Effects of L‐asparaginase on protein and glycoprotein synthesis

  title={Effects of L‐asparaginase on protein and glycoprotein synthesis},
  author={David Kessel and H. Bruce Bosmann},
  journal={FEBS Letters},
The anti-neoplastic enzyme L-asparaginase inhibits the growth of certain malignant cells by interference with cell nutrition [ 1,2] . We have recently reported [3] that Lasparaginase inhibits the incorporation of labeled L-fucose and D-glucosamine into glycoproteins of L5 178Y murine leukemia cells. Three questions arise with respect to this finding: 1) Is the inhibition of glycoprotein synthesis a consequence of a general inhibition of all protein formation? 2) Can the observed results be… Expand
A rapid and efficient method of radioactively labeling L‐asparaginase
A method is described for the production of radioactively labeled ASNase, an enzyme that hydrolyzes the amide group of asparagine that inhibits the growth of certain neoplasms and may have early effects on the cell plasma membrane topography, fluidity, and electrokinetic properties. Expand
L-asparaginase effects on intact murine leukemia cells and on isolated cell plasma membranes.
The mechanism of asparaginase action involves inhibition of glycoprotein and protein synthesis required for main-tenance of membrane structure, rather than a direct lytic action on preformed membranes of the intact cell. Expand
Expression and characterization of recombinant l-asparaginase from Pseudomonas fluorescens.
The enzyme exhibited a high affinity towards l-asparagine and showed a very minimal activity with glutamine as a substrate and demonstrated deglycosylation activity which could exhibit an additional barrier for proliferating cancer cells. Expand
L-asparaginase inhibits invasive and angiogenic activity and induces autophagy in ovarian cancer
Data and the known mechanism of action of L‐ASP on glycosylation of nascent proteins suggest that L‐ ASP reduces of ovarian cancer dissemination and progression through modification of its microenvironment. Expand
L-asparaginase pharmacokinetics and asparagine levels in cerebrospinal fluid of rhesus monkeys and humans.
Data indicate that systemic L-asparaginase therapy may be a feasible means of treating central nervous system involvement in patients with acute lymphoblastic leukemia and that there is no therapeutic advantage to using intrathecal L- asparagine. Expand
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The results suggest that the methylation of tRNA in murine leukemic cells may be modulated in cells with drug-resistant properties. Expand
Electrokinetic properties of asparaginase sensitive or resistant mouse leukemic cells treated with L-asparaginase
Abstract The electrophoretic mobility of L5178Y cells in 0.0145 M NaCl, 4.5% sorbitol, 0.6 mM NaHCO 3 , pH 7.2, at 25°C was — 1.78 μ·s −1 ·V −1 ·cm −1 while that of an L -asparaginase resistantExpand
L-Asparaginase: Basic Aspects
L-Asparaginase (L-asparagine amidohydrolase, E.C. catalyzes the hydrolysis of L-asparagine to yield L-aspartic acid and ammonia. The enzyme was first reported by Lang (1904), who demonstratedExpand
Asparaginyl-transfer RNA: a substrate for L-asparaginase.
  • D. Kessel
  • Biology, Medicine
  • Biochimica et biophysica acta
  • 1971
Abstract The enzyme l -asparaginase (E.C. could convert asparaginyl-tRNAAsn to aspartyl-tRNAAsn, although at a rate slower by a factor of 2.5 · 107 than the analogous conversion of lExpand
Haemostatic alterations induced by treatment with asparaginases and clinical consequences.
Therapeutic or prophylactic heparin doses are only partially effective, and direct thrombin or factor Xa inhibitors could play significant roles in the near future. Expand


Inhibition of Glycoprotein Synthesis in L5178Y Mouse Leukaemic Cells by L-Asparaginase in vitro
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. Expand
The requirement for L-asparagine of mouse leukemia cells L5178Y in culture.
Among the compounds tested, the requirement for the amide is replaced only by certain peptide derivatives of asparagine, and these are less active on a molar basis than is l-Asparagine; l-aspartic acid, d-asparagin, and l-glutamine are inactive. Expand
Glutaminase activity of L-asparagine amidohydrolase.
Observations point strongly to the presence of a single enzymatic site of Escherechia coliL-asparagine amido-hydrolase, however, the two activities have different pH dependencies. Expand
The synthesis of deoxyribonucleic acid by Lymphoma 6C3HED-OG cells, as measured by the incorporation of thymidme-H3, was also altered by exposure of the lymphoma cells to the effects of heated guinea pig serum in vivo, and DNA synthesis by -OG cells normally proceeds at an intense level that leads to some 60% of these cells being heavily labeled in autoradiographs. Expand
Evaluation of 4-(2-Hydroxyethyl)-1-piperazineëthanesulfonic Acid (HEPES) as a Tissue Culture Buffer∗
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HEPES had a minimal effect on the oxidation-reduction potential of well-poised media and had no effect on rubella virus titrations or on hemagglutination assays of polyoma or Sendai virus. Expand
L-asparaginase and L-asparagine metabolism.
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