Five specificity patterns of (1 → 3)-α-l-fucosyltransferase activity defined by use of synthetic oligosaccharide acceptors. Differential expression of the enzymes during human embryonic development and in adult tissues

Mollicone, Rosella; Candelier, Jean-Jacques; Mennesson, Benoît; Couillin, Phillippe; Venot, André; Oriol, Rafaël

doi:10.1016/s0008-6215(00)90564-0

Cited by 74 publications

(44 citation statements)

References 19 publications

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“…Each encoded enzyme displays a characteristic pattern of activity for potential glycolipid, protein and carbohydrate acceptors (8, 40 -42). In addition, each FUT gene is expressed in a tissue and cell line characteristic pattern (15,16,20,39,(43)(44)(45), suggesting unique regulation of individual gene expression. Functionally, the ␣(1,3)-FucTs fucosylate cell surface proteins and lipids that mediate cell adhesion, sorting, and activation (5, 46 -49).…”

Section: Discussionmentioning

confidence: 99%

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Human α(1,3)-Fucosyltransferase IV (FUTIV) Gene Expression Is Regulated by Elk-1 in the U937 Cell Line

Withers¹,

Hakomori²

2000

Journal of Biological Chemistry

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Section: Discussionmentioning

confidence: 99%

“…Expression is regulated during normal development (16,19,20) and in tumors (11)(12)(13). We sought to identify the trans-acting factors responsible for up-regulating FUTIV expression in tumor cell lines.…”

Section: Among Nine Fucosyltransferases (Fucts)mentioning

confidence: 99%

Human α(1,3)-Fucosyltransferase IV (FUTIV) Gene Expression Is Regulated by Elk-1 in the U937 Cell Line

Withers¹,

Hakomori²

2000

Journal of Biological Chemistry

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“…Human ␣1,3/4-fucosyltransferases and their genetic expression are developmentally regulated (17,18). We have previously shown that FUT4 and FUT9 genes are derepressed early in human embryogenesis, whereas FUT6 and FUT3 appear sequentially after the 8th week of development (19).…”

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confidence: 99%

Activity, Splice Variants, Conserved Peptide Motifs, and Phylogeny of Two New α1,3-Fucosyltransferase Families (FUT10 and FUT11)

Mollicone

Moore

Bovin

et al. 2009

Journal of Biological Chemistry

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We report the cloning of three splice variants of the FUT10 gene, encoding for active ␣-L-fucosyltransferase-isoforms of 391, 419, and 479 amino acids, and two splice variants of the FUT11 gene, encoding for two related ␣-L-fucosyltransferases of 476 and 492 amino acids. The FUT10 and FUT11 appeared 830 million years ago, whereas the other ␣1,3-fucosyltransferases emerged 450 million years ago. FUT10-391 and FUT10-419 were expressed in human embryos, whereas FUT10-479 was cloned from adult brain and was not found in embryos. Recombinant FUT10-419 and FUT10-479 have a type II trans-membrane topology and are retained in the endoplasmic reticulum (ER) by a membrane retention signal at their NH 2 termini. The FUT10-479 has, in addition, a COOH-ER membrane retention signal. The FUT10-391 is a soluble protein without a transmembrane domain or ER retention signal that transiently localizes to the Golgi and then is routed to the lysosome. After transfection in COS7 cells, the three FUT10s and at least one FUT11, link ␣-L-fucose onto conalbumin glycopeptides and biantennary N-glycan acceptors but not onto short lactosaminyl acceptor substrates as do classical monoexonic ␣1,3-fucosyltransferases. Modifications of the innermost core GlcNAc of the N-glycan, by substitution with ManNAc or with an opened GlcNAc ring or by the addition of an ␣1,6-fucose, suggest that the FUT10 transfer is performed on the innermost GlcNAc of the core chitobiose. We can exclude ␣1,3-fucosylation of the two peripheral GlcNAcs linked to the trimannosyl core of the acceptor, because the FUT10 fucosylated biantennary N-glycan product loses both terminal GlcNAc residues after digestion with human placenta ␣-N-acetylglucosaminidase.

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“…The individual members of the human ␣(1,2)-fucosyltransferase family, H 1 (21,22) and Se (23,24) and the human ␣(1,3)-fucosyltransferase family (FUC-T3, FUC-T4, FUC-T5, FUC-T6, and FUC-T7), are discriminated by differences in substrate specificities, cation requirement, sensitivity to inhibitors, and tissue distribution (25)(26)(27)(28). Besides humans and to a lesser extent mice (29), little is known about the molecular mechanisms that determine the tissue-specific (30) and the developmentally regulated expression patterns of fucosyltransferases (31)(32)(33)(34).…”

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confidence: 99%

Molecular Cloning and Expression of a Bovine α(1,3)-Fucosyltransferase Gene Homologous to a Putative Ancestor Gene of the Human FUT3-FUT5-FUT6 Cluster

Oulmouden

Wierinckx

Petit

et al. 1997

Journal of Biological Chemistry

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Five specificity patterns of (1 → 3)-α-l-fucosyltransferase activity defined by use of synthetic oligosaccharide acceptors. Differential expression of the enzymes during human embryonic development and in adult tissues

Cited by 74 publications

References 19 publications

Human α(1,3)-Fucosyltransferase IV (FUTIV) Gene Expression Is Regulated by Elk-1 in the U937 Cell Line

Human α(1,3)-Fucosyltransferase IV (FUTIV) Gene Expression Is Regulated by Elk-1 in the U937 Cell Line

Activity, Splice Variants, Conserved Peptide Motifs, and Phylogeny of Two New α1,3-Fucosyltransferase Families (FUT10 and FUT11)

Molecular Cloning and Expression of a Bovine α(1,3)-Fucosyltransferase Gene Homologous to a Putative Ancestor Gene of the Human FUT3-FUT5-FUT6 Cluster

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