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Expression and activity of steroid sulphatase in the boar testis


Mutembei, H M; Kowalewski, M P; Ugele, B; Schuler, G; Hoffmann, B (2009). Expression and activity of steroid sulphatase in the boar testis. Reproduction in Domestic Animals=Zuchthygiene, 44(1):17-23.

Abstract

Oestrogens are essential for male fertility targeting the testicular-epididymal compartment. However, the underlying mechanisms are only vaguely known and species specificities must be considered. The boar has a remarkably high testicular-oestrogen output, with the biologically inactive oestrone-sulphate being the major oestrogen occurring in the testicular vein. In the boar testis and epididymis, activity of steroid sulphatase (StS) and oestrogen sulphotransferase has been demonstrated. Thus apart from their synthesis in Leydig cells, provision of biologically active free oestrone seems also to depend on the activity and localization of these enzymes. Our aim was to establish expression patterns and activity of StS in boar testis. Testes were randomly collected from healthy boars and allotted to five age groups, five animals in each, aged 50, 100, 150, 200 and 250 days. Three extra boars aged over 250 days were castrated to obtain fresh tissue for enzyme activity tests. Immunohistochemistry detected StS only in the cytoplasm of Leydig cells and - except for day-50 group in which 65.1 +/- 4.9% (X +/- SD) of the cells were positive - expression was constant with virtually all the cells staining positive. RT-PCR and in situ hybridization confirmed expression and localization of StS mRNA. The V(max) and K(m) value (X +/- SD) for StS was 24.05 +/- 0.3 fmol/s/microg protein and 2.15 +/- 0.12 microM. These data suggest that StS within the Leydig cells of the boar is involved in modulation of testicular oestrogen bioavailability and that the site of sulpho-conjugation is not the testis but a different compartment of the testes-epididymidis complex.

Oestrogens are essential for male fertility targeting the testicular-epididymal compartment. However, the underlying mechanisms are only vaguely known and species specificities must be considered. The boar has a remarkably high testicular-oestrogen output, with the biologically inactive oestrone-sulphate being the major oestrogen occurring in the testicular vein. In the boar testis and epididymis, activity of steroid sulphatase (StS) and oestrogen sulphotransferase has been demonstrated. Thus apart from their synthesis in Leydig cells, provision of biologically active free oestrone seems also to depend on the activity and localization of these enzymes. Our aim was to establish expression patterns and activity of StS in boar testis. Testes were randomly collected from healthy boars and allotted to five age groups, five animals in each, aged 50, 100, 150, 200 and 250 days. Three extra boars aged over 250 days were castrated to obtain fresh tissue for enzyme activity tests. Immunohistochemistry detected StS only in the cytoplasm of Leydig cells and - except for day-50 group in which 65.1 +/- 4.9% (X +/- SD) of the cells were positive - expression was constant with virtually all the cells staining positive. RT-PCR and in situ hybridization confirmed expression and localization of StS mRNA. The V(max) and K(m) value (X +/- SD) for StS was 24.05 +/- 0.3 fmol/s/microg protein and 2.15 +/- 0.12 microM. These data suggest that StS within the Leydig cells of the boar is involved in modulation of testicular oestrogen bioavailability and that the site of sulpho-conjugation is not the testis but a different compartment of the testes-epididymidis complex.

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Additional indexing

Item Type:Journal Article, refereed, original work
Communities & Collections:05 Vetsuisse Faculty > Institute of Veterinary Anatomy
Dewey Decimal Classification:570 Life sciences; biology
Date:2009
Deposited On:17 Feb 2010 11:12
Last Modified:05 Apr 2016 13:57
Publisher:Wiley-Blackwell
ISSN:0936-6768
Publisher DOI:https://doi.org/10.1111/j.1439-0531.2007.00983.x
PubMed ID:18537908
Permanent URL: https://doi.org/10.5167/uzh-31214

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