Inhibition of type II topoisomerase by fostriecin.
作者： Theodore J. Boritzki , Tammy S. Wolfard , Judith A. Besserer , Robert C. Jackson , David W. Fry
DOI: 10.1016/0006-2952(88)90096-2
关键词: Fostriecin 、 Type II topoisomerase 、 Mechanism of action 、 Topoisomerase 、 L1210 cells 、 Biology 、 Amsacrine 、 Biochemistry 、 Non-competitive inhibition 、 Ehrlich ascites carcinoma
摘要: Abstract Fostriecin is a new antitumor antibiotic which being developed further as an anticancer agent based on its marked activity in murine leukemias. Its mechanism of action, however, has thus far remained unknown. The present study demonstrates that fostriecin inhibits the catalytic partially purified type II topoisomerase from Ehrlich ascites carcinoma. Under experimental conditions employed, completely inhibited enzyme at 100 μM. A general kinetic analysis showed uncompetitive manner with K i ,app 110 μM and produced kinetics were distinctly different those VM-26 exhibited noncompetitive inhibition. did not cause DNA strand breaks L1210 cells, suggesting it stabilize cleavable complex do other known inhibitors this enzyme. Fostriecin, inhibit by amsacrine. An flow cytometry cells exposed to 5 for 12 hr caused block G 2 phase cell cycle. These studies suggest produces effects may be through inhibition markedly existing agents
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