymes. The plasma type of alpha-3-fucosyltransferase activity was more sensitive to N-ethylmaleimide and heat inactivation than the samples with myeloid-like alpha-3-fucosyltransferase activity.
Mollicone
R
R
Faculté de Pharmacie, Châtenay-Malabry, France.
Gibaud
A
A
François
A
A
Ratcliffe
M
M
Oriol
R
R
D001921:Brain / Q000201:enzymology; D002240:Carbohydrate Sequence; D005643:Fucose / Q000378:metabolism*; D005647:Fucosyltransferases / Q000032:analysis / Q000172:deficiency / Q000235:genetics; D005704:Gallbladder / Q000201:enzymology; D006602:Hexosyltransferases / Q000032:analysis*; D006358:Hot Temperature; D006801:Humans; D007668:Kidney / Q000201:enzymology; D007700:Kinetics; D007962:Leukocytes / Q000201:enzymology; D007983:Lewis Blood Group Antigens; D008099:Liver / Q000201:enzymology; D008895:Milk, Human / Q000201:enzymology; D008969:Molecular Sequence Data; D009844:Oligosaccharides / Q000032:analysis
D007983:Lewis Blood Group Antigens; D009844:Oligosaccharides; D005643:Fucose; D005647:Fucosyltransferases; D006602:Hexosyltransferases; C031692:galactoside 3-fucosyltransferase; C019818:3-galactosyl-N-acetylglucosaminide 4-alpha-L-fucosyltransferase; C020559:Glycoprotein 6-alpha-L-fucosyltransferase