Evaluation of effectiveness of chemical and physical sewage treatment technologies for removal of retinoic acid receptor agonistic activity detected in sewage effluent

2009 ◽  
Vol 59 (12) ◽  
pp. 2447-2453 ◽  
Author(s):  
D. Inoue ◽  
H. Matsui ◽  
K. Sei ◽  
J. Hu ◽  
M. Yang ◽  
...  

Retinoic acid receptor (RAR) is a nuclear receptor involved in vertebrate morphogenesis, growth, cellular differentiation, and tissue homeostasis. Excess expression of the retinoid signaling can cause various developmental toxicities in animals and humans. We previously found that influents from sewage treatment plants (STPs) in Japan had a RAR agonistic activity and the activity cannot be removed completely by conventional biological treatments. In this study, we assessed the performance of chemical and physical sewage treatment technologies—ozonation, ultraviolet treatment, chlorination, coagulation using polyaluminium chloride (PAC) and ferric sulfate, and filtration with ultrafiltration (UF), nanofiltration (NF), and reverse osmosis (RO) membranes—in removal of RAR agonistic activity of STP effluent. All water treatment experiments were conducted in laboratory-scale reactors. The RAR agonistic activity of samples was measured using a yeast two-hybrid assay. Results showed that the effectiveness of tested technologies on the removal of RAR agonistic activity can be ranked as RO or NF > chlorination > ozonation > MF > UV > coagulation with ferric sulfate>>coagulation with PAC. Furthermore, the effectiveness of chlorination might rank lower because excess reaction might bring a side effect by producing some RAR agonistic by-product(s).

1999 ◽  
Vol 13 (2) ◽  
pp. 276-285 ◽  
Author(s):  
Xiao-Feng Zhou ◽  
Xi-Qiang Shen ◽  
Lirim Shemshedini

Abstract In the presence of retinoic acid (RA), the retinoid receptors, retinoic acid receptor (RAR) and retinoid X receptor (RXR), are able to up-regulate transcription directly by binding to RA-responsive elements on the promoters of responsive genes. Liganded RARs and RXRs are also capable of down-regulating transcription, but, by contrast, this is an indirect effect, mediated by the interaction of these nuclear receptors not with DNA but the transcription factor activating protein-1 (AP-1). AP-1 is a dimeric complex of the protooncoproteins c-Jun and c-Fos and directly regulates transcription of genes important for cellular growth. Previous in vitro results have suggested that RARs can block AP-1 DNA binding. Using a mammalian two-hybrid system, we report here that human RARα (hRARα) can disrupt in a RA-dependent manner the homo- and heterodimerization properties of c-Jun and c-Fos. This inhibition of dimerization is cell specific, occurring only in those cells that exhibit RA-induced repression of AP-1 transcriptional activity. Furthermore, this mechanism appears to be specific for the RARs, since another potent inhibitor of AP-1 activity, the glucocorticoid receptor, does not affect AP-1 dimerization. Our data argue for a novel mechanism by which RARs can repress AP-1 DNA binding, in which liganded RARs are able to interfere with c-Jun/c-Jun homodimerization and c-Jun/c-Fos heterodimerization and, in this way, may prevent the formation of AP-1 complexes capable of DNA binding.


2009 ◽  
Vol 43 (17) ◽  
pp. 6611-6616 ◽  
Author(s):  
Huajun Zhen ◽  
Xiaoqin Wu ◽  
Jianying Hu ◽  
Yang Xiao ◽  
Min Yang ◽  
...  

2003 ◽  
Vol 23 (21) ◽  
pp. 7498-7509 ◽  
Author(s):  
Koichi Watashi ◽  
Makoto Hijikata ◽  
Ayako Tagawa ◽  
Takahiro Doi ◽  
Hiroyuki Marusawa ◽  
...  

ABSTRACT Hepatitis C virus (HCV) core protein (core) plays a significant role in the development of chronic liver diseases caused by HCV infection. We have discovered that the core sensitized all-trans-retinoic acid (ATRA)-induced cell death in MCF-7 cells. Activation of retinoic acid receptor alpha (RARα)-mediated transcription by the core was also seen in all the cell lines tested. By use of a yeast two-hybrid system, we identified Sp110b as a candidate for a core-interacting cellular factor. Although the function of Sp110b has remained unknown, we observed that Sp110b interacts with RARα and suppresses RARα-mediated transcription. These data suggest that Sp110b is a transcriptional cofactor negatively regulating RARα-mediated transcription. RNA interference-mediated reduction of endogenous Sp110b levels depressed the ability of the core to activate RARα-mediated transcription, suggesting an essential role for Sp110b in this pathway. The normal nuclear subcellular localization of Sp110b was altered by molecular interaction with the core to the cytoplasmic surface of the endoplasmic reticulum. This evidence suggests a model in which the core sequesters Sp110b from the nucleus and inactivates its corepressor function to activate RARα-mediated transcription. These findings likely describe a novel system in which a cytoplasmic viral protein regulates host cell transcription.


2008 ◽  
Vol 22 (4) ◽  
pp. 1050-1061 ◽  
Author(s):  
Ryo Kamata ◽  
Fujio Shiraishi ◽  
Jun-ichi Nishikawa ◽  
Junzo Yonemoto ◽  
Hiroaki Shiraishi

2015 ◽  
Vol 25 (9) ◽  
pp. 1998-2001 ◽  
Author(s):  
Ken-ichi Nakashima ◽  
Toshiyuki Tanaka ◽  
Hiroko Murata ◽  
Kouichi Kaburagi ◽  
Makoto Inoue

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