Studies on uridine-diphosphate-glucose

Paladini, Alejandro C.; Leloir, Luis F.

doi:10.1042/bj0510426

Cited by 659 publications

(134 citation statements)

References 9 publications

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“…; Paladini and Leloir, 1952). Standard monosaccharides and derivatives of these were run at 1 pmol/track and visualized by spraying with 1 ?LO aniline in 50% ethanol/O.l M citric acid (Montreuil and Spik, 1968).…”

Section: Paper Chromatographymentioning

confidence: 99%

Apparent lack of N‐glycosylation in the asexual intraerythrocytic stage of Plasmodium falciparum

Dieckmann-Schuppert

Bender

Odenthal-Schnittler

et al. 1992

European Journal of Biochemistry

118

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This study investigates protein glycosylation in the asexual intraerythrocytic stage of the malaria parasite, Plasmodium ,fakiparum, and the presence in the infected erythrocyte of the respective precursors.In in vitro cultures, P. fakiparum can be metabolically labeled with radioactive sugars, and its multiplication can be affected by glycosylation inhibitors, suggesting the capability of the parasite to perform protein-glycosylation reactions. Gel-filtration analysis of sugar-labeled malarial proteins before and after specific cleavage of N-glycans or 0-glycans, respectively, revealed the majority of the protein-bound sugar label to be incorporated into 0-glycans, but only little (7-12% of the glucosamine label) or no N-glycans were found. Analysis of the nucleotide sugar and sugar-phosphate fraction showed that radioactive galactose, glucosamine, fucose and ethanolamine were converted to their activated derivatives required for incorporation into protein. Mannose was mainly recovered as a bisphosphate, whereas the level of radiolabeled GDP-mannose was below the detection limit. The analysis of organic-solvent extracts of sugar-labeled cultures showed no evidence for the formation by the parasite of dolichol cycle intermediates, the dedicated precursors in protein N-glycosylation. Consistently, the amount of UDP-N-acetylglucosamine formed did not seem to be affected by the presence of tunicamycin in the culture. Oligosaccharyl-transferase activity was not detectable in a lysate of P. fakiparum, using exogenous glycosyl donors and acceptors.Our studies show that 0-glycosylation is the major form of protein glycosylation in intrderythrocytic P. julciparum, whereas there is little or no protein N-glycosylation. A part of these studies has been published in abstract form [Dieckmann-Schuppert, A,, Hensel, J. and Schwarz, R. T. (1991) Biol. Chem. Hoppe-Seyler 372,6451.Plasmodium fakiparum is the causative agent of human malignant malaria tropica. Despite huge efforts in vaccine and chemotherapy development, today this disease still causes the death of several million people/year (World Health Organization, 1989). A more thorough understanding of the biochemistry and cell biology of this parasite is required in order to develop better chemotherapy and vaccination strategies. One of the neglected areas of malaria biochemistry is the glycobiology of the parasite. Very little is known to date about the biological significance of oligosaccharides in P. julcipurum, be they linked to lipids or to proteins. Glycolipids may be membrane components and as such be potential antigens, or be involved in the formation of glycoproteins, e. g. dolichol

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Section: Paper Chromatographymentioning

confidence: 99%

Apparent lack of N‐glycosylation in the asexual intraerythrocytic stage of Plasmodium falciparum

Dieckmann-Schuppert

Bender

Odenthal-Schnittler

et al. 1992

European Journal of Biochemistry

118

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“…Paper chromatography of sugars was carried out with the butanol/acetic acid/water solvent of Partridge (1948) and the ethanol/ammonium acetate solvent of Paladini & Leloir (1952) as described for nucleotide chromatography. The sugar spots were developed by the silver nitrate method of Trevelyan, Procter & Harrison (1950).…”

Section: And E M Harpermentioning

confidence: 99%

“…yielded UPP and a sugar corresponding to acetylglucosamine in the solvents of Partridge (1948) and of Paladini & Leloir (1952). The positions of some sugars in this latter solvent, hitherto used only for nucleotides, are shown in Fig.…”

