NDLI: ATP inhibits nuclear and mitochondrial type I topoisomerases from human leukemia cells.

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ATP inhibits nuclear and mitochondrial type I topoisomerases from human leukemia cells.

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ATP inhibits nuclear and mitochondrial type I topoisomerases from human leukemia cells.

Content Provider	World Health Organization (WHO)-Global Index Medicus
Author	Castora, F. J. Kelly, W. G.
Abstract	Type I topoisomerases have been purified from nuclei and mitochondria of human acute lymphoblastic leukemia cells. Both of these ATP-independent enzymes are actually found to be inhibited by ATP at physiologically significant concentrations. Other adenine nucleotides showed varying effects: ADP inhibited only at high concentrations; AMP had no effect on either topoisomerase. Both enzymes were also inhibited by dATP. The importance of the adenine ring structure was confirmed by the lack of an inhibitory effect observed with equivalent levels of GTP, UTP, CTP, or their deoxy counterparts. Assays performed in the presence of nonhydrolyzable analogs of ATP suggest that hydrolysis of ATP does not accompany this enzyme inhibition. This was supported by direct determination of the ATPase activity of the purified enzymes. Type I topoisomerase from calf thymus and HeLa cells were also found to be sensitive to ATP. These results suggest that mammalian type I topoisomerases in general may possess a nucleotide-binding site that may be involved in regulation of enzyme activity.
ISSN	00278424
e-ISSN	10916490
Journal	Proceedings of the National Academy of Sciences of the United States of America
Issue Number	6
Volume Number	83
Language	English
Publisher	National Academy of Sciences
Publisher Date	1986-04-01
Publisher Place	United States
Access Restriction	Open
Subject Keyword	Adenosine Triphosphate Pharmacology Leukemia, Lymphoid Enzymology Topoisomerase I Inhibitors Animals Cell Nucleus DNA, Superhelical Metabolism Deoxyribonucleotides HeLa Cells Hydrolysis Mitochondria Nucleic Acid Conformation Ribonucleotides Research Support, Non-U.S. Gov't Multidisciplinary
Content Type	Text
Resource Type	Article
Subject	Multidisciplinary

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