Molecular genetics of α-L-fucosyltransferase genes (H, Se, Le, FUT4, FUT5 and FUT6)

Mollicone, Rosella; Candelier, Jean-Jacques; Reguigne, I.; Couillin, P.; Fletcher, Anne; Oriol, Rafaël

doi:10.1016/s1246-7820(94)80002-2

Cited by 29 publications

(12 citation statements)

References 27 publications

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“…The recently cloned rat GalNAc-T5 had a stem region of more than 500 residues, which underscores the fact that there are large differences outside the catalytic domain (7). One previous exception to this pattern of similarity was found with three of the ␣-1,4-fucosyltransferases (FUT3, FUT5, and FUT6) (26,27), which share an exceptionally high degree of sequence similarity. Interestingly, these three fucosyltransferases also share a similar simple genomic organization (one coding exon), and the genes localize to a single locus on chromosome 19 (28).…”

Section: Discussionmentioning

confidence: 96%

Cloning and Characterization of a Close Homologue of Human UDP-N-acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6

Bennett¹,

Hassan²,

Mandel³

et al. 1999

Journal of Biological Chemistry

178

177

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The UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, designated GalNAc-T3, exhibits unique functions. Specific acceptor substrates are used by GalNAc-T3 and not by other GalNAc-transferases. The expression pattern of GalNAc-T3 is restricted, and loss of expression is a characteristic feature of poorly differentiated pancreatic tumors. In the present study, a sixth human UDP-GalNAc:polypeptide N-acetylgalactosaminyltransferase, designated GalNAc-T6, with high similarity to GalNAc-T3, was characterized. GalNAc-T6 exhibited high sequence similarity to GalNAc-T3 throughout the coding region, in contrast to the limited similarity that exists between homologous glycosyltransferase genes, which is usually restricted to the putative catalytic domain. The genomic organizations of GALNT3 and GALNT6 are identical with the coding regions placed in 10 exons, but the genes are localized differently at 2q31 and 12q13, respectively. Acceptor substrate specificities of GalNAc-T3 and -T6 were similar and different from other GalNAc-transferases. Northern analysis revealed distinct expression patterns, which were confirmed by immunocytology using monoclonal antibodies. In contrast to GalNAc-T3, GalNAc-T6 was expressed in WI38 fibroblast cells, indicating that GalNAc-T6 represents a candidate for synthesis of oncofetal fibronectin. The results demonstrate the existence of genetic redundancy of a polypeptide GalNAc-transferase that does not provide full functional redundancy.

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Section: Discussionmentioning

confidence: 96%

Cloning and Characterization of a Close Homologue of Human UDP-N-acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6

Bennett¹,

Hassan²,

Mandel³

et al. 1999

Journal of Biological Chemistry

178

177

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“…FUT2 encodes the enzyme that synthesizes the H type 1, and FUT3 encodes the enzyme that synthesizes the Le a (13,70); in combination these two enzymes are responsible for synthesis of the Le b epitope. It should be noted that FUT1, which encodes the ␣1-2 fucosyltransferase responsible for H-blood group generation, does not contribute significantly to ␣1-2 fucosylation of HMGs.…”

Section: Specific Lectins and Antibodies Identify Determinants Of Thementioning

confidence: 99%

“…It is known that a different fucosyltransferase that is not FUT3 adds the ␣1-3 linked fucose on Le x and Le y structures. This enzyme prefers the type 2 precursor and is constitutively expressed in all milk donors (70,71); the Le x determinant is found to be more common in the milk of non-secretors (72). Previously, we noticed that the widely used anti-CD15 antibody does not recognize all Le x -containing HMGs (25).…”

Section: Specific Lectins and Antibodies Identify Determinants Of Thementioning

confidence: 99%

Human Milk Contains Novel Glycans That Are Potential Decoy Receptors for Neonatal Rotaviruses

