T. Sano et al., 17 beta-hydroxysteroid dehydrogenase type 2 expression and enzyme activityin the human gastrointestinal tract, CLIN SCI, 101(5), 2001, pp. 485-491
The 17 beta -hydroxysteroid dehydrogenases (17 beta HSDs) play an important
role in the regulation of intracellular levels of biologically active sex
steroid hormones in various human tissues. To date, eight distinctive 17 be
ta HSD enzymes have been cloned and characterized in humans. Among these is
oenzymes, 17 beta HSD type 2 (17 beta HSD2) catalyses the conversion of tes
tosterone into androstenedione and/or oestradiol into oestrone in various t
issues, and it has thus been suggested to be involved in the biological ina
ctivation of these sex steroids. The human gastrointestinal tract and liver
are considered as the principle sites of inactivation and metabolism of va
rious forms of orally administered sex steroids. We therefore examined 17 b
eta HSD2 expression and activity in human adult non-pathological gastrointe
stinal tract in order to clarify further the biological significance of thi
s enzyme. A total of 80 specimens (40 from males and 40 from females) of no
rmal oesophageal, stomach, duodenal, ileal, colonic and rectal tissues were
examined for immunohistochemistry. Altogether, 17 tissue specimens were us
ed for enzyme assay, and eight for RNA analysis. 17 beta HSD2 activity was
detected in the stomach, duodenum, ileum, colon and rectum. 17 beta HSD2 mR
NA was most abundant in the small intestine. 17 beta HSD2 immunoreactivity
was localized almost exclusively to the absorptive epithelium, which may be
involved in the inactivation of excessive endogenous and exogenous active
sex steroids. Results from the present study thus suggest that the human ga
strointestinal tract is an important sex steroid metabolizing organ in huma
ns.