scholarly journals Synthesis and Comparative Evaluation of Polymethoxy Substituted 1,4-Naphthoquinones and their Acetyl-O-glucosides as Cytotoxic Agents

2017 ◽  
Vol 12 (7) ◽  
pp. 1934578X1701200 ◽  
Author(s):  
Yuri E. Sabutski ◽  
Marina N. Semenova ◽  
Ekaterina A. Yurchenko ◽  
Nikita S. Polonik ◽  
Vladimir A. Denisenko ◽  
...  
Keyword(s):  
Comparative Evaluation ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Cytotoxic Agents ◽  
Cytotoxic Effects ◽  
Micromolar Concentration ◽  
Sea Urchin Embryo ◽  
Ehrlich Ascites ◽  
Methoxy Groups ◽  
Derivatives Of

Twenty five hydroxy-, chloro- and methoxy derivatives of natural and synthetic naphthazarins and their acetylated O-glycosides were synthesized. Targeted compounds were screened as cytotoxic agents on mouse Ehrlich ascites carcinoma cells using MTT test. Chloro- and methoxy-substituted naphthoquinones as well as naphthoquinone O-acetylglucosides were the most potent with IC50 in low micromolar concentration range. Glucosidation of hydroxynaphthoquinones was shown to enhance cytotoxicity, whereas methoxylation yielded both more active and less active derivatives depending on the number and position of methoxy groups. Evaluation using a phenotypic sea urchin embryo assay suggested that naphthazarins exerted their cytotoxic effects through tubulin-unrelated mechanism.

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.

METABOLISM OF 6-MERCAPTOPURINE RIBONUCLEOSIDE BY EHRLICH ASCITES CARCINOMA CELLS

1964 ◽  
Vol 42 (10) ◽  
pp. 1415-1423 ◽  
Author(s):  
A. R. P. Paterson ◽  
Aiko Sutherland
Keyword(s):  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Glycosidic Linkage ◽  
Ascites Tumor ◽  
Resistant Line ◽  
Cell Compartment ◽  
Ehrlich Ascites ◽  
A Cell ◽  
Derivatives Of

Ribonucleoside derivatives of 6-mercaptopurine (6-MP) and other purine bases were rapidly catabolized when incubated with Ehrlich ascites carcinoma cells in vitro. The catabolism of purine ribonucleosides proceeded by way of phosphorolytic cleavage of the glycosidic linkage and resulted in accumulation of the liberated base in the incubation medium. The ribosyl portions of ribonucleoside substrates were utilized with the formation of lactate, which also appeared extracellularly.Cells of a 6-MP-resistant subline of the Ehrlich ascites tumor degraded 6-MP ribonucleoside (6-MPR) at rates comparable to those of the parent line. This finding, when considered with other characteristics of the resistant line of cells, implied that cleavage of 6-MPR took place in a cell compartment from which inosinate pyrophosphorylase was absent.

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

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.

COMPETITION BETWEEN AMINO ACIDS FOR TRANSPORT INTO EHRLICH ASCITES CARCINOMA CELLS

1961 ◽  
Vol 39 (11) ◽  
pp. 1717-1735 ◽  
Author(s):  
P. G. Scholefield
Keyword(s):  
Carbon Dioxide ◽  
Amino Acids ◽  
Amino Acid ◽  
Ehrlich Ascites Carcinoma ◽  
Carcinoma Cells ◽  
Transport Systems ◽  
Radioactive Carbon ◽  
Ehrlich Ascites ◽  
Competitive Inhibitors ◽  
Amino Acid Analogues

The cumulative entry of amino acids into Ehrlich ascites carcinoma cells is due to the presence of active transport systems, each with its own specific range of substrates. Several amino acids and amino acid analogues may have an affinity for the same transport system and thus may inhibit transport of other amino acids by acting as competitive inhibitors or competitive substrates. Loss of methionine from ascites cells takes place by a diffusion process which obeys Fick's law. Leucine accumulation by ascites cells is small and is increased on addition of certain other amino acids. The increase is not due to inhibition of leucine oxidation as increase in the rate of production of radioactive carbon dioxide from labeled leucine also occurs. Kinetic aspects of these results are discussed.

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