Roland B L, Funder J W
Baker Institute of Medical Research, Prahan, Victoria, Australia.
Endocrinology. 1996 Mar;137(3):1123-8. doi: 10.1210/endo.137.3.8603583.
In the rat, the enzyme 11beta-hydroxysteroid dehydrogenase 2 (11betaHSD2) converts the glucocorticoid corticosterone into receptor-inactive 11-dehydrocorticosterone, thereby allowing preferential access of aldosterone to mineralocorticoid receptors (MR). The present study examines the distribution of this enzyme by in situ hybridization, using a homologous complementary RNA probe for 11betaHSD2. 11betaHSD2 messenger RNA was detected in classic epithelial aldosterone target tissues (kidney, salivary glands, and colon), the female reproductive system (ovary, oviduct, uterus, and placenta), and the adrenals; levels in heart, testis, and liver were below the limits of detection. We interpret the finding of 11betaHSD2 expression in both classical MR-containing aldosterone target tissues and a variety of other tissue as evidence that in the rat, the enzyme may play physiological roles in addition to that of excluding glucocorticoids from epithelial MR.
在大鼠中,11β-羟基类固醇脱氢酶2(11βHSD2)可将糖皮质激素皮质酮转化为无受体活性的11-脱氢皮质酮,从而使醛固酮能够优先作用于盐皮质激素受体(MR)。本研究使用针对11βHSD2的同源互补RNA探针,通过原位杂交检测该酶的分布。在典型的上皮性醛固酮靶组织(肾脏、唾液腺和结肠)、雌性生殖系统(卵巢、输卵管、子宫和胎盘)以及肾上腺中检测到了11βHSD2信使核糖核酸;心脏、睾丸和肝脏中的水平低于检测限。我们将在含经典MR的醛固酮靶组织和多种其他组织中发现11βHSD2表达这一结果解释为,在大鼠中,该酶除了具有将糖皮质激素排除在上皮MR之外的作用外,可能还发挥着生理作用。