Carvacrol induces mitochondria-mediated apoptosis via disruption of calcium homeostasis in human choriocarcinoma cells

2018 ◽  
Vol 234 (2) ◽  
pp. 1803-1815 ◽  
Author(s):  
Whasun Lim ◽  
Jiyeon Ham ◽  
Fuller W. Bazer ◽  
Gwonhwa Song
Keyword(s):  
Calcium Homeostasis ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells

scholarly journals The biosynthesis, processing, and secretion of laminin by human choriocarcinoma cells.

1985 ◽  
Vol 260 (27) ◽  
pp. 14732-14742 ◽  
Author(s):  
B P Peters ◽  
R J Hartle ◽  
R F Krzesicki ◽  
T G Kroll ◽  
F Perini ◽  
...  
Keyword(s):  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells

scholarly journals Silencing of the Gene for the α-Subunit of Human Chorionic Gonadotropin by the Embryonic Transcription Factor Oct-3/4

1997 ◽  
Vol 11 (11) ◽  
pp. 1651-1658 ◽  
Author(s):  
Limin Liu ◽  
Douglas Leaman ◽  
Michel Villalta ◽  
R. Michael Roberts
Keyword(s):  
Transcription Factor ◽  
Binding Site ◽  
Gene Promoter ◽  
Site Directed Mutagenesis ◽  
Mobility Shift ◽  
Α Subunit ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells ◽  
Electrophoretic Mobility Shift Assays ◽  
Jar Cells

Abstract CG is required for maintenance of the corpus luteum during pregnancy in higher primates. As CG is a heterodimeric molecule, some form of coordinated control must be maintained over the transcription of its two subunit genes. We recently found that expression of human CG β-subunit (hCGβ) in JAr human choriocarcinoma cells was almost completely silenced by the embryonic transcription factor Oct-3/4, which bound to a unique ACAATAATCA octameric sequence in the hCGβ gene promoter. Here we report that Oct-3/4 is also a potent inhibitor of hCG α-subunit (hCGα) expression in JAr cells. Oct-3/4 reduced human GH reporter expression from the −170 hCGα promoter in either the presence or absence of cAMP by about 70% in transient cotransfection assays, but had no effect on expression from either the −148 hCGα or the −99 hCGα promoter. Unexpectedly, no Oct-3/4-binding site was identified within the −170 to −148 region of the hCGα promoter, although one was found around position −115 by both methylation interference footprinting and electrophoretic mobility shift assays. Site-directed mutagenesis of this binding site destroyed the affinity of the promoter for Oct-3/4, but did not affect repression of the promoter. Therefore, inhibition of hCGα gene transcription by Oct-3/4 appears not to involve direct binding of this factor to the site responsible for silencing. When stably transfected into JAr cells, Oct-3/4 reduced the amounts of both endogenous hCGα mRNA and protein by 70–80%. Oct-3/4 is therefore capable of silencing both hCGα and hCGβ gene expression. We suggest that as the trophoblast begins to form, reduction of Oct-3/4 expression permits the coordinated onset of transcription from the hCGα and hCGβ genes.

scholarly journals Expression of the Germ Cell Alkaline Phosphatase Gene in Human Choriocarcinoma Cells

1989 ◽  
Vol 264 (21) ◽  
pp. 12611-12619
Author(s):  
S Watanabe ◽  
T Watanabe ◽  
W B Li ◽  
B W Soong ◽  
J Y Chou
Keyword(s):  
Alkaline Phosphatase ◽  
Germ Cell ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells

Uptake and Degradation of Plasma Lipoproteins by Human Choriocarcinoma Cells in Culture*

Endocrinology ◽  
1979 ◽  
Vol 104 (1) ◽  
pp. 8-16 ◽  
Author(s):  
E. R. SIMPSON ◽  
D. W. BILHEIMER ◽  
P. C. MACDONALD ◽  
J. C. PORTER
Keyword(s):  
Plasma Lipoproteins ◽  
Cells In Culture ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells

scholarly journals DNA Binding of TEA/ATTS Domain Factors Is Regulated by Protein Kinase C Phosphorylation in Human Choriocarcinoma Cells

2001 ◽  
Vol 276 (26) ◽  
pp. 23464-23470 ◽  
Author(s):  
Shi-Wen Jiang ◽  
Maoqing Dong ◽  
Miguel A. Trujillo ◽  
Laurence J. Miller ◽  
Norman L. Eberhardt
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Dna Binding ◽  
Kinase C ◽  
Choriocarcinoma Cells ◽  
Human Choriocarcinoma Cells

In vitro study of placental trophoblast calcium uptake using JEG-3 human choriocarcinoma cells

1991 ◽  
Vol 98 (3) ◽  
pp. 333-342
Author(s):  
R.S. Tuan ◽  
C.J. Moore ◽  
J.W. Brittingham ◽  
J.J. Kirwin ◽  
R.E. Akins ◽  
...  
Keyword(s):  
Vitamin D3 ◽  
Calcium Uptake ◽  
In Vitro Model ◽  
Dependent Manner ◽  
Choriocarcinoma Cells ◽  
Vitro Model ◽  
Human Choriocarcinoma Cells ◽  
Functional Components ◽  
1,25 Dihydroxy Vitamin D3

During human fetal development, placental syncytiotrophoblasts actively transport calcium from the maternal to the fetal circulation. Two functional components, a cytosolic Ca2(+)-binding protein (CaBP) and a Ca2(+)-ATPase have been identified in the syncytiotrophoblasts of the chorionic villi. We report here the calcium uptake properties of a human choriocarcinoma cell line, JEG-3, which was used as an in vitro model cell system for the syncytiotrophoblasts. In culture, JEG-3 proliferated as large syncytial aggregates expressing typical syncytiotrophoblast markers. 45Ca uptake by JEG-3 was a substrate- and temperature-dependent, membrane-mediated active process that exhibited linear kinetics for up to 7 min. Both the CaBP and the Ca2(+)-ATPase were expressed by JEG-3, on the basis of biochemical, histochemical, immunochemical and or mRNA assays. Immunohistochemistry and in situ hybridization revealed that JEG-3 cells were heterogeneous with respect to the expression of the CaBP. The Ca2(+)-ATPase activity of JEG-3 was similar to the placental enzyme in terms of sensitivity to specific inhibitors, and was detected histochemically along the cell membrane. Fura-2 Ca2+ imaging revealed that calcium uptake by JEG-3 was not accompanied by a concomitant increase in cytosolic [Ca2+], suggesting a specific Ca2+ sequestration mechanism. The involvement of calciotropic hormonal regulation was evaluated by studying the response of JEG-3 to 1,25-dihydroxy vitamin D3. Calcium uptake was significantly stimulated in a dose-dependent manner by a 24-h treatment of the cells with 1,25-dihydroxy vitamin D3 (optimal dose approximately 0.5 nM); the CaBP level doubled whereas steady-state CaBP mRNA did not, suggesting that CaBP expression was regulated by 1,25-dihydroxy vitamin D3. These observations strongly suggest that the JEG-3 human choriocarcinoma cells should serve as a convenient in vitro model system for studying the cellular mechanism and regulation of transplacental calcium transport.

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