THE SUBCELLULAR LOCALIZATION OF CYTIDINE 5′‐MONOPHOSPHO‐<i>N</i>‐ACETYLNEURAMINIC ACID SYNTHETASE IN CALF BRAIN

Eijnden, D. H. Van Den

doi:10.1111/j.1471-4159.1973.tb07539.x

Cited by 43 publications

(15 citation statements)

References 34 publications

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“…2), as has been shown for other sugar-nucleotide synthetases (Coates et al, 1980). In contrast, CMP-NeuAc synthetase activity was predominantly localized in the nuclear fraction, which is in agreement with the results reported by others (Kean, 1970;Gielen et al, 1970Gielen et al, , 1971Van den Eijnden, 1973;Van Dijk et al, 1973;Coates et al, 1980). No CMP-NeuAc synthetase activity was detected in the soluble cell fraction.…”

Section: Subcellular Localizationsupporting

confidence: 82%

“…No CMP-NeuAc synthetase activity was detected in the soluble cell fraction. This might be due to our mild homogenization technique resulting in few broken nuclei or to inactivation of the non-nucleus-bound enzyme by sucrose (Van den Eijnden, 1973). We did not dialyse our fractions, because sucrose did not influence our radioactive assay.…”

Section: Subcellular Localizationmentioning

confidence: 99%

“…The synthesis of NeuAc from UDP-GlcNAc is thought to be cytosol-mediated. The NeuAc-activating enzyme, CMP-NeuAc synthetase (CTP:Nacetylneuraminic acid cytidylyltransferase, EC 2.7.7.43), has been found in the nucleus of many tissues (Kean, 1970;Gielen et al, 1970Gielen et al, , 1971; Van den Eijnden, 1973;Van Dijk et al, 1973;Coates et al, 1980). CMP-NeuAc appears to be used in the Golgi system, since the sialyltransferases are mainly present in this organelle (Schachter, 1974;Carey & Hirschberg, 1980Creek & Morre, 1981).…”

mentioning

confidence: 99%

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Subcellular localization and tissue distribution of sialic acid precursor-forming enzymes

Rinsum¹,

Dijk²,

Hooghwinkel³

et al. 1983

Biochemical Journal

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The enzymes UDP-N-acetylglucosamine pyrophosphorylase, UDP-N-acetylglucosamine 2-epimerase, N-acetylmannosamine kinase, N-acetylglucosamine kinase and N-acetylglucosamine 2-epimerase, which are involved in the metabolism of N-acetylneuraminic acid, were studied in rat with regard to their subcellular localization and tissue distribution. The subcellular distribution studies in liver indicated that the enzymes are localized in the soluble cell fraction. In other tissues the comparison of enzyme activities in homogenates with that in high-speed supernatants led to a similar conclusion. UDP-N-acetylglucosamine pyrophosphorylase, N-acetylglucosamine kinase and N-acetylglucosamine 2-epimerase were detected in almost all tissues studied. UDP-N-acetylglucosamine 2-epimerase and N-acetylmannosamine kinase, two enzymes considered to be key enzymes in the N-acetylneuraminic acid biosynthesis, were detected only in sialoglycoprotein-secreting tissues, i.e. liver, salivary gland and intestinal mucosa. The low activity of the key enzymes in other tissues suggests that the biosynthetic pathway of N-acetylneuraminic acid is not the same in various tissues.

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Section: Subcellular Localizationsupporting

confidence: 82%

Section: Subcellular Localizationmentioning

confidence: 99%

mentioning

confidence: 99%

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Subcellular localization and tissue distribution of sialic acid precursor-forming enzymes

Rinsum¹,

Dijk²,

Hooghwinkel³

et al. 1983

Biochemical Journal

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“…It is known that the sialic acid-activating enzyme, CMPNeuAc (N-acetylneuraminate) synthase (EC 2.7.7.43) is located in the nucleus [2][3][4][5][6][7], whereas all other known sugar-activating enzymes are located in the cytosol [6,7]. Until now the reason for this peculiar localization is unknown, although it is questionable whether the enzyme is functionally active in the nucleus [8].…”

