Placental estrogen synthetase (aromatase): evidence for phosphatase-dependent inactivation.
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Bellino FL, Holben L
Placental estrogen synthetase (aromatase): evidence for phosphatase-dependent inactivation.
Biochem Biophys Res Commun. 1989 Jul 14;162(1):498-504.
- PubMed ID
- 2546553 [ View in PubMed]
- Abstract
The acute regulation of estrogen synthetase (aromatase), the cytochrome P450 enzyme system responsible for estrogen production, is not well explored. We report here that aromatase, but not NADPH-cytochrome c (P450) reductase, activity from human term placental microsomes decreased when incubated in phosphate-free buffer at 37 degrees C. Aromatase activity was stabilized by phosphate buffer or by the phosphatase inhibitors tartaric acid or EDTA, but not NaF, in phosphate-free buffer. Alkaline phosphatase also inhibited aromatase in phosphate-free buffer relative to phosphate buffer, but the inactivation appears to be due primarily to proteolytic solubilization of NADPH-cytochrome c reductase from the microsomes by proteases within the alkaline phosphatase preparation. Based on these data, we suggest that the cytochrome P450 component of aromatase may be regulated acutely by phosphorylation-dependent processes.
DrugBank Data that Cites this Article
- Drug Enzymes
Drug Enzyme Kind Organism Pharmacological Action Actions Edetate calcium disodium anhydrous Cytochrome P450 19A1 Protein Humans UnknownModulatorDetails Edetate disodium anhydrous Cytochrome P450 19A1 Protein Humans UnknownModulatorDetails Edetic acid Cytochrome P450 19A1 Protein Humans UnknownSubstrateDetails