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. 2005 Dec 22:3:72.
doi: 10.1186/1477-7827-3-72.

Cytochrome P450 aromatase expression in human seminoma

Vittoria Rago  1 , Francesco Romeo, Saveria Aquila, Daniela Montanaro, Sebastiano Andò, Amalia Carpino
Affiliations

Cytochrome P450 aromatase expression in human seminoma

Vittoria Rago et al. Reprod Biol Endocrinol. .

Abstract

Background: The enzyme cytochrome P450 aromatase, catalysing the conversion of androgens into estrogens, has been detected in normal human testicular cells suggesting a physiological role of local estrogen biosynthesis on spermatogenesis control. Estrogens, regulating cell growth and apoptosis, can also be involved in tumorigenesis process, but the possible link between estrogens and testicular neoplastic process is, up to now, scarcely known. This study examined aromatase expression in human seminoma, which is the most common germ cell tumour of the testis.

Methods: The tumour-bearing testes were obtained from 20 patients with classic seminoma undergoing to therapeutic orchidectomy. Paraffin embedded tissues were processed for immunohistochemistry using a mouse monoclonal antibody generated against human placental cytochrome P450 arom, as primary antibody, and a biotinylated goat-anti-mouse IgG, as secondary antibody. Furthermore, Western blot analysis of seminoma extracts was carried out.

Results: Intense P450 arom immunoreactivity was observed in the seminoma cells and Western blot analysis confirmed the immunodetection. A strong immunostaining was also detected in cells of intratubular germ cell neoplasia (IGCN), adjacent to seminoma.

Conclusion: The present study demonstrated, for the first time in human, aromatase expression in neoplastic cells of seminoma suggesting a relation between local estrogen biosynthesis and germ cell tumorigenesis. The P450 arom immunolocalization in the cells of IGCN, representing the common precursor of most germ cell tumors, seems to support these findings.

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Figures

Figure 1
Figure 1
Morphology and P450 arom immunoreactivity of tumoral region in human testis with seminoma. A-B: Haematoxylin-eosin staining. C-D: Strong P450 arom immunoreactivity in cytoplasm of neoplastic cells (Nc) and unstained lymphocytes (L). Insert: absorption control. Scale bars: A, 20 μm; B-C, 12.5 μm; D, 5 μm.
Figure 2
Figure 2
P450 arom immunoreactivity in testicular region adjacent to seminoma and in controls A: Intense aromatase immunostaining in IGCN cells. B: Placental-like alkaline phosphatase staining of IGCN basal cells C: Strong aromatase immunoreactivity of interstitial Leydig cells in normal testis (Lc) D: Intense immunostaining of luteal cells (Luc) in ovarian tissue Scale bars: A-B, 8 μm; C,12.5 μm; D, 5 μm.
Figure 3
Figure 3
Immunoblot of aromatase from seminoma extracts. Lane 1: purified P450 arom protein from human placenta (positive control). Lane 2: negative control prepared as described in Material and Methods. Lanes 3, 4, 5: 55 kDa P450 arom immunoreactive bands from lysates of three different seminoma extracts. Numbers on the left correspond to molecular weights of marker proteins.
See this image and copyright information in PMC

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