H. Peltoketo et al., Two 17 beta-hydroxysteroid dehydrogenases (17HSDs) of estradiol biosynthesis: 17HSD type 1 and type 7, J STEROID B, 69(1-6), 1999, pp. 431-439
Citations number
46
Categorie Soggetti
Biochemistry & Biophysics
Journal title
JOURNAL OF STEROID BIOCHEMISTRY AND MOLECULAR BIOLOGY
Two 17 beta-hydroxysteroid dehydrogenases (17HSDs), type 1 and type 7, are
enzymes of estradiol biosynthesis, in addition to which rodent type 1 enzym
es are also able to catalyze androgens. Both of the 17HSDs are abundantly e
xpressed in ovaries, the type 1 enzyme in granulosa cells and type 7 in lut
einized cells. The expression of 17HSD7, which has also been described as a
prolactin receptor-associated protein (PRAP), is particularly up-regulated
in corpus luteum during the second half of rodent pregnancy. A moderate or
slight signal for mouse 17HSD7/PRAP mRNA has also been demonstrated in sam
ples of placenta and mammary gland, for example. Human, but not rodent, 17H
SD1 is expressed in placenta, breast epithelium and endometrium in addition
to ovaries. A cell-specific enhancer, silencer and promoter in the hHSD17B
1 gene participate in the regulation of type 1 enzyme expression. The enhan
cer consists of several subunits, including a retinoic acid response elemen
t, the silencer has a binding motif for GATA factors, and the proximal prom
oter contains adjacent and competing AP-2 and Sp binding sites. (C) 1999 El
sevier Science Ltd. All rights reserved.