Section: Introductionmentioning

confidence: 99%

Pyrimidine metabolism and sugar nucleotide synthesis in rat liver

Rijcken

Hooghwinkel

Ferwerda

1990

Biochemical Journal

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With radioactive precursors, the labelling kinetics of the soluble pyrimidine nucleotides and of RNA were measured in rat liver to determine the contribution of the metabolic flows through synthesis de novo and the salvage pathway. To separate and quantify all pyrimidine nucleotides, an h.p.l.c. technique was developed using anion-exchange chromatography and reversed-phase chromatography. The concentrations of cytidine nucleotides were in the range of 30-45 nmol/g wet weight, and the concentrations of the uridine phosphates and of the UDP-sugars were approx. 6 and 20 times higher respectively. After a single injection of [14C]orotic acid and of [3H]cytidine, the specific radioactivities were determined as a function of time. The 1'C/3H ratio was calculated and gave a good indication of the involvement of the different flows. It could be concluded that UTP derived from synthesis de novo and from the salvage pathway is not completely mixed before being utilized. The flow of the salvage pathway is relatively more directed to RNA synthesis in the nucleus and that of synthesis de novo to cytoplasmic processes. For CTP it could also be concluded that the flow of the salvage pathway was relatively more directed to RNA synthesis in the nucleus. Because of the nuclear localization of the enzyme CMP-NeuAc (N-acetylneuraminate) synthase, special attention was paid to CMP-NeuAc. However, a conclusion about a location about the synthesis of CMP-NeuAc could not unequivocally be drawn, because of the small differences in 14C/3H ratio and the different values for the CDP-lipids.

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“…The synthetase has not been detected in mammalian red cells (12), but has been detected in most nucleated cells and is localized only within the nucleus of the cell (13)(14)(15). It might be argued, therefore, that the nucleated chicken erythrocyte would have the capability to make available CMP-N-acylneuraminate to the sialyltransferase to resialate the cell surface and thereby remain in circulation.…”

mentioning

confidence: 99%

Effect of galactose oxidase, with and without prior sialidase treatment, on the viability of erythrocytes in circulation.

Bell

Levy

Williams

et al. 1977

Proc. Natl. Acad. Sci. U.S.A.

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Previous studies have shown that sialidasetreated mammalian erythrocytes were rapidly eliminated from circulation. In contrast, chicken asialoerythrocytes remained fully viable. This investigation was undertaken to ascertain the reason for this difference in behavior as well as to determine the extent of the similarity of the physiological mechanism for the elimination from circulation of asialoglycoproteins and mammalian asialoerythrocytes. To that end, erythrocytes from dogs, rabbits, and chickens were each subjected to the action of galactose oxidase (D-galactose:oxygen 6-oxidoreductase; EC 1.1.3.9) both before and after sialidase (acylneuraminyl hydrolase; EC 3.2.1.18) treatment. The viability of the autologously transfused erythrocytes in circulation was monitored by Na251CrO4 labeling. Galactose oxidase had no deleterious effect on the viability of either dog or chicken erythrocytes, nor did it restore the viability of dog or rabbit asialoerythrocytes. On the other hand, desialated chicken erythrocytes, which were fully viable, were rendered nonviable upon treatment with galactose oxidase. It may be concluded therefore that (a) the physiological mechanism of elimination of mammalian asialoerythrocytes from circulation is not the same as that for plasma asialoglycoproteins and (b) the treatment of chicken asialoerythrocytes with galactose oxidase results in the oxidation at carbons 6 of the galactosyl-or N-acetylgalactosaminyl residues, thereby rendering the erythrocytes nonviable.

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THE SUBCELLULAR LOCALIZATION OF CYTIDINE 5′‐MONOPHOSPHO‐N‐ACETYLNEURAMINIC ACID SYNTHETASE IN CALF BRAIN

Cited by 43 publications

References 34 publications

Subcellular localization and tissue distribution of sialic acid precursor-forming enzymes

Subcellular localization and tissue distribution of sialic acid precursor-forming enzymes

Pyrimidine metabolism and sugar nucleotide synthesis in rat liver

Effect of galactose oxidase, with and without prior sialidase treatment, on the viability of erythrocytes in circulation.

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