Study of the conversion of GDP‐mannose into GDP‐fucose in Nereids: a biochemical marker of oocyte maturation

Bulet, Philippe; Hoflack, Bernard; Porchet, M.; Verbert, André

doi:10.1111/j.1432-1033.1984.tb08458.x

Cited by 26 publications

(22 citation statements)

References 11 publications

(1 reference statement)

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“…An explanation for these low values would be metabolic conversions of mannose, leading to products other than GDP-mannose, such as GDP-fucose, as has been shown in both mammalian cells (Martin et al, 1989) and non-mammalian cells (Bulet et al, 1984). Such a possibility had been proposed earlier by Ginsburg (1961).…”

Section: Resultsmentioning

confidence: 89%

The effect of increasing nucleotide-sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes

Rijcken

Overdijk

Eijnden

et al. 1995

Biochemical Journal

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Treatment of rat hepatocytes with 0.5 mM concentrations ofThe latter increase did not result in an increased incorporation of uridine and cytidine results in increased cellular concentrations radioactivity into the glycoconjugates. It was estimated that, in of UTP, UDP-sugars and CTP, whereas that of CMP-Nuntreated cells, the ratio of radioactivity incorporated from acetylneuraminate remained unchanged [Pels Rijcken, Overdijk, [3H]glucosamine into glycoconjugate-bound N-acetylhexosamine Van den Eijnden and Ferwerda (1993) Biochem. J. 293,207-213]. and N-acetylneuraminate amounted to 2:3. In pretreated cells The incorporation of radioactivity from 3H-labelled sugars into this ratio changed to approx. 2: 1. Overall, the data show that the cell-associated and secreted glycoconjugate fraction was pretreatment resulted in an increased incorporation of N-acetylinfluenced by these altered cellular concentrations of the nucleohexosamine into cell-associated and secreted glycoconjugates, tides. For [3H]glucosamine, pretreatment with uridine resulted in accompanied by a reduction in sialylation. It was concluded that a reduction of the glycosylation in both fractions. Increases in an increased availability of UDP-N-acetylhexosamine caused the the secreted fractions were observed for fucose with both uridine increased incorporation of N-acetylhexosamine. The elevated and cytidine and for N-acetylglucosamine with uridine only. This study demonstrates that protein glycosylation can be acetylmannosamine, the specific radioactivity of CMP-N-acetylregulated at the level of the availability of the various nucleotideneuraminate showed an almost 2-fold increase on pretreatment.sugars in the Golgi lumen.

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Section: Resultsmentioning

confidence: 89%

The effect of increasing nucleotide-sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes

Rijcken

Overdijk

Eijnden

et al. 1995

Biochemical Journal

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“…Another serious problem of this reaction cascade is the instability of GDP-6-deoxy-D-lyxo-4-hexulose. Recently, groups working with Perinereis cultrifera and A. thaliana have also observed instability of GDP-6-deoxy-D-lyxo-4-hexulose (14,15), and the same has been reported for dTDP-6-deoxy-L-lyxo-4-hexulose (29,48). Because of the instability of dTDP-6-deoxy-L-lyxo-4-hexulose, this substrate was generated in situ for kinetic analysis of dTDP-6-deoxy-L-lyxo-4-hexulose reductase (29).…”

Section: Discussionmentioning

confidence: 99%

“…1). The first step is the dehydration of GDP-D-mannose (GDP-mannose 4,6-dehydratase, Gmd), which leads to the unstable intermediate GDP-6-deoxy-D-lyxo-4-hexulose (14,15). This keto-derivative is further converted to the final product GDP-D-rhamnose by the action of GDP-6-deoxy-D-lyxo-4-hexulose reductase (Rmd).…”

Section: S-layersmentioning

confidence: 99%

Identification of Two GDP-6-deoxy-d-lyxo-4-hexulose Reductases Synthesizing GDP-d-rhamnose in Aneurinibacillus thermoaerophilus L420-91T

Kneidinger

Graninger

Adam

et al. 2001

Journal of Biological Chemistry

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The glycan repeats of the surface layer glycoprotein of Aneurinibacillus thermoaerophilus L420-91 T contain Drhamnose and 3-acetamido-3,6-dideoxy-D-galactose, both of which are also constituents of lipopolysaccharides of Gram-negative plant and human pathogenic bacteria. The two genes required for biosynthesis of the nucleotide-activated precursor GDP-D-rhamnose, gmd and rmd, were cloned, sequenced, and overexpressed in Escherichia coli. The corresponding enzymes Gmd and Rmd were purified to homogeneity, and functional studies were performed. GDP-D-mannose dehydratase (Gmd) converted GDP-D-mannose to GDP-6-deoxy-D-lyxo-4-hexulose, with NADP ؉ as cofactor. The reductase Rmd catalyzed the second step in the pathway, namely the reduction of the keto-intermediate to the final product GDP-D-rhamnose using both NADH and NADPH as hydride donor. The elution behavior of the intermediate and end product was analyzed by high performance liquid chromatography. Nuclear magnetic resonance spectroscopy was used to identify the structure of the final product of the reaction sequence as GDP-␣-D-rhamnose. This is the first characterization of a GDP-6-deoxy-Dlyxo-4-hexulose reductase. In addition, Gmd has been shown to be a bifunctional enzyme with both dehydratase and reductase activities. So far, no enzyme catalyzing these two types of reactions has been identified. Both Gmd and Rmd are members of the SDR (short chain dehydrogenase/reductase) protein family.