Section: Uridine Nucleotide Analysismentioning

confidence: 99%

A Comparison of the Uridine Pyrophosphoglycosyl Metabolism of Capsulated and Non-capsulated Pneumococci

Smith¹,

Mills²,

Harper³

1957

Journal of General Microbiology

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SUMMARY: A study has been made of the uridine pyrophosphoglycosyl compounds present in a non-capsulated pneumococcus (Streptococcus pneumoniae, strain R 19, derived from a type I1 organism) and a capsulated pneumococcus (type 111; Streptococcus pneumoniae, strain A66), and also of certain enzymes involved in the metabolism of these compounds. It has been found that both the pneumococcal strains contained considerable amounts of uridine pyrophosphoglucuronic acid (UPPGA) and uridine pyrophosphoacetylglucosamine (UPPAG), with lesser amounts of uridine pyrophosphoglucose (UPPG), uridine-5'-monophosphate (UMP), uridine pyrophosphate (UPP) and uridine triphosphate (UTP). The patterns shown by these two strains with respect to uridine nucleotide content were very similar.Cell-free extracts of strain R 19, derived from a type I1 organism, were obtained ; these extracts contained the following enzymes : glucose-6-phosphate dehydrogenase, uridyl transferase, inorganic pyrophosphatase, nucleoside diphosphokinase, hexokinase and phosphoglucomutase. Examination of the strain A 66 capsulated (type 111) organism showed the presence of uridyl transferase, nucleoside diphosphokinase and inorganic pyrophosphatase.

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“…The radioactivity was identified as UDP-5-C-glucose or its decomposition product. a-D-glucopyranose 1 ,2-cyclic phosphate (10). Preincubation with water or buffer alone did not produce a similar action.…”

Section: Resultsmentioning

confidence: 76%

“…Paper chromatography of nucleotides was performed as described by Paladini and Leloir (10). Paper electrophoresis was carried out according to Recondo et al (11) or with acetic acidpyridine buffer, pH 6.5, at 80 v/cm for 2 hr (4 ml of acetic acid, 100 ml of pyridine, and 900 ml of water).…”

Section: Methodsmentioning

confidence: 99%

Effect of Cetyltrimethylammonium Bromide on the Activity of Particulate Starch Synthetase from Potato Tuber

Lavintman

Cardini

1972

Plant Physiol.

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The action of some detergents on the incorporation of glucose from uridine diphosphate glucose or adenosine diphosphate glucose into the potato tuber starch grain was studied. It was found that the cationic detergent, cetyltrimethylammonium bromide, produces a rapid binding of both sugar nucleotides to the grain and a great increase in the incorporation of glucose into the polysaccharide. Kinetic constants of starch synthetase are also modified, there being an affinity increase for both sugar nucleotides. Neutral detergents are without effect and anionic detergents are inhibitors.In a previous communication (6) on the synthesis of sterylglucosides from UDP-glucose in amyloplasts of sweet corn endosperm, we have found that the cationic detergent, cetyltrimethylammonium bromide, inhibited that synthesis but increased considerably the incorporation of radioactivity into the grains. We have now tried to investigate the latter effect to see if it was related to an increase in the activity of starch synthetase (UDP-glucose: a-1,4-glucan a-4-glucosyltransferase, EC 2.4.1.21) included inside the grain (4,8,12) or to some modification of the permeability of the granule.

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Studies on uridine-diphosphate-glucose

Cited by 659 publications

References 9 publications

Apparent lack of N‐glycosylation in the asexual intraerythrocytic stage of Plasmodium falciparum

Apparent lack of N‐glycosylation in the asexual intraerythrocytic stage of Plasmodium falciparum

A Comparison of the Uridine Pyrophosphoglycosyl Metabolism of Capsulated and Non-capsulated Pneumococci

Effect of Cetyltrimethylammonium Bromide on the Activity of Particulate Starch Synthetase from Potato Tuber

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