scholarly journals Heat shock protein 47 stress responses in Chinese hamster ovary cells exposed to raw and reclaimed wastewater

2012 ◽  
Vol 14 (2) ◽  
pp. 492-498 ◽  
Author(s):  
Mokhtar Guizani ◽  
Yosuke Nogoshi ◽  
Fahmi Ben Fredj ◽  
Junkyu Han ◽  
Hiroko Isoda ◽  
...  
2016 ◽  
Vol 74 (10) ◽  
pp. 2407-2416 ◽  
Author(s):  
Selma Etteieb ◽  
Atsushi Kawachi ◽  
Junkyu Han ◽  
Foued Elayni ◽  
Jamila Tarhouni ◽  
...  

Combining bioassays and analytical chemistry screening is a powerful approach to assess organic micropollutants which are the main contributors to toxic potential in complex mixtures of treated wastewater (TWW). The aim of this study was to perform a comprehensive toxicity assessment of treated effluents using stress response bioassays and then to assess the occurrence of the organic micropollutants which were responsible for this biological response using gas chromatography coupled with a mass spectrometry detector (GC/MS). Results showed that TWW samples induced significant stress response on Chinese hamster ovary cells, stably transfected with heat shock protein 47 promoter, at 0.1%, 1%, 5% and 10% concentrations. The organic chemical compounds responsible for stress response potential were identified at different percentage values using non-target chemical screening. Of the compounds detected in TWW1 and TWW4, 55.09% and 74.5% respectively, fell within the class of aliphatic hydrocarbons. Aliphatic hydrocarbons were also present in TWW3 at 26.46% whereas 11.96% corresponded to 6-acetyl-1,1,2,4,4,7-hexamethyltetralin and 16.08% to triethoxysilane. Moreover, 76.73% of TWW2 was recorded as decamethylcyclopentasiloxane (D5) and 17.44% as n-hexadecanoic acid.


1983 ◽  
Vol 97 (5) ◽  
pp. 1389-1395 ◽  
Author(s):  
J R Subjeck ◽  
T Shyy ◽  
J Shen ◽  
R J Johnson

A rabbit antiserum has been prepared using as antigen the 110,000-dalton mammalian heat-shock protein. This protein was purified for injection by two-dimensional PAGE of heat-shocked Chinese hamster ovary cells. Characterization by immunoautoradiography and immunoprecipitation reveals that the antiserum is specific for the 110,000-dalton protein. Both techniques also reveal that the protein against which the antiserum is directed is induced by heat shock. Indirect immunofluorescence shows that the antigen is primarily localized at or near the nucleolus in cultured cells and numerous murine tissues. Treatment of cultured cells with deoxyribonuclease destroys the organization of staining within the nucleus while ribonuclease appears to completely release the antigen from the nucleus. A binding of the antiserum to cytoplasmic structures is also observed by immunofluorescence. This association with nucleoli may have implications in the regulatory aspects of the heat-shock response.


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