Inhibition of protein, glycoprotein, ribonucleic acid and deoxyribonucleic acid synthesis by D-glucosamine and other sugars in mouse leukemic cells L5178Y and selective inhibition in SV-3T3 compared with 3T3 cells.

@article{Bosmann1971InhibitionOP,
  title={Inhibition of protein, glycoprotein, ribonucleic acid and deoxyribonucleic acid synthesis by D-glucosamine and other sugars in mouse leukemic cells L5178Y and selective inhibition in SV-3T3 compared with 3T3 cells.},
  author={H. Bruce Bosmann},
  journal={Biochimica et biophysica acta},
  year={1971},
  volume={240 1},
  pages={
          74-93
        }
}
  • H. Bosmann
  • Published 17 June 1971
  • Biology, Chemistry
  • Biochimica et biophysica acta
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42 Citations
Highly Influential Citations
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42 Citations

The inhibition of thymidine kinase in glial tumor cells by an amino sugar, D-glucosamine.

Thymidine kinase activity in rat C6 glioma cells is inhibited by 50 to 70% after 4 hr incubation with 20 mM D-glucosamine, and the kinetics of recovery of amino acid incorporation from inhibition was rapid, but the activity was depressed for at least 6 hr after drug washout.

Selective inhibition of herpes simplex virus glycoprotein synthesis by a benz-amidinohydrazone derivative

Benzhydrazone reduced HSV glycoprotein synthesis selectively since it did not significantly modify i) the saccharide uptake into glycoproteins of uninfected and of Sindbis virus-infected cells, and ii) viral growth and cell fusion in paramyxovirus- infected cells, two activities which depend on viral glycop protein synthesis.

Nucleotide contents of ascites hepatoma cells and their changes induced by D-galactosamine.

The extremely low UDP-glucose levels in both hepatoma cell lines may explain the virtual absence of glycogen and the relative ratios of adenosine phosphates determined by direct enzymatic analysis are significantly higher than those obtained by chromatographic separation of the nucleotides after labeling with adenosines-8- 14 C.

D-glucosamine down-regulates HIF-1alpha through inhibition of protein translation in DU145 prostate cancer cells.

Effect of D-glucosamine on growth and several functions of cultured mastocytoma P-815 cells.

The elevation of cAMP levels was the earliest detectable change, indicating that growth and functions of mastocytoma cells are also regulated by cAMP, and suggesting the necessity of intact membrane structure for the action of glucosamine.

Uridylate trapping induced by the C-2-modified D-glucose analogs glucosone, fluoroglucose, and glucosamine.

The depletion of UTP, induced by these C-2-modified d-glucose analogs, and additionally of GTP in the case of fluoroglucose, represent a metabolic lesion that may explain their growth inhibitory and cytotoxic effects.

Suppression of human natural killer cell activity by amino sugars.

D-glucosamine inhibits proliferation of human cancer cells through inhibition of p70S6K.

Utilization of hexoses and synthesis of glycogen in two strains of HeLa cells.

In one of the cell strains, the glycolytic breakdown of mannose was relatively inefficient, resulting in toxic morphological manifestations and in markedly reduced growth, while in the other cell strain some competition was observed also with D-fructose, D-galactose, and 3-O-methylglucose.

Transport and metabolism of glucosamine by cultured Novikoff rat hepatoma cells and effects on nucleotide pools.

It is suggested that transport of glucosamine is a reaction distinct from phosphorylation, as estimated from initial uptake rates, by cultured Novikoff rat hepatoma cells in glucose-free basal medium following normal Michaelis-Menten kinetics.

26 References

Inhibitory effect of D-glucosamine and other sugars on the biosynthesis of protein, ribonucleic acid, and deoxyribonucleic acid in normal and neoplastic tissues.

The effect of exogenous glucosamine in vitro on the incorporation of the labeled precursors into normal tissues was much less than that into neoplastic tissues.

The effect of D-glucosamine on the adenine and uridine nucleotides of sarcoma 180 ascites tumor cells.

Glycoprotein biosynthesis. Subcellular localization and activity in 3T3 and SV‐3T3 fibroblasts of glycoprotein. N‐acetylglucosaminyl transferases

Alternative pathways of glucose metabolism. II. Nucleotides from the acid-soluble fraction of normal and tumor tissues and studies on nucleic acid synthesis in tumors.

Since the free adenine nucleotides of the livers of the tumor-bearing animals contained no demonstrable radioactivity at 1 hour, while the total acid-soluble radioactivity of the livers was about the same as that of the tumors, further study of the non-nucleotide radioactive of the acid- soluble fraction may indicate how the flow of glucose to the pentose moieties of the nucleotide is regulated.

Glycoprotein biosynthesis: the characterization of two glycoprotein:frucosyl transferases in HeLa cells.

The effect of N-acetylglucosamine and glucosamine on carbohydrate metabolism in rat liver slices.

  • R. Spiro
  • Biology, Chemistry
    The Journal of biological chemistry
  • 1958

SYNTHESIS OF GLYCOPROTEIN, GLYCOLIPID, PROTEIN, AND LIPID IN SYNCHRONIZED L5178Y CELLS

Cell protein was found to be synthesized throughout the cell cycle, with the highest synthesis occurring in the S period; synthesis was depressed in the M period; and secreted glycoprotein was similar to secreted protein.

Intraneural mitochondria. Incorporation of amino acids and monosaccharides into macromolecules by isolated synaptosomes and synaptosomal mitochondria.

Glycoprotein and glycolipid synthesis in the intraneural mitochondria showed a marked requirement for divalent cations, with Mn++ being the best activator; some ions substituted for Mn++ but others were inhibitory to incorporation.

Inhibition of Glycoprotein Synthesis in L5178Y Mouse Leukaemic Cells by L-Asparaginase in vitro

  • H. BRUCE BOSMANND. Kessel
  • Biology, Chemistry
    Nature
  • 1970
The preparation of L-asparaginase was free of contaminating enzymatic activity, although it was slightly active, and the synthesis of carbohydrate–amino-acid linkages in glycoproteins which involve the amide group of asparagine and N-acetyl-glucosamine residues was investigated.

The metabolism of glucosamine by tissue culture cells.