Differential display analysis of oxygen-mediated changes in gene expression in first trimester human trophoblast cells

Placenta ◽  
1998 ◽  
Vol 19 (7) ◽  
pp. 483-488 ◽  
Author(s):  
B.J. Pak ◽  
H. Park ◽  
E.R. Chang ◽  
S.C. Pang ◽  
C.H. Graham
2017 ◽  
Vol 2017 ◽  
pp. 1-12
Author(s):  
Chang-ying Xing ◽  
De-xiang Zhang ◽  
Sui-qi Gui ◽  
Min-fang Tao

Kidney-replenishing herb is a traditional medicine formula in China which has been widely used for clinical treatment of recurrent miscarriage. Our previous study showed that Kidney-replenishing herb could promote proliferation and inhibit apoptosis of the human first-trimester trophoblasts. In the present study, we further explored the potential mechanism and signal pathway of Kidney-replenishing herb on human trophoblast cells. Our research showed that Kidney-replenishing herb stimulated proliferation and reduced apoptosis of human trophoblast cells in vitro, and this appeared to be positive correlation with SOCS-3 transcription, suggesting that Kidney-replenishing herb regulated biological functions of human trophoblast cells by inducing SCOS-3 expression. Furthermore, the Kidney-replenishing herb treatment stimulated the phosphorylation of ERK1/2, and blocking the signaling pathway by mitogen-activated protein MAPK (MEK) inhibitor, U0126, inhibited Kidney-replenishing herb-induced SOCS-3 transcription, depressed proliferation, and promoted apoptosis of human trophoblasts. Kidney-replenishing herbs still induced ERK1/2 phosphorylation after SOCS-3 siRNA silence. Overexpression of SOCS-3 stimulated the proliferation of trophoblast. These findings suggest that SOCS-3 expression is induced by Kidney-replenishing herbs via activation of MAPK pathways, and this may possibly be involved in promoting human trophoblast cells growth which is contributed to embryo development.


1989 ◽  
Vol 161 (2) ◽  
pp. 446-453 ◽  
Author(s):  
Mrinal K. Sanyal ◽  
Charles J. Brami ◽  
Paul Bischof ◽  
Edwina Simmons ◽  
Eytan R. Barnea ◽  
...  

PLoS ONE ◽  
2014 ◽  
Vol 9 (6) ◽  
pp. e99680 ◽  
Author(s):  
Víctor A. Francis ◽  
Aron B. Abera ◽  
Mushi Matjila ◽  
Robert P. Millar ◽  
Arieh A. Katz

Placenta ◽  
2011 ◽  
Vol 32 (1) ◽  
pp. 33-43 ◽  
Author(s):  
R. Apps ◽  
A. Sharkey ◽  
L. Gardner ◽  
V. Male ◽  
M. Trotter ◽  
...  

Endocrinology ◽  
2005 ◽  
Vol 146 (3) ◽  
pp. 1482-1490 ◽  
Author(s):  
Laura Julan ◽  
Haiyan Guan ◽  
Jonathan P. van Beek ◽  
Kaiping Yang

Accumulating evidence suggests that the human placental enzyme 11β-hydroxysteroid dehydrogenase type 2 (11β-HSD2) plays a key role in fetal development by controlling fetal exposure to maternal glucocorticoids. Recently, the nuclear peroxisome proliferator-activated receptor δ (PPARδ) has been found to be the most abundantly expressed PPAR subtype in the human placenta, but its function in this organ is unknown. Given that PPARδ-null mice exhibited placental defects and consequent intrauterine growth restriction, the present study was undertaken to examine the hypothesis that PPARδ regulates human placental function in part by targeting 11β-HSD2. Using cultured human trophoblast cells as a model system, we demonstrated that 1) the putative PPARδ agonist carbaprostacyclin (cPGI2) reduced 11β-HSD2 activity as well as 11β-HSD2 expression at both protein and mRNA levels; 2) GW610742 (a selective PPARδ agonist) mimicked the effect of cPGI2, whereas indomethacin (a known ligand for PPARα and PPARγ) had no effect; 3) the cPGI2-induced down-regulation of 11β-HSD2 mRNA did not require de novo protein synthesis; 4) cPGI2 suppressed HSD11B2 promoter activity, but did not alter the half-life of 11β-HSD2 mRNA; and 5) the inhibitory effect of cPGI2 on HSD11B2 promoter activity was abrogated in trophoblast cells cotransfected with a dominant negative PPARδ mutant. Taken together, these findings suggest that activation of PPARδ down-regulates HSD11B2 gene expression in human trophoblast cells, and that this effect is mediated primarily at the transcriptional level. Thus, the present study reveals 11β-HSD2 as an additional target for PPARδ and identifies a molecular mechanism by which this nuclear receptor may regulate human placental function.


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