Activation of 2-Aminofluorene by Prostaglandin Endoperoxide H Synthase 2
| Autor: | Wendell W. Weber, Gerald N. Levy, Ying Liu |
|---|---|
| Rok vydání: | 1995 |
| Předmět: |
Male
inorganic chemicals Umbilical Veins DNA Complementary Placenta Indomethacin Biophysics Gene Expression Transfection Biochemistry Adduct DNA Adducts chemistry.chemical_compound fluids and secretions Complementary DNA Animals Humans Inducer Molecular Biology Carcinogen chemistry.chemical_classification Fluorenes Sheep Aspirin ATP synthase biology Seminal Vesicles Cell Biology equipment and supplies Molecular biology Isoenzymes Enzyme chemistry Prostaglandin-Endoperoxide Synthases Carcinogens biology.protein Tetradecanoylphorbol Acetate bacteria Female Arachidonic acid Endothelium Vascular DNA |
| Zdroj: | Biochemical and Biophysical Research Communications. 215:346-354 |
| ISSN: | 0006-291X |
| DOI: | 10.1006/bbrc.1995.2472 |
| Popis: | Prostaglandin endoperoxide H synthase is the key enzyme in the conversion of arachidonic acid to tissue prostanoids. Two isoforms of prostaglandin endoperoxide H synthase have been identified: PHS-1 is constitutively expressed in most tissues under normal physiological conditions and PHS-2 is expressed in response to inflammatory agents, tumor promoters, and other agents related to mitogenesis. Previous work demonstrated that PHS-1 can activate arylamine carcinogens. We report here that PHS-2 can also activate an arylamine carcinogen to form DNA adducts. This is shown by: (1) use of purified ovine PHS-2 to form DNA adducts; (2) increased DNA adduct formation, PHS-2 mRNA, and PHS-2 protein after treatment of HUVEC cells with the PHS-2 inducer PMA; and (3) transient expression of PHS-2 cDNA in COS-1 cells gave rise to both elevations of PHS-2 enzyme protein and DNA adduct formation. Finally, two PHS inhibitors, aspirin and indomethacin, showed significant inhibition of PHS-2-mediated DNA adduct formation. |
| Databáze: | OpenAIRE |
| Externí odkaz: |
|
Full Text from ScienceDirect