It is known that there is a local biosynthesis of
estradiol (E2) in
breast carcinoma. The steroidogenic
enzymes involved in E2 formation are
aromatase which transforms
testosterone into E2 and
androstenedione into
estrone (E1) and reductive 17beta-hydroxysteroid
dehydrogenases (17beta-HSDs) which convert E1 into E2. Using immunocytochemistry, we have studied the expression of
aromatase and the three reductive 17beta-HSDs 17beta-HSD types 1, 7 and 12 in 41 specimens of female human
breast carcinoma and adjacent non-malignant tissues. These results were correlated with the
estrogen receptor alpha (
ERalpha) and beta (
ERbeta),
progesterone receptor,
androgen receptor, CDC47 and c-erb B-2 expressions and with the
tumor stages.
Aromatase was found in 58%, 17beta-HSD type 7 in 47% and 17beta-HSD type 12 in 83% of the
breast cancer specimens. The 17beta-HSD type 1 could be detected in only one
tumor. A significant correlation was observed between the
aromatase, 17beta-HSD type 7 and 17beta-HSD type 12 expression, as well as between each of the two
enzymes 17beta-types 7 and 12 and the
ERbeta expression. The expression of 17beta-HSD type 12 was significantly higher in
breast carcinoma specimens than in normal tissue. There was also a significant association of CDC 47 expression with
ERbeta, AR and 17beta-HSD type 12. The results indicate that
aromatase, 17beta-HSD type 7 and 17beta-HSD type 12, but not 17beta-HSD type 1, are commonly expressed in human
breast cancer. Moreover, the high expression of both 17beta-HSD type 12 and
ERbeta in
breast carcinoma cells may play a role in the development and/or progression of
breast cancer.