Asparagine Synthetase Activity in Malignant and Non-malignant Human Kidney and Prostate Specimens

Prager, Morton D.; Peters, Paul C.; Janes, Jefferson O.; Derr, Ina

doi:10.1038/2211064a0

Cited by 7 publications

(2 citation statements)

References 7 publications

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“…Many types of malignant cells have been shown to be deficient in the enzyme asparag:i.n.e synthetase, which, in mammalian t.:ells, catalyzes the synthesis of asparagine from aspartate and glutamine (10,12,40,86,87,92). To grow, the deficient cells require as exogenous supply of asparagine (35,85,110).…”

Section: Asparaginase As An Antitumor Agentmentioning

confidence: 99%

L-Asparagine degradation in saccharomyces cerevisiae: Genetic control and biochemical properties of yeast L-asparaginase

Jones¹

1970

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Section: Asparaginase As An Antitumor Agentmentioning

confidence: 99%

L-Asparagine degradation in saccharomyces cerevisiae: Genetic control and biochemical properties of yeast L-asparaginase

Jones¹

1970

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“…Glutamine is the donor in growing cultures of HELA cells (LEVINTOW, 1953, in embryonic liver (ARFIN, 1967, and in tumour tissue ORR, 1967, 1968;PRAGER and BACHYNSKY, 1968). Ammonia is not active in Hela cells or in embryonic liver, but can serve as an amide donor in Jensen sarcoma (PATTERSON and O m , 1967), Novikoff hepatoma ( P A~R S O N and ORR, 1968), normal and malignant lymphoid tissue from the mouse and guinea pig (PRAGER and BACHYNSKY, 1968), various guinea pig tissues (HOLCENBERG, 1969) and normal or malignant human kidney and prostate tissue (PRAGER, PETERS, JANES and DERR, 1969). Product inhibition was observed in mammalian tissues, but it was not as strong as that observed in L. arabinosus and S. bouis.…”

mentioning

confidence: 99%

Formation of Asparagine From Aspartic Acid in Rat Brain

Benuck¹,

Stern²,

Lajtha³

1970

Journal of Neurochemistry

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The synthesis of asparagine in rat brain was studied both in vitro and in uivo. A conversion in viiro of about 2 per cent of the added ~-[l~C]aspartic acid into asparagine was found after a 2 h incubation with the 100,OOOg supernatant fraction from brain. This corresponded to a formation of 4.8 nmol of asparaginelmg of protein/h. The reaction required ATP and glutamine, and was linear with time during the 2 h incubation. When the crude mitochondrial fraction was added to the incubation mixture the reaction was inhibited, probably because of the presence of ATF' ase activity in the mitochondrial preparation. Inhibition by the reaction product seemed unlikely since removal of endogenous asparagine did not stimulate the reaction; only when asparagine was added at levels of 0.5 or 1.0 mM was significant inhibition found. Ammonium chloride was less effective than glutamine as an amide donor. Endogenous asparaginase (EC 3.5.1.1.) activity was low in the in vitro preparation and did not significantly affect the conversion. Synthesis of asparagine from aspartic acid did not occur in slices of brain nor was there a significant conversion of aspartic acid or glucose to asparagine after their intracerebral administration in vivo.INFORMATION about the synthesis of asparagine by nervous tissue is meagre. BERL, LAJTHA and WAELSCH (1 961) have demonstrated the presence of radioactive asparagine in brain after intracisternal injection of labelled aspartic acid. However, the conversion was low in comparison with the conversion of glutamic acid to glutamine. To our knowledge only two recent studies on the synthesis in vitro of asparagine in mammalian tissues have included data for the synthesis of asparagine by brain. HOROWITZ MADRAS, MEISTER, OLD, BOYSE and STOCKERT (1968) reported a rate of conversion of aspartic acid to asparagine of 5.2 nmol/mg of protein/h in the soluble, supernatant fraction from rat brain. HOLCENBERG (1969) found a conversion of 3-4 nmols /mg of protein/h in the soluble, supernatant fraction from the guinea pig brain.A number of systems demonstrating the synthesis of asparagine have been described. In plants, cyanide could provide the amide carbon and nitrogen for the synthesis of asparagine, with beta-cyano-L-alanine as the immediate precursor (LEES, FARNDEN and ELLIOTT, 1968 ; BLUMENTHAL-GOLDSCHMIDT, BUTLER and CONN, 1963 ; RESSLER, NAGARAJAN and LAUINGER, 1969). In the bacteria Lactobacillur arabinosus and Streptococcus bovis, asparagine was synthesized from aspartic acid and ammonium ion (RAVEL, NORTON, HUMPHREYS and SHIVE, 1962; BURCHALL, REICHELT and WOLM, 1964). The reaction was ATP-dependent and strongly productinhibited. The presence of asparagine not only inhibited the reaction, but controlled the synthesis of the enzyme (RAVEL et al., 1962). Glutamine did not serve as an amide donor. CEDAR and SCHWARTZ (1969) have described a similar system for the asparagine synthetase of E. coli. In the bacterial systems, ATP is cleaved to AMP and PPi. NAIR (1969) has described a system for the synthesis of as...

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Toxicity of E. coli L-asparaginase in man

Oettgen

Stephenson

Schwartz

et al. 1970

Cancer

245

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During therapeutic trials with E. coli L‐asparaginase in 131 children and 143 adults with neoplastic disease the following signs of toxicity have been observed: fever, nausea and vomiting, weight loss, somnolence, lethargy, confusion, hypolipidemia, hyperlipidemia, hypoproteinemia, abnormal liver function tests, fatty metamorphosis of the liver, pancreatitis (in rare instances), azotemia, granulocytopenia, lymphopenia, thrombocytopenia, and hypersensitivity reactions. While these effects have been moderately severe and reversible in most instances, some patients have shown dangerous degrees of toxicity. This has been the case most frequently in adult patients receiving a dose of 5000 IU/kg/day.

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Asparagine Synthetase Activity in Malignant and Non-malignant Human Kidney and Prostate Specimens

Cited by 7 publications

References 7 publications

L-Asparagine degradation in saccharomyces cerevisiae: Genetic control and biochemical properties of yeast L-asparaginase

L-Asparagine degradation in saccharomyces cerevisiae: Genetic control and biochemical properties of yeast L-asparaginase

Formation of Asparagine From Aspartic Acid in Rat Brain

Toxicity of E. coli L-asparaginase in man

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