Effect of magnetic fields on antioxidant system enzymes in mice with Ehrlich ascites carcinoma. 2011

E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
Krasnoyarsk State Medical University; Siberian Federal University, Krasnoyarsk, Russia. e.sergeeva77@mail.ru

The combination of weak steady-state and weak low-frequency alternating magnetic fields activates SOD in Ehrlich ascites carcinoma cells and catalase in liver cells by 3.7 and 1.3 times, respectively (p<0.05), which can result from enhanced production of ROS induced by combined exposure to magnetic fields with the specified parameters.

UI MeSH Term Description Entries
D008280 Magnetics The study of MAGNETIC PHENOMENA. Magnetic
D010088 Oxidoreductases The class of all enzymes catalyzing oxidoreduction reactions. The substrate that is oxidized is regarded as a hydrogen donor. The systematic name is based on donor:acceptor oxidoreductase. The recommended name will be dehydrogenase, wherever this is possible; as an alternative, reductase can be used. Oxidase is only used in cases where O2 is the acceptor. (Enzyme Nomenclature, 1992, p9) Dehydrogenases,Oxidases,Oxidoreductase,Reductases,Dehydrogenase,Oxidase,Reductase
D001854 Bone Marrow Cells Cells contained in the bone marrow including fat cells (see ADIPOCYTES); STROMAL CELLS; MEGAKARYOCYTES; and the immediate precursors of most blood cells. Bone Marrow Cell,Cell, Bone Marrow,Cells, Bone Marrow,Marrow Cell, Bone,Marrow Cells, Bone
D002286 Carcinoma, Ehrlich Tumor A transplantable, poorly differentiated malignant tumor which appeared originally as a spontaneous breast carcinoma in a mouse. It grows in both solid and ascitic forms. Ehrlich Ascites Tumor,Ascites Tumor, Ehrlich,Ehrlich Tumor Carcinoma,Tumor, Ehrlich Ascites
D002374 Catalase An oxidoreductase that catalyzes the conversion of HYDROGEN PEROXIDE to water and oxygen. It is present in many animal cells. A deficiency of this enzyme results in ACATALASIA. Catalase A,Catalase T,Manganese Catalase,Mn Catalase
D004789 Enzyme Activation Conversion of an inactive form of an enzyme to one possessing metabolic activity. It includes 1, activation by ions (activators); 2, activation by cofactors (coenzymes); and 3, conversion of an enzyme precursor (proenzyme or zymogen) to an active enzyme. Activation, Enzyme,Activations, Enzyme,Enzyme Activations
D005979 Glutathione Peroxidase An enzyme catalyzing the oxidation of 2 moles of GLUTATHIONE in the presence of HYDROGEN PEROXIDE to yield oxidized glutathione and water. Cytosolic Glutathione Peroxidase,Glutathione Lipoperoxidase,Selenoglutathione Peroxidase,Glutathione Peroxidase, Cytosolic,Lipoperoxidase, Glutathione,Peroxidase, Glutathione,Peroxidase, Selenoglutathione
D000818 Animals Unicellular or multicellular, heterotrophic organisms, that have sensation and the power of voluntary movement. Under the older five kingdom paradigm, Animalia was one of the kingdoms. Under the modern three domain model, Animalia represents one of the many groups in the domain EUKARYOTA. Animal,Metazoa,Animalia
D013482 Superoxide Dismutase An oxidoreductase that catalyzes the reaction between SUPEROXIDES and hydrogen to yield molecular oxygen and hydrogen peroxide. The enzyme protects the cell against dangerous levels of superoxide. Hemocuprein,Ag-Zn Superoxide Dismutase,Cobalt Superoxide Dismutase,Cu-Superoxide Dismutase,Erythrocuprein,Fe-Superoxide Dismutase,Fe-Zn Superoxide Dismutase,Iron Superoxide Dismutase,Manganese Superoxide Dismutase,Mn-SOD,Mn-Superoxide Dismutase,Ag Zn Superoxide Dismutase,Cu Superoxide Dismutase,Dismutase, Ag-Zn Superoxide,Dismutase, Cobalt Superoxide,Dismutase, Cu-Superoxide,Dismutase, Fe-Superoxide,Dismutase, Fe-Zn Superoxide,Dismutase, Iron Superoxide,Dismutase, Manganese Superoxide,Dismutase, Mn-Superoxide,Dismutase, Superoxide,Fe Superoxide Dismutase,Fe Zn Superoxide Dismutase,Mn SOD,Mn Superoxide Dismutase,Superoxide Dismutase, Ag-Zn,Superoxide Dismutase, Cobalt,Superoxide Dismutase, Fe-Zn,Superoxide Dismutase, Iron,Superoxide Dismutase, Manganese
D017382 Reactive Oxygen Species Molecules or ions formed by the incomplete one-electron reduction of oxygen. These reactive oxygen intermediates include SINGLET OXYGEN; SUPEROXIDES; PEROXIDES; HYDROXYL RADICAL; and HYPOCHLOROUS ACID. They contribute to the microbicidal activity of PHAGOCYTES, regulation of SIGNAL TRANSDUCTION and GENE EXPRESSION, and the oxidative damage to NUCLEIC ACIDS; PROTEINS; and LIPIDS. Active Oxygen Species,Oxygen Radical,Oxygen Radicals,Pro-Oxidant,Reactive Oxygen Intermediates,Active Oxygen,Oxygen Species, Reactive,Pro-Oxidants,Oxygen, Active,Pro Oxidant,Pro Oxidants,Radical, Oxygen

Related Publications

E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
January 2009, Biofizika,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
December 1984, Cancer letters,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
September 1954, Gan,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
January 1959, Voprosy onkologii,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
July 2009, Bioelectromagnetics,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
April 2000, Cancer letters,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
April 2003, Indian journal of experimental biology,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
January 1971, Experientia,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
January 1957, Zeitschrift fur Krebsforschung,
E Yu Sergeeva, and N M Titova, and A S Sherbinina, and N V Sergeev, and A V Shirokova
September 1969, British journal of cancer,
Copied contents to your clipboard!