Localization of 11 beta-hydroxysteroid dehydrogenase: specific protector of the mineralocorticoid receptor in mammalian olfactory mucosa.
The enzyme 11 beta-hydroxysteroid dehydrogenase (11 beta HSD) plays a major role in the protection of the mineralocorticoid (type I) receptor. The cellular mechanism of aldosterone selectivity relies on the coexpression of mineralocorticoid receptors and 11 beta HSD in the same cells. In the current study, 11 beta HSD activity was localized in the mammalian olfactory mucosa by a histochemical technique which links steroid metabolism with the deposition of formazan. The histochemical reaction results from oxidation of the synthetic substrate 11 beta-hydroxyandrostenedione and is dependent on nicotine-adenine dinucleotide (NAD). This demonstrates the presence of a dehydrogenase activity separate from the nicotineamide-adenine dinucleotide phosphate (NADP)-dependent 11 beta HSD. In the olfactory mucosa, the presence of NAD-dependent 11 beta HSD activity is localized to the sustentacular cells and acinar cells of Bowman's glands. No definite NAD-dependent activity was demonstrated in the olfactory receptor neurons. These data suggest that mineralocorticoid receptors present in acinar cells and sustentacular cells are aldosterone selective.
Kern
R C
RC
Department of Otolaryngology-Head and Neck Surgery, Northwestern University Medical School, Chicago, IL 60611, USA.
Pitovski
D Z
DZ
D042842:11-beta-Hydroxysteroid Dehydrogenases; D000818:Animals; D006168:Guinea Pigs; D006651:Histocytochemistry; D006913:Hydroxysteroid Dehydrogenases / Q000032:analysis*; D008297:Male; D009831:Olfactory Mucosa / Q000201:enzymology*
D006913:Hydroxysteroid Dehydrogenases; D042842:11-beta-Hydroxysteroid Dehydrogenases