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Biochemical actions of follice-stimulating hormone in the sertoli cell of the rat testis.

Publication ,  Journal Article
Fakunding, JL; Tindall, DJ; Dedman, JR; Mena, CR; Means, AR
Published in: Endocrinology
February 1976

The sequenc of biochemical events associated with the action of follicle-stimulating hormone (FSH) in the testis has been investigated using a Sertoli cell-enriched testis model system. The Sertoli cell-encriched testis, created by irradiation of male rats in utero, is devoid of germinal elements but contains a normal complement of supportive Sertoli cells. Comparison of the Sertoli cell-enriched testis with normal testis, demonstrates that the two types of testes contain equal numbers of FSH specific receptors, judged by the binding of labeled hormone. In addition, FSH over a concentration range from 6 X 10(-11) to 6 X 10(-9)M will stimulate the production of adenosine 3',5' monophosphate (cAMP) in the Sertoli cell-enriched testis in a manner indistinguishable from that of the normal testis. Incubation of Sertoli cell enriched testis also results in the activation of soluble cAMP-dependent protein kinase. This response to FSH is dependent upon the age of the animal and disappears at about 32 days of age. While sensitivity to the hormone can still be detected in mature Sertoli cell-enriched animals by the addition of the phosphodiesterase inhibitor 1-methyl-3-isobutyl-xanthine, no detectable increase in phosphodiesterase activity is apparent after 30 days of age. Injection of FSH into Sertoli cell-enriched animals results in an increase in total testicular protein synthesis as well as in the production of the Sertoli cell-specific protein, androgen-binding protein within 30 minutes. Furthermore, while hypophysectomy of Sertoli cell-enriched animals result in a decline of the testicular concentration of androgen-binding protein, the injection of FSH will stimulate and maintain the levels of androgen-binding protein in such animals. These results demonstrate that the Sertoli cell-enriched testis is capable of carrying out the sequence of biochemical events previously described for FSH in the normal testis and therefore, suggest that the Sertoli cell is the primary target cell for FSH action.

Duke Scholars

Published In

Endocrinology

DOI

ISSN

0013-7227

Publication Date

February 1976

Volume

98

Issue

2

Start / End Page

392 / 402

Location

United States

Related Subject Headings

  • Xanthines
  • Sertoli Cells
  • Seminiferous Tubules
  • Receptors, Cell Surface
  • Rats
  • Radiation Effects
  • Protein Kinases
  • Protein Biosynthesis
  • Phosphoric Diester Hydrolases
  • Male
 

Citation

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Fakunding, J. L., Tindall, D. J., Dedman, J. R., Mena, C. R., & Means, A. R. (1976). Biochemical actions of follice-stimulating hormone in the sertoli cell of the rat testis. Endocrinology, 98(2), 392–402. https://doi.org/10.1210/endo-98-2-392
Fakunding, J. L., D. J. Tindall, J. R. Dedman, C. R. Mena, and A. R. Means. “Biochemical actions of follice-stimulating hormone in the sertoli cell of the rat testis.Endocrinology 98, no. 2 (February 1976): 392–402. https://doi.org/10.1210/endo-98-2-392.
Fakunding JL, Tindall DJ, Dedman JR, Mena CR, Means AR. Biochemical actions of follice-stimulating hormone in the sertoli cell of the rat testis. Endocrinology. 1976 Feb;98(2):392–402.
Fakunding, J. L., et al. “Biochemical actions of follice-stimulating hormone in the sertoli cell of the rat testis.Endocrinology, vol. 98, no. 2, Feb. 1976, pp. 392–402. Pubmed, doi:10.1210/endo-98-2-392.
Fakunding JL, Tindall DJ, Dedman JR, Mena CR, Means AR. Biochemical actions of follice-stimulating hormone in the sertoli cell of the rat testis. Endocrinology. 1976 Feb;98(2):392–402.
Journal cover image

Published In

Endocrinology

DOI

ISSN

0013-7227

Publication Date

February 1976

Volume

98

Issue

2

Start / End Page

392 / 402

Location

United States

Related Subject Headings

  • Xanthines
  • Sertoli Cells
  • Seminiferous Tubules
  • Receptors, Cell Surface
  • Rats
  • Radiation Effects
  • Protein Kinases
  • Protein Biosynthesis
  • Phosphoric Diester Hydrolases
  • Male