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Interconversion of estrone and estradiol-17 beta in lung slices of the adult human.

The metabolism of tritium-labeled estrone and estradiol-17 beta in slices of lung tissue obtained from an adult human was studied; estrone was identified as the only metabolite of estradiol-17 beta and estradiol-17 beta as the exclusive product of estrone metabolism. Product formation remained linear as a function of time of incubation up to 3 h and of wet lung tissue mass up to 300 mg/ml. At equimolar substrate concentrations, the rates of estrone formation were at least 2-fold greater than those of estradiol-17 beta. The apparent KM of 17 beta-hydroxysteroid oxidoreductase for estrone was 11 microM and that for estradiol-17 beta was 10 microM. These results are suggestive that the human lung enzyme binds estrone and estradiol-17 beta with similar affinities; however, the oxidative pathway is favored as indicated by the greater Vmax attained in the formation of estrone. It is possible that, in vivo, the human lung constitutes a site for estradiol-17 beta inactivation to estrone as well as a site for the conversion of estrone to estradiol-17 beta. This last process may become particularly important in instances in which the ovaries have ceased to function and secrete estradiol-17 beta, e.g. the postmenopausal women.