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The Journal of biological chemistry1987; 262(12); 5717-5722;

Aromatization of 19-norandrogens by equine testicular microsomes.

Abstract: In the stallion testis, aromatase activity was localized in the microsomal fraction. Androgen aromatization occurred through the loss of 1 beta,2 beta hydrogen atoms and appeared to involve free sulfhydryl groups. A single enzyme system seemed to aromatize androgen and norandrogen at the same rate while having a much lower affinity for norandrogens.
Publication Date: 1987-04-25 PubMed ID: 3571232
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  • Journal Article

Summary

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This research investigates the process through which certain hormones known as 19-norandrogens are converted into other forms by enzyme activity (aromatization) within microsomal structures in stallion testes. It was found that the process involves the loss of hydrogen atoms and the involvement of certain sulfur-containing groups, and that a single enzyme system can convert both androgen and norandrogen hormones, though it has a lower affinity for norandrogens.

Methodology

The study uses a biochemical approach to investigate the process of androgen aromatization.

  • The primary procedure involves the use of microsomal fractions from stallion testes. Microsomes are small vesicle-like structures derived from the endoplasmic reticulum in cells, and serve as the primary site of various enzymatic reactions in the body.
  • Through the use of these structures, the researchers were able to isolate the enzymatic reactions of interest and study their properties.

Aromatization Process

This process is the conversion of androgens to estrogens, and it’s carried out by the enzyme aromatase.

  • The researchers found that the process involved the loss of 1 beta,2 beta hydrogen atoms. This suggest a specific chemical manipulation occurring on the androgen molecule as it is converted into something else.
  • They also found that this aromatization seemed to involve free sulfhydryl groups. Sulfhydryl groups are sulfur-containing chemical groups that are often involved in enzyme reactions and can take part in bonding/interaction processes with other molecules.

Role of Enzymes

One interesting finding was that a single enzyme seemed to be responsible for the aromatization of both androgen and norandrogen molecules.

  • However, this enzyme seemed to have a much lower affinity for norandrogens, meaning that it was less likely to interact with and convert these molecules when compared to regular androgens.
  • This could have interesting implications for the regulation of hormone balance within the testes, as it suggests a possible mechanism for selectively controlling the conversion of different types of androgens.

Conclusion

The research provides new insights into the chemical and enzymatic processes that regulate hormone conversion in the testes. It expands our understanding of how different forms of androgens can be converted via the same enzymatic process, yet with different rates of conversion based on the enzyme’s affinity. This could in future help in the development of specific chemicals or drugs that can modulate these processes.

Cite This Article

APA
Gaillard JL, Silberzahn P. (1987). Aromatization of 19-norandrogens by equine testicular microsomes. J Biol Chem, 262(12), 5717-5722.

Publication

ISSN: 0021-9258
NlmUniqueID: 2985121R
Country: United States
Language: English
Volume: 262
Issue: 12
Pages: 5717-5722

Researcher Affiliations

Gaillard, J L
    Silberzahn, P

      MeSH Terms

      • Aging
      • Androgens
      • Animals
      • Aromatase / isolation & purification
      • Aromatase / metabolism
      • Horses
      • Male
      • Microsomes / enzymology
      • Mitochondria / enzymology
      • Subcellular Fractions / enzymology
      • Substrate Specificity
      • Testis / enzymology
      • Testis / growth & development
      • Tritium

      Citations

      This article has been cited 1 times.
      1. Cheng Q, Sohl CD, Yoshimoto FK, Guengerich FP. Oxidation of dihydrotestosterone by human cytochromes P450 19A1 and 3A4. J Biol Chem 2012 Aug 24;287(35):29554-67.
        doi: 10.1074/jbc.M112.390047pubmed: 22773874google scholar: lookup