Immunohistochemical Localization of Cytochrome P-450 and Reduced Nicotinamide Adenine Dinucleotide Phosphate: Cytochrome P-450 Reductase in the Rat Ventral Prostate

Tapio Haaparanta, Maria Norgârd, Lena Haglund, Hans Glaumann, Jan-Ake Gustafsson

Research output: Contribution to journalArticlepeer-review

10 Scopus citations

Abstract

Rabbit antibodies raised against the major isozymes of cytochrome P-450 isolated from hepatic microsomes of β-naphthoflavone- (BNF) and phenobarbital-treated rats (cytochrome P-450 BNF-B2 and cytochrome P-450 PB-B2, respectively) and against rat liver NADPH-cytochrome P-450 reductase were used to localize these enzymes immunohistochemically in the rat ventral prostate. Using the unlabeled antibody peroxidase-antiperoxidase technique, NADPH-cytochrome P-450 reductase was detected exclusively in the epithelial cells of the gland to the same magnitude in untreated, phenobarbital-, and BNF-treated rats. Cytochrome P-450 BNF-B2-like immunoreactivity was exclusively present in the glandular epithelium in BNF-treated rats, whereas staining could not be visualized in untreated or in phenobarbital-treated rats. The staining for NADPH-cytochrome P-450 reductase was more uniformly distributed within the epithelium than was the cytochrome P-450 BNF-B2-like immunoreactivity. Cytochrome P-450 PB-B2-like immunoreactivity was not found, regardless of animal pretreatment. These findings support our previous results demonstrating the presence of constitutive NADPH-cytochrome P-450 reductase in the prostate and that an isozyme of cytochrome P-450 is highly inducible by BNF in this gland. The significance of these findings are discussed in view of the essentially unknown etiology of human prostatic cancer.

Original languageEnglish (US)
Pages (from-to)1259-1262
Number of pages4
JournalCancer research
Volume45
Issue number3
StatePublished - Mar 1 1985

ASJC Scopus subject areas

  • Oncology
  • Cancer Research

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