Sources of nitrogen as rate-limiting factors for purine biosynthesis de novo in Ehrlich ascites tumor cells

1969 ◽  
Vol 177 (1) ◽  
pp. 88-93 ◽  
Author(s):  
Lydia J. Fontenelle ◽  
J.Frank Henderson
Keyword(s):  
Tumor Cells ◽  
De Novo ◽  
Ehrlich Ascites Tumor ◽  
Purine Biosynthesis ◽  
Limiting Factors ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Ehrlich Ascites ◽  
Rate Limiting

Effects of Actinomycin D on Purine Ribonucleotide Metabolism in Ehrlich Ascites Tumor Cells In Vitro

1974 ◽  
Vol 52 (3) ◽  
pp. 263-267 ◽  
Author(s):  
Floyd F. Snyder ◽  
J. Frank Henderson
Keyword(s):  
Tumor Cells ◽  
Actinomycin D ◽  
De Novo ◽  
Acid Synthesis ◽  
Purine Metabolism ◽  
Ehrlich Ascites Tumor ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Ehrlich Ascites

Actinomycin D treatment of Ehrlich ascites tumor cells in vitro causes slight to moderate inhibition of purine ribonucleotide synthesis de novo and from purine bases, and strong inhibition of inosinate dehydrogenase activity. These effects have the same dose–response relationship as inhibition of RNA synthesis by this drug. Daunomycin has similar effects on purine metabolism at a concentration that substantially inhibits nucleic acid synthesis. Actinomycin D treatment leads to elevated intracellular concentrations of ATP and GTP, and the effects of this drug on purine metabolism are believed to be mediated by these purine ribonucleoside triphosphates.

Inhibition of glycolysis in Ehrlich ascites tumor cells incubated with formimino-L-glutamate

1969 ◽  
Vol 47 (4) ◽  
pp. 419-422 ◽  
Author(s):  
Lydia J. Fontenelle ◽  
J. Frank Henderson
Keyword(s):  
Tumor Cells ◽  
De Novo ◽  
Ehrlich Ascites Tumor ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Phosphoribosyl Pyrophosphate ◽  
Triose Phosphate ◽  
Glucose Inhibition ◽  
Ehrlich Ascites ◽  
Inhibition Of Glycolysis

Incubation of tumor cells with formiminoglutamate leads to inhibition of lactate synthesis from glucose, inhibition of phosphoribosyl pyrophosphate synthesis, and inhibition of purine ribonucleotide synthesis de novo and from purine bases. Lactate synthesis from inosine was increased. These effects may result from inhibition of triose phosphate isomerase by a metabolite of formiminoglutamate.

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