Characterization of a sialate pyruvate-lyase in the cytosol of human erythrocytes

Bulai, Tatiana; Bratosin, Daniela; Artenie, Vlad; Montreuil, Jean

doi:10.1016/s0300-9084(02)01436-0

Cited by 18 publications

(16 citation statements)

References 28 publications

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“…2) is not considered reversible due to involvement of GNE, there are likely other pathways for the turnover of Neu5Gc that are just starting to be exploited. The breakdown of Neu5Gc into ManNGc is well described (67,68), and in our preceding paper (1), we propose a pathway for degradation of Neu5Gc, also demonstrating subsequent turnover of ManNGc into GlcNGc. In addition, our accompanying paper (5) shows that mammalian cells are able to incorporate exogenous GlcNGc to form UDP-GlcNGc via the GlcNAc salvage pathway and subsequent incorporation as O-GlcNGc modification.…”

Section: Exogenous Galngc Incorporates As Glcngc Into Cellularsupporting

confidence: 72%

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

Bergfeld

Pearce

Díaz

et al. 2012

Journal of Biological Chemistry

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Background: N-Acetylhexosamines are precursors of all major vertebrate glycan types. Results: Mammalian cells can incorporate N-glycolylgalactosamine (GalNGc) and N-glycolylglucosamine (GlcNGc) into most major cellular glycans and utilize GalNGc for de novo biosynthesis of Neu5Gc. Conclusion: N-Acetylhexosamine biosynthetic pathways and glycan assembly are mostly tolerant toward the N-glycolyl substituent. Significance: Catabolism of Neu5Gc might create novel N-glycolylated glycan epitopes in vivo.

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Section: Exogenous Galngc Incorporates As Glcngc Into Cellularsupporting

confidence: 72%

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

Bergfeld

Pearce

Díaz

et al. 2012

Journal of Biological Chemistry

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“…For the measurement of Neu5Ac lyase activity, the reaction was initiated by the addition of 500 l of the cytosol (about 16 g of total proteins) as an enzyme source to 25 l of 32 mM Neu5Ac in aqueous solution and 75 l of 1 M potassium phosphate buffer, pH 7.4. After incubation at 37°C for 2 h, the reaction was stopped by heating at 96°C for 3 min, and the liberated ManNAc was determined by a colorimetric method using p-dimethylamino-benzaldehyde as described elsewhere (4,31). One unit of Neu5Ac lyase activity is defined as the amount that releases 1 mol of ManNAc per min under the reaction conditions used.…”

Section: Methodsmentioning

confidence: 99%

The Capability of Catabolic Utilization of N -Acetylneuraminic Acid, a Sialic Acid, Is Essential for Vibrio vulnificus Pathogenesis

Jeong

Kim

et al. 2009

Infect Immun

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N-acetylneuraminic acid (Neu5Ac, sialic acid) could provide a good substrate for enteropathogenic bacteria in the intestine, when the bacteria invade and colonize in human gut. In order to analyze the role of Neu5Ac catabolism in Vibrio vulnificus pathogenesis, a mutant with disruption of the nanA gene encoding Neu5Ac lyase was constructed by allelic exchanges. The nanA mutant was not able to utilize Neu5Ac as a sole carbon source and revealed an altered colony morphotype with reduced opacity in the presence of Neu5Ac. Compared to the wild type, the nanA mutant exhibited a low level of cytotoxicity toward INT-407 epithelial cells in vitro and reduced virulence in a mouse model. The disruption of nanA also resulted in a substantial decrease in histopathological damage in jejunum and colon tissues from the mouse intestine. These results indicated that NanA plays an important role in V. vulnificus pathogenesis. In addition, the nanA mutant was significantly diminished in growth with and adherence to INT-407 epithelial cells in vitro, and was defective for intestinal colonization, reflecting the impaired ability of the mutant to grow and survive with, persist in, and adhere to the intestine in vivo. Consequently, the combined results suggest that NanA and the capability of catabolic utilization of Neu5Ac contribute to V. vulnificus virulence by ensuring growth, adhesion, and survival during infection.

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“…B, proposed pathway for the metabolic turnover of excess Neu5Gc in mammalian cells. Neu5Gc is known be a substrate for the pyruvate lyase, which results in the formation of ManNGc (a) (41,42). Following epimerization from ManNGc toward GlcNGc, which is potentially catalyzed by the GlcNAc-2Ј-epimerase (b) (73,74,90), phosphorylation of GlcNGc in the 6 position might occur by action of the GlcNAc kinase (c) (75,76) resulting in the formation of GlcNGc-6-P.…”

Section: Cmah-deficient Human and Mouse Cells Do Not Synthesize Neu5gmentioning

confidence: 99%

“…Examples include the CMP-sialic acid synthetase from various animals, including humans (39) and mammalian sialyltransferases (40). Moreover, mammalian N-acetylneuraminate pyruvate-lyase was found to release pyruvate from Neu5Ac and Neu5Gc to give ManNAc and ManNGc, respectively (41,42). In this study, we hypothesized that additional enzymes involved in further breakdown of ManNAc and ManNGc may also tolerate the N-glycolyl group.…”

mentioning

confidence: 99%

“…However, the other steps of the degradative pathway are potentially reversible. The human sialate pyruvatelyase has already been demonstrated to cleave Neu5Gc at ϳ60% of the rate obtained for Neu5Ac (41), and cultured rodent neural cells have been demonstrated to efficiently incorporate per-O-acetylated ManNGc (per-O-acetyl-ManNGc) from the feeding media and convert it to Neu5Gc (80). Peracetylation has previously been shown to greatly enhance uptake of carbohydrates in cells (81) and increased conversion of ManNGc into Neu5Gc up to 100-fold (80).…”

mentioning

confidence: 99%

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Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

Bergfeld

Pearce

Díaz

et al. 2012

Journal of Biological Chemistry

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Background: Pathways for turnover and degradation of the mammalian sialic acid N-glycolylneuraminic acid (Neu5Gc) are currently unknown. Results: Mammalian cells can degrade Neu5Gc by sequential conversion into N-glycolylmannosamine, N-glycolylglucosamine, and N-glycolylglucosamine 6-phosphate, following release of glycolate and glucosamine 6-phosphate. Conclusion: Basic N-acetylhexosamine pathways seem tolerant toward the N-glycolyl substituent. Significance: We elucidate the metabolic turnover of the diet-derived human xeno-autoantigen Neu5Gc.

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Characterization of a sialate pyruvate-lyase in the cytosol of human erythrocytes

Cited by 18 publications

References 28 publications

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

The Capability of Catabolic Utilization of N -Acetylneuraminic Acid, a Sialic Acid, Is Essential for Vibrio vulnificus Pathogenesis

Metabolism of Vertebrate Amino Sugars with N-Glycolyl Groups

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