A time-course regulatory and kinetic expression study of steroid metabolizing enzymes by calcitriol in primary cultured human placental cells

Abstract 1,25-dihydroxivitamin D 3 (calcitriol), is a secoesteroid involved in several placental functions. In particular, we and others showed that calcitriol regulates peptides, proteins, cytokines and hormones production in human trophoblastic cells. On the other hand, calcitriol modifies the activity and expression of some steroidogenic enzymes, a process that is considered tissue-specific. However, the effects of calcitriol on the expression of enzymes involved in the synthesis of sex steroids in placental tissue have not yet been entirely studied. The aim of the present study was to investigate the effects of calcitriol upon gene expression of several steroid enzymes such as cytochrome P450scc ( CYP11A1 ), type 1 3β-hydroxysteroid dehydrogenase( 3β-HSDI ), 17β-HSD3 , 17α-hydroxylase/17,20 lyase ( CYP17A1 ) and aromatase ( CYP19A1 ) in primary cultures of human placental cells. Cell cultures were performed using placentas obtained immediately after delivery by caesarean section from normotensive healthy women and calcitriol effects were evaluated, at level of transcription, by qPCR. The results showed that: 1) from basal expression values of the five genes studied, 3β-HSDI was the most expressed gene (P  CYP11A1 , CYP19A1 and 17β-HSD3 gene expression at 3 h of treatment whereas 3β-HSDI was induced at 6 h (P