Article
A naturally occurring basically charged human follicle-stimulating hormone (FSH) variant inhibits FSH-induced androgen aromatization and tissue-type plasminogen activator enzyme activity in vitro.
Neuroendocrinology - 1 Mar 1998
Timossi C M, Barrios de Tomasi J, Zambrano E, González R, Ulloa-Aguirre A
Abstract excerpt
It is well known that deglycosylation of gonadotropins by enzymatic or chemical procedures or by deletion of sites for N-linked glycosylation produces antagonistic analogs which are able to interact strongly with the receptor and to inhibit binding of the wild-type hormone. In the present study,...
Topics
- Androgens
- Animals
- Aromatase
- Aromatase Inhibitors
- Bucladesine
- Cells, Cultured
- Cyclic AMP
- Electrochemistry
- Enzyme Inhibitors
- Estrogens
- Female
- Follicle Stimulating Hormone
- Genetic Variation
- Granulosa Cells
- Humans
- Protein Kinase C
- Rats
- Rats, Wistar