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Androgen binding in human testis
The Journal of Urology
|July 1, 1977
Summary
Human testes cytosol contains molecules that bind dihydrotestosterone (DHT), similar to serum binding proteins. This binding is intrinsic to the testes and not solely due to blood contamination.
Area of Science:
- Endocrinology
- Molecular Biology
- Andrology
Background:
- Testosterone and its metabolites are crucial for male reproductive functions.
- The transport and availability of androgens are regulated by specific binding proteins.
- Understanding androgen-binding mechanisms in testicular tissue is vital.
Purpose of the Study:
- To investigate the presence and characteristics of dihydrotestosterone-binding macromolecules in human testicular cytosol.
- To determine if these binding macromolecules are similar to known serum binding proteins.
Main Methods:
- Preparation of human testis cytosol.
- Binding assays using tritiated dihydrotestosterone.
- Steroid competition studies.
- Analysis of heat sensitivity and dissociation rate constants.
Main Results:
- Human testis cytosol contains macromolecules that bind tritiated dihydrotestosterone.
- Binding characteristics (steroid competition, heat sensitivity, dissociation rates) resemble serum testosterone-estradiol-binding globulin (SHBG).
- The quantity of DHT binding in testicular cytosol exceeds levels attributable to serum contamination.
Conclusions:
- Human testicular cytosol possesses intrinsic dihydrotestosterone-binding macromolecules.
- These testicular binding macromolecules share properties with serum SHBG.
- The presence of these binding proteins suggests a role in local androgen regulation within the testis.