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. 2019 Sep 12;20(18):4528. doi: 10.3390/ijms20184528

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© 2019 by the authors.

Licensee MDPI, Basel, Switzerland. This article is an open access article distributed under the terms and conditions of the Creative Commons Attribution (CC BY) license (http://creativecommons.org/licenses/by/4.0/).

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(A) Effects of exogenous copper upon changes in the fibrinogen expression of HepG2 cells. After HepG2 cells had been treated with 0.5 and 100 μM copper, the intracellular localizations and level of fibrinogen (green) and nucleus (red) were examined by immunofluorescence microscopy. (B) Silence of ceruloplasmin (siCp) treatment induced the protein expression of fibrinogen, while the significant reduction in protein level for SOD was observed under siCp applications. β-actin was used as a loading control. Quantification of the result was presented as the bar diagram and the results represent the mean ± SD of three independent experiments (*** p < 0.0001; ** p < 0.001). (C) Levels of protein carbonylation. Significantly increased expression of carbonylated proteins were observed in the ceruloplasmin-silenced group (siCp) compared to the control (Mock). β-actin performed by Western blot analysis was utilized as the loading control and the individual carbonylated proteins separated by 2-DE analysis then could be normalized to the intensity of the β-actin protein for determining the protein oxidation levels.

(A) Effects of exogenous copper upon changes in the fibrinogen expression of HepG2 cells. After HepG2 cells had been treated with 0.5 and 100 μM copper, the intracellular localizations and level of fibrinogen (green) and nucleus (red) were examined by immunofluorescence microscopy. (B) Silence of ceruloplasmin (siCp) treatment induced the protein expression of fibrinogen, while the significant reduction in protein level for SOD was observed under siCp applications. β-actin was used as a loading control. Quantification of the result was presented as the bar diagram and the results represent the mean ± SD of three independent experiments (*** p < 0.0001; ** p < 0.001). (C) Levels of protein carbonylation. Significantly increased expression of carbonylated proteins were observed in the ceruloplasmin-silenced group (siCp) compared to the control (Mock). β-actin performed by Western blot analysis was utilized as the loading control and the individual carbonylated proteins separated by 2-DE analysis then could be normalized to the intensity of the β-actin protein for determining the protein oxidation levels.