Activities of antioxidant enzymes and lipid peroxidation in endometrial cancer. 1993

R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
Department of Obstetrics and Gynecology, University Hospital, Tampere, Finland.

Antioxidant enzyme activities and lipid peroxidation were analysed in normal endometrium and endometrial cancer tissues from Finnish and Japanese patients. The catalase and glutathione peroxidase activities of normal endometrium were significantly lower in Finns than in Japanese. Lipid peroxidation was slightly higher in endometrial cancer as compared with normal endometrium both in the Finns and in the Japanese. When cancer tissues were compared with normal endometrium both in Finns and Japanese the activity of superoxide dismutase was significantly lower in cancer tissue than in normal endometrium. In Finns glutathione S-transferase activity was also lower in endometrial cancer tissue than in normal endometrium, and a similar tendency was also found in Japanese. This study suggests that endometrial cancer tissue is associated with an impaired enzymic antioxidant defence system.

UI MeSH Term Description Entries
D008875 Middle Aged An adult aged 45 - 64 years. Middle Age
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
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
D005260 Female Females
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
D005982 Glutathione Transferase A transferase that catalyzes the addition of aliphatic, aromatic, or heterocyclic FREE RADICALS as well as EPOXIDES and arene oxides to GLUTATHIONE. Addition takes place at the SULFUR. It also catalyzes the reduction of polyol nitrate by glutathione to polyol and nitrite. Glutathione S-Alkyltransferase,Glutathione S-Aryltransferase,Glutathione S-Epoxidetransferase,Ligandins,S-Hydroxyalkyl Glutathione Lyase,Glutathione Organic Nitrate Ester Reductase,Glutathione S-Transferase,Glutathione S-Transferase 3,Glutathione S-Transferase A,Glutathione S-Transferase B,Glutathione S-Transferase C,Glutathione S-Transferase III,Glutathione S-Transferase P,Glutathione Transferase E,Glutathione Transferase mu,Glutathione Transferases,Heme Transfer Protein,Ligandin,Yb-Glutathione-S-Transferase,Glutathione Lyase, S-Hydroxyalkyl,Glutathione S Alkyltransferase,Glutathione S Aryltransferase,Glutathione S Epoxidetransferase,Glutathione S Transferase,Glutathione S Transferase 3,Glutathione S Transferase A,Glutathione S Transferase B,Glutathione S Transferase C,Glutathione S Transferase III,Glutathione S Transferase P,Lyase, S-Hydroxyalkyl Glutathione,P, Glutathione S-Transferase,Protein, Heme Transfer,S Hydroxyalkyl Glutathione Lyase,S-Alkyltransferase, Glutathione,S-Aryltransferase, Glutathione,S-Epoxidetransferase, Glutathione,S-Transferase 3, Glutathione,S-Transferase A, Glutathione,S-Transferase B, Glutathione,S-Transferase C, Glutathione,S-Transferase III, Glutathione,S-Transferase P, Glutathione,S-Transferase, Glutathione,Transfer Protein, Heme,Transferase E, Glutathione,Transferase mu, Glutathione,Transferase, Glutathione,Transferases, Glutathione
D006801 Humans Members of the species Homo sapiens. Homo sapiens,Man (Taxonomy),Human,Man, Modern,Modern Man
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
D015227 Lipid Peroxidation Peroxidase catalyzed oxidation of lipids using hydrogen peroxide as an electron acceptor. Lipid Peroxidations,Peroxidation, Lipid,Peroxidations, Lipid
D016889 Endometrial Neoplasms Tumors or cancer of ENDOMETRIUM, the mucous lining of the UTERUS. These neoplasms can be benign or malignant. Their classification and grading are based on the various cell types and the percent of undifferentiated cells. Cancer of Endometrium,Endometrial Cancer,Endometrial Carcinoma,Cancer of the Endometrium,Carcinoma of Endometrium,Endometrium Cancer,Neoplasms, Endometrial,Cancer, Endometrial,Cancer, Endometrium,Cancers, Endometrial,Cancers, Endometrium,Carcinoma, Endometrial,Carcinomas, Endometrial,Endometrial Cancers,Endometrial Carcinomas,Endometrial Neoplasm,Endometrium Cancers,Endometrium Carcinoma,Endometrium Carcinomas,Neoplasm, Endometrial

Related Publications

R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
January 1993, Acta biochimica Polonica,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
January 2004, Free radical research,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
June 2006, Biological trace element research,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
October 2003, Indian journal of physiology and pharmacology,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
January 1996, Renal failure,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
January 2002, Journal of postgraduate medicine,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
January 1996, Free radical biology & medicine,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
March 2007, International journal of gynaecology and obstetrics: the official organ of the International Federation of Gynaecology and Obstetrics,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
October 1998, Biochemistry and molecular biology international,
R Punnonen, and R Kudo, and K Punnonen, and E Hietanen, and T Kuoppala, and H Kainulainen, and K Sato, and M Ahotupa
October 1998, Clinical chemistry and laboratory medicine,
Copied contents to your clipboard!