Acceptor Specificity of Different Length Constructs of Human Recombinant α1,3/4-Fucosyltransferases

Vries, Theodora de; Srnka, Cheryl A.; Palcic, Monica M.; Swiedler, Stuart J.; Eijnden, Dirk H. van den; Macher, Bruce A.

doi:10.1074/jbc.270.15.8712

Cited by 140 publications

(81 citation statements)

References 64 publications

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“…This fits with previous observations (Kobayashi et al 1993) and probably reflects different FucT III enzyme activities towards different acceptor substrates (e.g. glycolipids vs glycoproteins) (De Vries et al 1995). Seven of the cases with a Lewis positive expression profile in the gastric mucosa are homozygous for one of the deleterious polymorphisms (202T>C, 508G>A or 1067T>A) ( antigens.…”

Section: Discussionsupporting

confidence: 78%

“…The other two polymorphisms that we identified (202T>C and 314C>T) are localised in the catalytic domain and are associated with a negative Lewis phenotype in Sweden (De Vries et al 1995;Elmgren et al 1996) and in Denmark (Ørntoft et al 1996). Curiously, De Vries et al (1995) showed that the 314C>T polymorphism has enzymatic activity similar to wild type enzyme when it catalyses the Le antigens synthesis on glycoprotein acceptors.…”

Section: Discussionmentioning

confidence: 99%

“…Curiously, De Vries et al (1995) showed that the 314C>T polymorphism has enzymatic activity similar to wild type enzyme when it catalyses the Le antigens synthesis on glycoprotein acceptors. Both in Sweden and in Denmark 202T>C and 314C>T polymorphisms co-localised in the same allele (Elmgren et al 1996;Ørntoft et al 1996).…”

Section: Discussionmentioning

confidence: 99%

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Lewis enzyme (α1–3/4 fucosyltransferase) polymorphisms do not explain the Lewis phenotype in the gastric mucosa of a Portuguese population

et al. 2003

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The human a-1,3/4 fucosyltransferase III (FucT III) catalyses the synthesis of Lewis antigens including Le b antigen which is a ligand for Helicobacter pylori adhesion. Several polymorphisms have been described in the FUT3 gene affecting both the transmembrane and catalytic domains, some of which affect the enzyme activity. The aim of the present work was to study the Lewis gene polymorphisms in a Caucasian Portuguese population, with a high rate of H. pylori infection, and to evaluate the implications of mutant enzymes in Le b expression in the gastric mucosa. We studied 460 asymptomatic or dyspeptic individuals from northern Portugal. Screening for Lewis gene polymorphisms was performed by SSCP and direct sequencing. Lewis phenotype in gastric mucosa was determined by immunohistochemistry. In 47 individuals with a Lewis negative blood group, we found FUT3 gene polymorphisms that were previously described in other populations: 59T>G, 202T>C, 314C>T, 508G>A and 1067T>A. Among the 47 Lewis negative individuals in blood, only nine were also negative in gastric mucosa, suggesting the existence of another a 1-4 fucosyltransferase that is responsible for Le a and Le b synthesis in gastric mucosa.

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Section: Discussionsupporting

confidence: 78%

Section: Discussionmentioning

confidence: 99%

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Lewis enzyme (α1–3/4 fucosyltransferase) polymorphisms do not explain the Lewis phenotype in the gastric mucosa of a Portuguese population

et al. 2003

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“…Properties of pPROTA-expressed enzymes have been shown to be very similar to those of full-length enzymes (26). Site-directed mutagenesis of FucT V in pPROTA forming the two mutants K255R and K255A was conducted as follows via recombinant PCR (19).…”

Section: Methodsmentioning

confidence: 99%

“…The reaction mixture was incubated for 1 h at room temperature and stopped and quantitated as described previously utilizing Dowex-1 for oligosaccharide acceptors (26) or C 18 columns for 8-methoxycarbonyl glycoside derivatives as acceptors (26).…”

Section: Methodsmentioning

confidence: 99%

Human α1,3/4-Fucosyltransferases

Sherwood

Nguyen

Whitaker

et al. 1998

Journal of Biological Chemistry

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Amino acid sequence alignment of human ␣1,3/4-fucosyltransferases (FucTs) demonstrates that three highly conserved Lys residues are present in the catalytic domain of FucTs III, IV, V, and VI. Two of these sites are conserved in FucT VII, with the third located within the ␣1,3-FucT motif as a conservative change to Arg at position 223. and the R223K mutant; however, the purified R223K mutant enzyme had a 2-fold increased specific activity compared with purified native FucT VII. No change in GDP-fucose-protectable pyridoxal-P/NaBH 4 inactivation was observed for native or mutant FucT V or VII, further supporting the absence of involvement of this residue in sugar nucleotide binding. The results indicate that a basic residue in this position is required for enzyme activity, with a Lys residue providing higher intrinsic activity. The lack of influence of this site on substrate binding parameters and its location within the ␣1,3-FucT motif suggest that at least some of the residues within this motif are involved in catalysis rather than substrate binding.Five distinct human ␣1,3/4-fucosyltransferases (FucTs) 1 have been cloned (1-7), as well as related enzymes from other species (8 -16). Analysis of their deduced amino acid sequences demonstrates that a variable number of Lys residues are present. FucTs III, V, and VI are highly homologous and contain 13, 12, and 12 Lys residues, respectively. In contrast, FucTs VII and IV contain only two and five Lys residues, respectively. Sequence alignment analysis of these forms demonstrate that nine of the Lys residues present in FucT III, V, and VI are in equivalent positions. Of these, three Lys residues can be aligned with Lys residues found in the FucT III, IV, V, and VI sequences. The FucT VII sequence contains two of these Lys residues, and a conservative substitution (Arg 223

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