Exp Clin Endocrinol Diabetes 1995; 103(2): 105-112
DOI: 10.1055/s-0029-1211337
Original

© J. A. Barth Verlag in Georg Thieme Verlag KG Stuttgart · New York

Distribution of rat hepatic steroid 5α-reductase 1 as shown by immunohistochemistry

W. Eicheler1 , J. Seitz1 , M. Steinhoff1 , WG. Forssmann2 , K. Adermann2 , G. Aumüller1
  • 1Philipps-University Marburg, Department of Anatomy and Cell Biology, Marburg, Germany
  • 2Lower Saxony Institute for Peptide Research (IPF), Hannover, Germany
Further Information

Publication History

Publication Date:
15 July 2009 (online)

Summary

Peptide fragments of rat liver 5a-reductase were synthesized according to the published primary sequence data. The peptides were used (i) in free form and (ii) linked to keyhole limpet hemocyanin (KLH), respectively, for immunization of rabbits. Resulting antisera showed positive reaction with the respective peptide-antigen in an ELISA. In Western blot experiments the antisera specifically recognized a 26,000 mol wt protein in extracts from female and male rat liver. All antisera, as well as isolated immunoglobulins, showed inhibition of 5α-reductase activity in microsomes prepared from rat liver. Positive immunohistochemical reactions were observed in the perinuclear cytoplasm of hepatocytes. No reaction was seen in Kupffer- and connective tissue cells. Acinar heterogeneity of the immunoreaction was seen in the male rat liver with a gradient from the portal canal to the central vein. After androgen-deprivation a considerable increase in immunoreactivity was seen in male rat liver cells, indicating androgen-dependent suppression of the enzyme in male liver.