Biomedical subjects
Publications and source records attributed to C M Goos.
A method has been developed for the first time that allows the evaluation of the effect of therapeutic concentrations of 5 alpha-reductase inhibitors in human skin, without applying radioactivity to the skin. Moreover, the method makes it possible to determine whether inhibition is found only at the application site or also in other parts of the skin.
Human scalp hair follicles contain an enzyme system that metabolizes the carcinogen benzo[a]pyrene. The major ethyl acetate soluble metabolites are 7,8-dihydro-7,8-dihydroxybenzo[a]pyrene,9,10-dihydro-9,10-dihydroxybenzo[a]pyrene and 3-hydroxybenzo[a]pyrene. Addition of 1,1,1-trichloropropene-2,3-oxide (TCPO), an inhibitor of epoxide hydratase, prevents the formation of the dihydrodiols. The overall metabolism can be inhibited by the addition of alpha-naphthoflavone. The metabolism of benzo[a]pyrene in a cell culture of human scalp hair follicles has also been investigated. The results show that the activity of arylhydrocarbon hydroxylase (AHH) and epoxide hydratase (EH) is maintained in culture.
The dehydroepiandrosterone hydroxylating enzyme system in the hair follicle has been characterized. It is found in the particulate fraction of the follicle, and is inhibited by carbon monoxide and the cytochrome P450 inhibitor metyrapone, and appears to be dependent upon NADPH. In these major characteristics the hair follicle enzyme is very similar to the liver monooxygenase system.
Dydrogesterone, an orally effective progestational compound, frequently used in a large spectrum of endocrine and gynecologic problems was evaluated for possible peripheric androgenic or anti-androgenic activity. The drug was tested in vivo in the hamster flank organ test and in vitro in tests based on molecular mechanisms of androgen action. Dydrogesterone appeared to have neither androgenic nor anti-androgenic properties. This is important in view of the fact that dydrogesterone can also be indicated during pregnancy.