Lasanajak

Song

et al. 2014

Molecular & Cellular Proteomics

118

126

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Human milk contains a rich set of soluble, reducing glycans whose functions and bioactivities are not well understood. Because human milk glycans (HMGs) have been implicated as receptors for various pathogens, we explored the functional glycome of human milk using shotgun glycomics. The free glycans from pooled milk samples of donors with mixed Lewis and Secretor phenotypes were labeled with a fluorescent tag and separated via multidimensional HPLC to generate a tagged glycan library containing 247 HMG targets that were printed to generate the HMG shotgun glycan microarray (SGM). To investigate the potential role of HMGs as decoy receptors for rotavirus (RV), a leading cause of severe gastroenteritis in children, we interrogated the HMG SGM with recombinant forms of VP8* domains of the RV outer capsid spike protein VP4 from human neonatal strains N155 (G10P[11]) and RV3(G3P[6]) and a bovine strain, B223 (G10P[11]). Glycans that were bound by RV attachment proteins were selected for detailed structural analyses using metadataassisted glycan sequencing, which compiles data on each glycan based on its binding by antibodies and lectins before and after exo-and endo-glycosidase digestion of the SGM, coupled with independent MS n analyses. These complementary structural approaches resulted in the identification of 32 glycans based on RV VP8* binding, many of which are novel HMGs, whose detailed structural assignments by MS n are described in a companion report. Although sialic acid has been thought to be important as a surface receptor for RVs, our studies indicated that sialic acid is not required for binding of glycans to individual VP8* domains. Remarkably, each VP8* recognized specific glycan determinants within a unique subset of related glycan structures where specificity differences arise from subtle differences in glycan structures. Molecular & Cellular Proteomics 13:

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“…In a previous report, we found that the expression levels of Golgi-related genes encoding glycosylation enzymes (sialyltransferase 4A (SIAT4A), sialyltransferase 10 (SIAT10), fucosyltransferase 1 (FUT1) and UDP-Nacetylhexosamine pyrophosphorylase-like 1 (UAP1L1)), a Golgi-structural protein (GCP60) and components of vesicular transport (syntaxin 3A, RAB20, WIPI49, Giantin and GM130) (Band and Kuismanen, 2005;Jeffries et al, 2004;Kitagawa and Paulson, 1994;Lutcke et al, 1994;Mio et al, 1998;Mollicone et al, 1994;Munro, 2011;Sohda et al, 2001;Taniguchi et al, 2001) were increased during Golgi stress (Oku et al, 2011). Analysis of the promoters of these genes revealed that their transcriptional induction in response to Golgi stress is commonly regulated by a novel enhancer element called the Golgi apparatus stress response element (GASE), whose consensus sequence is ACGTGGC.…”

Section: Introductionmentioning

confidence: 99%

TFE3 Is a bHLH-ZIP-type Transcription Factor that Regulates the Mammalian Golgi Stress Response

Taniguchi

Nadanaka

Tanakura

et al. 2015

Cell Struct. Funct.

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ABSTRACT. The Golgi stress response is a mechanism by which, under conditions of insufficient Golgi function (Golgi stress), the transcription of Golgi-related genes is upregulated through an enhancer, the Golgi apparatus stress response element (GASE), in order to maintain homeostasis in the Golgi. The molecular mechanisms associated with GASE remain to be clarified. Here, we identified TFE3 as a GASE-binding transcription factor. TFE3 was phosphorylated and retained in the cytoplasm in normal growth conditions, whereas it was dephosphorylated, translocated to the nucleus and activated Golgi-related genes through GASE under conditions of Golgi stress, e.g. in response to inhibition of oligosaccharide processing in the Golgi apparatus. From these observations, we concluded that the TFE3-GASE pathway is one of the regulatory pathways of the mammalian Golgi stress response, which regulates the expression of glycosylation-related proteins in response to insufficiency of glycosylation in the Golgi apparatus.

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Molecular genetics of α-L-fucosyltransferase genes (H, Se, Le, FUT4, FUT5 and FUT6)

Cited by 29 publications

References 27 publications

Cloning and Characterization of a Close Homologue of Human UDP-N-acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6

Cloning and Characterization of a Close Homologue of Human UDP-N-acetyl-α-d-galactosamine:Polypeptide N-Acetylgalactosaminyltransferase-T3, Designated GalNAc-T6

Human Milk Contains Novel Glycans That Are Potential Decoy Receptors for Neonatal Rotaviruses

TFE3 Is a bHLH-ZIP-type Transcription Factor that Regulates the Mammalian Golgi Stress Response

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