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“…The message for human GDP-mannose 4,6-dehydratase is expressed in all tissues examined, albeit at varying levels. The varying levels of expression of the dehydratase message suggest the enzyme may be regulated at the level of transcription, and in fact there is evidence for developmental regulation in rat and nereids (29,30). It also appears that, in both humans and E. coli, GDP-fucose biosynthesis is regulated by feedback inhibition of the dehydratase by GDPfucose, the final product in the pathway.…”

Section: Characterization Of Gdp-4-keto-6-deoxymannose By Esi-msmentioning

confidence: 99%

Molecular Cloning of Human GDP-mannose 4,6-Dehydratase and Reconstitution of GDP-fucose Biosynthesis in Vitro

Sullivan¹,

Kumar²,

Kriz³

et al. 1998

Journal of Biological Chemistry

143

128

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We have cloned the cDNA encoding human GDP-mannose 4,6-dehydratase, the first enzyme in the pathway converting GDP-mannose to GDP-fucose. The message is expressed in all tissues and cell lines examined, and the cDNA complements Lec13, a Chinese Hamster Ovary cell line deficient in GDP-mannose 4,6-dehydratase activity. The human GDP-mannose 4,6-dehydratase polypeptide shares 61% identity with the enzyme from Escherichia coli, suggesting broad evolutionary conservation. Purified recombinant enzyme utilizes NADP ؉ as a cofactor and, like its E. coli counterpart, is inhibited by GDPfucose, suggesting that this aspect of regulation is also conserved. We have isolated the product of the dehydratase reaction, GDP-4-keto-6-deoxymannose, and confirmed its structure by electrospray ionization-mass spectrometry and high field NMR. Using purified recombinant human GDP-mannose 4,6-dehydratase and FX protein (GDP-keto-6-deoxymannose 3,5-epimerase, 4-reductase), we show that the two proteins alone are sufficient to convert GDP-mannose to GDP-fucose in vitro. This unequivocally demonstrates that the epimerase and reductase activities are on a single polypeptide. Finally, we show that the two homologous enzymes from E. coli are sufficient to carry out the same enzymatic pathway in bacteria.Fucose is found as a component of glycoconjugates such as glycoproteins and glycolipids in a wide range of species from humans to bacteria. For example, fucose is a component of the capsular polysaccharides and antigenic determinants of bacteria, while in mammals fucose is present in many glycoconjugates, the most widely known being the human blood group antigens. Fucose-containing glycoconjugates have been implicated as playing key roles in embryonic development in the mouse (1) and more recently in the regulation of the immune response, specifically as a crucial component of the selectin ligand sialyl Lewis X (reviewed in Refs. 1 and 2). In all cases, fucose is transferred from GDP-fucose to glycoconjugate acceptors by specific transferases. Thus, defects in GDP-fucose biosynthesis will affect all fucosylation within the cell. Recently, individuals deficient in the biosynthesis of GDP-fucose have been identified (3, 4) and suffer from the immune disorder leukocyte adhesion deficiency type II (LADII).1 These patients fail to synthesize fucosylated blood groups, and their leukocytes do not express the fucose containing carbohydrate sialyl Lewis X. The patient's leukocytes do not extravasate normally, which leads to recurrent infections.In his pioneering work in the early 1960s, Ginsberg (5, 6) elucidated the enzymatic pathway converting GDP-mannose to GDP-fucose. Later, Yurchenco and Atkinson (7) showed that this was the primary biosynthetic route to GDP-fucose. As shown in Fig. 1, GDP-mannose is converted to GDP-fucose by GDP-mannose 4,6-dehydratase via the oxidation of mannose at C-4 followed by the reduction of C-6 to a methyl group, yielding GDP-4-keto-6-deoxymannose. The reaction has been reported to proceed with transfer of a hydride fro...

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Study of the conversion of GDP‐mannose into GDP‐fucose in Nereids: a biochemical marker of oocyte maturation

Cited by 26 publications

References 11 publications

The effect of increasing nucleotide-sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes

The effect of increasing nucleotide-sugar concentrations on the incorporation of sugars into glycoconjugates in rat hepatocytes

Identification of Two GDP-6-deoxy-d-lyxo-4-hexulose Reductases Synthesizing GDP-d-rhamnose in Aneurinibacillus thermoaerophilus L420-91T

Molecular Cloning of Human GDP-mannose 4,6-Dehydratase and Reconstitution of GDP-fucose Biosynthesis in Vitro

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