Human and quail aromatase activity is rapidly and reversibly inhibited by phosphorylating conditions.

ABSTRACT: Besides their slow genomic actions, estrogens also induce rapid physiological responses. To be functionally relevant, these effects must be associated with rapid changes in local concentrations of estrogens. Rapid changes in aromatase activity (AA) controlled by calcium-dependent phosphorylations of the enzyme can alter in a rapid manner local estrogen concentrations, but so far this mechanism was identified only in the avian (quail) brain. We show here that AA is also rapidly down-regulated by phosphorylating conditions in quail ovary homogenates and in various cell lines transfected with human aromatase (HEK 293, Neuro2A, and C6). Enzymatic activity was also rapidly inhibited after depolarization of aromatase-expressing HEK 293 cells with 100 mM KCl, and activity was fully restored when

SUBMITTER: Charlier TD 

PROVIDER: S-EPMC3199011 | biostudies-literature | 2011 Nov

REPOSITORIES: biostudies-literature