Phosphorylation of Adenosine and Deoxyadenosine in Ehrlich Ascites Carcinoma Cells Resistant to 6-(Methylmercapto)purine Ribonucleoside

1972 ◽  
Vol 50 (4) ◽  
pp. 423-427 ◽  
Author(s):  
Christopher A. Lomax ◽  
J. Frank Henderson
Keyword(s):  
Mutant Cell ◽  
Ehrlich Ascites Carcinoma ◽  
Adenosine Kinase ◽  
Carcinoma Cells ◽  
Ehrlich Ascites Tumor Cells ◽  
Nucleotide Synthesis ◽  
Ehrlich Ascites ◽  
Mutant Strains ◽  
Selection For ◽  
Reduced Activity

The metabolism of adenosine and deoxyadenosine has been studied in Ehrlich ascites tumor cells and in a subline (EAC-R2) resistant to growth inhibition by 6-(methylmercapto)purine ribonucleoside (6MeMPR). The mutant cell line showed reduced rates of conversion of adenosine and deoxyadenosine into nucleotides. It was concluded from this that both compounds probably are phosphorylated by adenosine kinase. Comparison of the rates of nucleotide synthesis at increasing concentrations of adenosine indicated differences in the Km and Vmax values of the adenosine kinases in the parent and mutant strains. Competition experiments between adenosine and 6MeMPR showed that adenosine kinase in EAC-R2 had probably lost all affinity for the analogue. Selection for resistance to 6MeMPR therefore seems to have altered the structure of adenosine kinase, such that it has no activity with 6MeMPR and reduced activity with adenosine and deoxyadenosine.

ARGININE UPTAKE AND ARGINASE ACTIVITY IN EHRLICH ASCITES CARCINOMA CELLS

1959 ◽  
Vol 37 (4) ◽  
pp. 589-598 ◽  
Author(s):  
R. M. Johnstone
Keyword(s):  
Amino Acids ◽  
Tumor Cells ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Arginase Activity ◽  
Anaerobic Glycolysis ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Arginine Uptake ◽  
Ehrlich Ascites

Anaerobic glycolysis in Ehrlich ascites tumor cells exposed to amino acids leads to an increased uptake of a number of the amino acids to levels comparable with those obtained under aerobic conditions. The arginine uptake in the cell is not increased by glucose. Anaerobically the arginase activity is inhibited when glucose is present. The inhibition appears to be the result of an increased retention in the cell of the ornithine produced by arginase activity.

ARGININE UPTAKE AND ARGINASE ACTIVITY IN EHRLICH ASCITES CARCINOMA CELLS

1959 ◽  
Vol 37 (1) ◽  
pp. 589-598 ◽  
Author(s):  
R. M. Johnstone
Keyword(s):  
Amino Acids ◽  
Tumor Cells ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Arginase Activity ◽  
Anaerobic Glycolysis ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Arginine Uptake ◽  
Ehrlich Ascites

Anaerobic glycolysis in Ehrlich ascites tumor cells exposed to amino acids leads to an increased uptake of a number of the amino acids to levels comparable with those obtained under aerobic conditions. The arginine uptake in the cell is not increased by glucose. Anaerobically the arginase activity is inhibited when glucose is present. The inhibition appears to be the result of an increased retention in the cell of the ornithine produced by arginase activity.

INHIBITION OF RIBONUCLEOSIDE METABOLISM IN EHRLICH ASCITES TUMOR CELLS BY PURINE ANALOGUE RIBONUCLEOSIDES

1965 ◽  
Vol 43 (10) ◽  
pp. 1701-1710 ◽  
Author(s):  
A. R. P. Paterson ◽  
A. I. Simpson
Keyword(s):  
Tumor Cells ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Ehrlich Ascites Tumor Cells ◽  
Purine Analogues ◽  
Intact Cells ◽  
Ehrlich Ascites ◽  
Derivatives Of ◽  
Related Compounds

Several aspects of the metabolism of inosine and uridine by Ehrlich ascites carcinoma cells in vitro have been found to be inhibited by ribonucleoside derivatives of four purine analogues. The synthesis of both inosine and uridine by intact tumor cells was profoundly inhibited in the presence of 6-methylmercaptopurine ribonucleoside. Also inhibited were inosine and uridine cleavage, and the exchange of isotope between these ribonucleosides and the corresponding C14 labelled bases. These reactions, however, were not inhibited when they took place in broken-cell preparations. Similarly, inosine metabolism in intact cells (but not in broken cells) was profoundly inhibited by three related compounds: the ribonucleosides of the 6-chloro, 6-methylmercapto, and 6-propylmercapto derivatives of 2-aminopurine.

Trichosanthes dioica seed lectin inhibits Ehrlich ascites carcinoma cells growth in vivo in mice by inducing G 0 /G 1 cell cycle arrest

2021 ◽  
Author(s):  
Shaikh Shohidul Islam ◽  
Md. Rezaul Karim ◽  
A. K. M. Asaduzzaman ◽  
A. H. M. Khurshid Alam ◽  
Zahid Hayat Mahmud ◽  
...  
Keyword(s):  
Cell Cycle ◽  
Cell Cycle Arrest ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Cycle Arrest ◽  
Ehrlich Ascites ◽  
Trichosanthes Dioica

scholarly journals Kinetic Studies of Adenosine Kinase from Ehrlich Ascites Tumor Cells

1972 ◽  
Vol 247 (7) ◽  
pp. 1972-1975 ◽  
Author(s):  
J. Frank Henderson ◽  
Aiko Mikoshiba ◽  
Samuel Y. Chu ◽  
Ian C. Caldwell
Keyword(s):  
Tumor Cells ◽  
Kinetic Studies ◽  
Adenosine Kinase ◽  
Ehrlich Ascites Tumor ◽  
Ehrlich Ascites Tumor Cells ◽  
Ascites Tumor ◽  
Ehrlich Ascites

STUDIES ON THE BIOSYNTHESIS OF NUCLEOTIDES IN EHRLICH ASCITES CARCINOMA CELLS IN VITRO

1965 ◽  
Vol 43 (2) ◽  
pp. 209-224 ◽  
Author(s):  
B. I. Uppin ◽  
P. G. Scholefield
Keyword(s):  
Exchange Reaction ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
The Other ◽  
Metabolic Inhibitors ◽  
Ehrlich Ascites ◽  
Oxidative Pathway ◽  
Time Courses ◽  
Oxidation Of Glucose

Studies have been made of the effects of metabolic inhibitors on the oxidation and incorporation of radioactivity into nucleotides of glucose labelled in the 1, 2, and 6 positions. The results indicate that in Ehrlich ascites carcinoma cells the predominant oxidative pathway is the hexosemonophosphate shunt. Investigation of the time courses of oxidation of the labelled glucose molecules confirms this conclusion. The pattern of incorporation of radioactivity initially suggests that nucleotide ribose is not formed via this pathway. However, it is shown that the coupling of an active transketolase system with the other enzymes of the hexosemonophosphate shunt provides a sufficient explanation of all the experimental observations. The conclusion is reached that pentose is formed by oxidation of glucose through the shunt but that the labelling pattern is largely established as the result of the exchange reaction catalyzed by transketolase.

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