Placental steroid hormones

Schubert, Kai; Schade, K

doi:10.1016/0022-4731(77)90234-5

Journal of Steroid Biochemistry

1977

DOI: 10.1016/0022-4731(77)90234-5

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Placental steroid hormones

Kai Schubert

K Schade

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Cited by 11 publications

(1 citation statement)

References 35 publications

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“…As a transitory endocrine organ, human placenta is responsible for the synthesis of a number of steroid hor-mones via their metabolizing enzymes (6,7). 11␤-hydroxysteroid dehydrogenase type 2 (11␤-HSD2) (encoded by hsd11b2), a high-affinity dehydrogenase that inactivates biologically active cortisol to inactive cortisone, is one such enzyme that is highly expressed in human placental trophoblasts.…”

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confidence: 99%

Up-regulation of 11β-Hydroxysteroid Dehydrogenase Type 2 Expression by Hedgehog Ligand Contributes to the Conversion of Cortisol Into Cortisone

et al. 2016

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The cortisol-inactivating enzyme 11␤-hydroxysteroid dehydrogenase type 2 (11␤-HSD2) that catalyzes the intracellular inactivation of glucocorticoids plays a pivotal role in human pregnant maintenance and normal fetal development. Given the fact that the main components of Hedgehog (HH) signaling pathway are predominantly expressed in syncytial layer of human placental villi where 11␤-HSD2 is robustly expressed, in the present study, we have investigated the potential roles and underlying mechanisms of HH signaling in 11␤-HSD2 expression. Activation of HH signaling by a variety of approaches robustly induced 11␤-HSD2 expression as well as the 11␤-HSD2 activity, whereas suppression of HH signaling significantly attenuated 11␤-HSD2 expression as well as the 11␤-HSD2 activity in both human primary cytotrophoblasts and trophoblast-like BeWo cells. Moreover, among glioma-associated oncogene (GLI) family transcriptional factors in HH signaling, knockdown of GLI2 but not GLI1 and GLI3 significantly attenuated HH-induced 11␤-HSD2 expression and activity, and overexpression of GLI2 activator alone was sufficient to induce 11␤-HSD2 expression and activity. Finally, GLI2 not only directly bound to the promoter region of gene hsd11b2 to transactivate hsd11b2 but also formed a heterodimer with RNA polymerase II, an enzyme that catalyzes the transcription of DNA to synthesize mRNAs, resulting in up-regulation of hsd11b2 gene transcription. Taken together, the present study has uncovered a hitherto uncharacterized role of HH/GLI2 signaling in 11␤-HSD2 regulation, implicating that HH signaling through GLI2 could be required for the human pregnant maintenance and fetal development. PTC1 from inhibiting the activity of SMO. Activated SMO in turn initiates a series of intracellular events that culminate in activation and nuclear localization of glioblastoma (glioma-associated oncogene [GLI]) family transcription factors, which further promotes transcription of HH-responsive genes, such as Bcl2, myc, and cyclin D as well as Ptc1 and Gli1, 2 components of the HH signaling pathway itself (3-5).As a transitory endocrine organ, human placenta is responsible for the synthesis of a number of steroid hor-

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confidence: 99%

Up-regulation of 11β-Hydroxysteroid Dehydrogenase Type 2 Expression by Hedgehog Ligand Contributes to the Conversion of Cortisol Into Cortisone

et al. 2016

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De novo biosynthesis of 6β-hydroperoxyandrostenedione in human placental microsomes

Tan

Navennec

Gévry

1984

Biochemical and Biophysical Research Communications

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Quantitation of progesterone and 20α-dihydroprogesterone in human placenta and fetal membranes

Laatikainen

Pesonen

Pelkonen

1981

Journal of Steroid Biochemistry

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Placental steroid hormones

Cited by 11 publications

References 35 publications

Up-regulation of 11β-Hydroxysteroid Dehydrogenase Type 2 Expression by Hedgehog Ligand Contributes to the Conversion of Cortisol Into Cortisone

Up-regulation of 11β-Hydroxysteroid Dehydrogenase Type 2 Expression by Hedgehog Ligand Contributes to the Conversion of Cortisol Into Cortisone

De novo biosynthesis of 6β-hydroperoxyandrostenedione in human placental microsomes

Quantitation of progesterone and 20α-dihydroprogesterone in human placenta and fetal membranes

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