BACKGROUND: Prostate trophism depends on DHT formed from T by the enzyme 5α-R. Two 5α-R isoforms with different biochemical characteristics have been cloned. Also estrogens might contribute to the prostate growth; however, their intraglandular formation by the enzyme aromatase is still debated. The aim of the present study was to verify whether (a) only one or both isoforms of the 5α-Rs are expressed in the prostate cancer cell line LNCaP and in BPH, or (b) the aromatase is present in these samples. METHODS:The profile of the pH optimum of the 5α-Rs was evaluated “in vitro” in LNCaP cells by the production of labeled 5α-reduced metabolites either from [14C]-T or [14C]-D4 at pH 3.5–8. The gene expression of the two 5α-Rs and of the aromatase in LNCaP cells and in BPH specimens was analyzed by RT-PCR combined to Southern blot analysis, using specific sets of oligonucleotides. The tissue localization of 5α-R1 was analyzed by immunohistochemistry using an anti-5α-R1 polyclonal antibody. RESULTS: (a) In LNCaP cells, the formation of 5α-reduced metabolites from the respective precursors increases progressively as a function of pH, being the highest at neutral pH values; (b) the 5α-R1 isoform is expressed in both LNCaP cells and in BPH, while the 5α-R2 mRNA is present only in BPH, but not in LNCaP cells; and (c) no aromatase transcripts were observed either in BPH or in LNCaP cells. CONCLUSIONS: A careful examination of the possible differential expression of T-activating enzymes, particularly in prostate cancer, would be of help to choose the appropriate treatment.

Presence of 5α-Reductase isozymes and aromatase in human prostate cancer cells and in benign prostate hyperplastic tissue / P. Negri-Cesi, A. Poletti, A. Colciago, P. Magni, P. Martini, M. Motta. - In: THE PROSTATE. - ISSN 0270-4137. - 34:4(1998 Mar 01), pp. 283-291. [10.1002/(SICI)1097-0045(19980301)34:4<283::AID-PROS6>3.0.CO;2-I]

Presence of 5α-Reductase isozymes and aromatase in human prostate cancer cells and in benign prostate hyperplastic tissue

NEGRI CESI, PAOLA;A. Poletti;A. Colciago;P. Magni;M. Motta
1998-03-01

Abstract

BACKGROUND: Prostate trophism depends on DHT formed from T by the enzyme 5α-R. Two 5α-R isoforms with different biochemical characteristics have been cloned. Also estrogens might contribute to the prostate growth; however, their intraglandular formation by the enzyme aromatase is still debated. The aim of the present study was to verify whether (a) only one or both isoforms of the 5α-Rs are expressed in the prostate cancer cell line LNCaP and in BPH, or (b) the aromatase is present in these samples. METHODS:The profile of the pH optimum of the 5α-Rs was evaluated “in vitro” in LNCaP cells by the production of labeled 5α-reduced metabolites either from [14C]-T or [14C]-D4 at pH 3.5–8. The gene expression of the two 5α-Rs and of the aromatase in LNCaP cells and in BPH specimens was analyzed by RT-PCR combined to Southern blot analysis, using specific sets of oligonucleotides. The tissue localization of 5α-R1 was analyzed by immunohistochemistry using an anti-5α-R1 polyclonal antibody. RESULTS: (a) In LNCaP cells, the formation of 5α-reduced metabolites from the respective precursors increases progressively as a function of pH, being the highest at neutral pH values; (b) the 5α-R1 isoform is expressed in both LNCaP cells and in BPH, while the 5α-R2 mRNA is present only in BPH, but not in LNCaP cells; and (c) no aromatase transcripts were observed either in BPH or in LNCaP cells. CONCLUSIONS: A careful examination of the possible differential expression of T-activating enzymes, particularly in prostate cancer, would be of help to choose the appropriate treatment.
5 alpha-reductase; aromatase; LNCaP cells; benign prostate hyperplasia
Settore BIO/09 - Fisiologia
Settore BIO/13 - Biologia Applicata
Settore MED/04 - Patologia Generale
Settore MED/05 - Patologia Clinica
Settore MED/13 - Endocrinologia
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Utilizza questo identificativo per citare o creare un link a questo documento: http://hdl.handle.net/2434/182106
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