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Reprod Nutr Dev. 1989;29(3):277-82. doi: 10.1051/rnd:19890305.

Steroid sulfatase activity in homogenates, microsomes and purified Leydig cells from adult rat testis.

Reproduction, nutrition, development

N Mouhadjer, M Bedin, G Pointis

Affiliations

  1. U166, groupe de recherches sur l'endocrinologie de la reproduction, INSERM, Paris, France.

PMID: 2531591 DOI: 10.1051/rnd:19890305
Free Article

Abstract

Steroid sulfatase (STS) activity was studied in the Long-Evans rat testis. The rate of dehydroepiandrosterone sulfate (DHA-S) hydrolysis determined in whole testis homogenates was low compared to that of the corresponding microsomal fractions, which was, in contrast, as high as that expressed in homogenates from purified Leydig cells. Such an increment in STS activity between total homogenates and the corresponding microsomes was not observed for the seminiferous tubules. The STS affinity reported for total testicular microsomes (Km = 3.47 +/- 0.54 microM; mean +/- SEM) was of the same magnitude as that previously reported for Leydig cells, but was about 3 times higher than that measured for whole testis homogenate (Km = 10.11 +/- 0.92 microM). In vivo hCG treatment decreased the STS affinity in total testicular microsomes without affecting this kinetic parameter in whole testis homogenate. These data suggest that the steroid sulfatase expressed in total testicular microsomes (activity and regulation by hCG) could be considered as a good index of Leydig cell STS activity.

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