scholarly journals Hormonal regulation of G i2 and mPR  in immortalized human oviductal cell line OE-E6/E7

2007 ◽  
Vol 13 (12) ◽  
pp. 845-851 ◽  
Author(s):  
K. S. Monkkonen ◽  
R. Aflatoonian ◽  
K.-F. Lee ◽  
W. S.B. Yeung ◽  
S.-W. Tsao ◽  
...  
Keyword(s):  
Cell Line ◽  
Hormonal Regulation ◽  
Oviductal Cell

Sulfate and chloride transport in Caco-2 cells: differential regulation by thyroxine and the possible role of DRAgene

2001 ◽  
Vol 280 (4) ◽  
pp. G603-G613 ◽  
Author(s):  
W. A. Alrefai ◽  
S. Tyagi ◽  
F. Mansour ◽  
S. Saksena ◽  
I. Syed ◽  
...  
Keyword(s):  
Cell Line ◽  
Hormonal Regulation ◽  
Competitive Inhibition ◽  
Chloride Transport ◽  
Exchange Process ◽  
Rnase Protection Assay ◽  
Maximum Velocity ◽  
Rnase Protection ◽  
Exchange Processes ◽  
Exchange Activity

The current studies were undertaken to establish an in vitro cellular model to study the transport of SO[Formula: see text] and Cl− and hormonal regulation and to define the possible function of the downregulated in adenoma ( DRA) gene. Utilizing a postconfluent Caco-2 cell line, we studied the OH− gradient-driven35SO[Formula: see text] and 36Cl−uptake. Our findings consistent with the presence of an apical carrier-mediated 35SO[Formula: see text]/OH−exchange process in Caco-2 cells include: 1) demonstration of saturation kinetics [Michaelis-Menten constant ( K m) of 0.2 ± 0.08 mM for SO[Formula: see text] and maximum velocity of 1.1 ± 0.2 pmol · mg protein−1 · 2 min−1]; 2) sensitivity to inhibition by DIDS ( K i = 0.9 ± 0.3 μM); and 3) competitive inhibition by oxalate and Cl−but not by nitrate and short chain fatty acids, with a higher K i (5.95 ± 1 mM) for Cl−compared with oxalate ( K i = 0.2 ± 0.03 mM). Our results also suggested that the SO[Formula: see text]/OH− and Cl−/OH− exchange processes in Caco-2 cells are distinct based on the following: 1) the SO[Formula: see text]/OH− exchange was highly sensitive to inhibition by DIDS compared with Cl−/OH−exchange activity ( K i for DIDS of 0.3 ± 0.1 mM); 2) Cl− competitively inhibited the SO[Formula: see text]/OH− exchange activity with a high K i compared with the K mfor SO[Formula: see text], indicating a lower affinity for Cl−; 3) DIDS competitively inhibited the Cl−/OH− exchange process, whereas it inhibited the SO[Formula: see text]/OH− exchange activity in a mixed-type manner; and 4) utilizing the RNase protection assay, our results showed that 24-h incubation with 100 nM of thyroxine significantly decreased the relative abundance of DRA mRNA along with the SO[Formula: see text]/OH− exchange activity but without any change in Cl−/OH− exchange process. In summary, these studies demonstrated the feasibility of utilizing Caco-2 cell line as a model to study the apical SO[Formula: see text]/OH− and Cl−/OH− exchange processes in the human intestine and indicated that the two transporters are distinct and that DRA may be predominantly a SO[Formula: see text]transporter with a capacity to transport Cl− as well.

scholarly journals Correction: Establishment of a New Cell Line from Lepidopteran Epidermis and Hormonal Regulation on the Genes

PLoS ONE ◽  
2008 ◽  
Vol 3 (10) ◽  
Author(s):  
Hong-Lian Shao ◽  
Wei-Wei Zheng ◽  
Peng-Cheng Liu ◽  
Qian Wang ◽  
Jin-Xing Wang ◽  
...  
Keyword(s):  
Cell Line ◽  
Hormonal Regulation ◽  
New Cell Line

Expression of human oviductin in an immortalized human oviductal cell line

2005 ◽  
Vol 84 ◽  
pp. 1095-1103 ◽  
Author(s):  
Ling Ling ◽  
Yin-Lau Lee ◽  
Kai-Fai Lee ◽  
Sai-Wah Tsao ◽  
William S.B. Yeung ◽  
...  
Keyword(s):  
Cell Line ◽  
Oviductal Cell

scholarly journals Expression of the liver 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase mRNA in FAO-1 cells

1993 ◽  
Vol 293 (1) ◽  
pp. 173-179 ◽  
Author(s):  
C Espinet ◽  
A M Vargas ◽  
M R el-Maghrabi ◽  
A J Lange ◽  
S J Pilkis
Keyword(s):  
Skeletal Muscle ◽  
Cell Line ◽  
Rat Liver ◽  
Hormonal Regulation ◽  
Hepatoma Cell ◽  
Hepatoma Cell Line ◽  
Bifunctional Enzyme ◽  
Dependent Manner ◽  
Rat Hepatoma Cell Line ◽  
Rat Hepatoma

The hormonal regulation of 6-phosphofructo-2-kinase/fructose-2,6-bisphosphatase gene expression was studied in the rat hepatoma cell line FAO-1. Both 6-phosphofructo-2-kinase and fructose-2,6-bisphosphatase activities were detected in FAO-1 cells, at 68% of the levels found in rat liver. Northern blot analysis showed that FAO-1 cells, like rat liver, contained a predominant species of bifunctional enzyme mRNA, which is 2.2 kb in size. A sensitive RNAase protection assay revealed the presence in FAO-1 cells of an additional mRNA species, which is generated when transcription is initiated from the skeletal muscle promoter of the rat liver/skeletal muscle gene. The liver/skeletal muscle mRNA ratio in FAO-1 cells was 10:1, which is similar to that observed in rat liver. In contrast, in another rat hepatoma cell line, FTO-2B, only the skeletal muscle mRNA was detected. Insulin and dexamethasone induced the liver bifunctional enzyme mRNA in FAO-1 cells by 2-4-fold and 10-20-fold respectively in a concentration- and time-dependent manner, and their effects were antagonized by cyclic AMP. Transcription of the gene in FAO-1 cells, measured by nuclear run-on assays, was also enhanced by dexamethasone and insulin. It is concluded that the FAO-1 cell line is similar to liver with respect to both the preferential use of the liver promoter of the gene and its regulation by hormones, and is therefore an excellent model for the study of the hepatic expression of this gene.

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