Inhibition of coenzyme Q10-enzymes, succinoxidase and NADH-oxidase, by adriamycin and other quinones having antitumor activity
| Autor: | Thomas H. Porter, Inge L. Hansen, Karl Folkers, Yoshifumi Iwamoto |
|---|---|
| Rok vydání: | 1974 |
| Předmět: |
Naphthacenes
Macromolecular Substances Ubiquinone Cellular respiration Daunorubicin Biophysics Pharmacology Biochemistry Electron Transport Structure-Activity Relationship chemistry.chemical_compound polycyclic compounds medicine NADH NADPH Oxidoreductases Doxorubicin Colloids Molecular Biology Phospholipids Lapachol chemistry.chemical_classification Coenzyme Q10 Alanine Antibiotics Antineoplastic biology Myocardium Succinate dehydrogenase Quinones Cell Biology Mitochondria Muscle Succinate Dehydrogenase carbohydrates (lipids) Kinetics Aminoglycosides Enzyme chemistry Coenzyme Q – cytochrome c reductase biology.protein medicine.drug |
| Zdroj: | Biochemical and Biophysical Research Communications. 58:633-638 |
| ISSN: | 0006-291X |
| DOI: | 10.1016/s0006-291x(74)80465-1 |
| Popis: | Summary Adriamycin, carminomycin, and daunorubicin inhibit the coenzyme Q 10 -enzymes, succinoxidase and NADH-oxidase. Adriamycin 14-octanoate, which is more lipoidal than adriamycin, was the most effective inhibitor of the anthracyclines for both enzymes, and was 1/12 as effective as the standard inhibitor, 6-ω-cyclohexylpentyl-5-hydroxy-2,3-dimethoxy-1,4-benzoquinone, of coenzyme Q 10 for NADH-oxidase. Lapachol and dichloroallyl lawsone inhibited succinoxidase, and the latter of all quinones was second only to the standard for inhibition. These data indicate that the antitumor activities of adriamycin could possibly be partly due to inhibition of CoQ 10 -enzymes in electron transfer processes of cell respiration in addition to intercalation within DNA helices. |
| Databáze: | OpenAIRE |
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