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. 2021 Feb 15;10(2):153. doi: 10.3390/biology10020153

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© 2021 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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Effect of BZ and CFZ on ER stress-associated proteins in B16-F1 cells. (A–C) Cells were treated with vehicle or various concentrations of BZ or CFZ for 24 h (A), or with vehicle or 100 nM BZ or CFZ for the indicated times in 2% FBS/DMEM (B,C). Cell lysates were analyzed by Western blotting with antibodies against ER stress-associated proteins (GRP94, GRP78, p90 ATF6α, ATF4, XBP1, CHOP, p-eIF2α, and eIF2α) and β-actin. The band densities were normalized against β-actin (n = 6 for total replicates) and the fold changes compared to that of vehicle-treated control (0 nM in A, −/− at 4 h in B) or that of early time point (2 h in C) are written under each band.

Effect of BZ and CFZ on ER stress-associated proteins in B16-F1 cells. (A–C) Cells were treated with vehicle or various concentrations of BZ or CFZ for 24 h (A), or with vehicle or 100 nM BZ or CFZ for the indicated times in 2% FBS/DMEM (B,C). Cell lysates were analyzed by Western blotting with antibodies against ER stress-associated proteins (GRP94, GRP78, p90 ATF6α, ATF4, XBP1, CHOP, p-eIF2α, and eIF2α) and β-actin. The band densities were normalized against β-actin (n = 6 for total replicates) and the fold changes compared to that of vehicle-treated control (0 nM in A, −/− at 4 h in B) or that of early time point (2 h in C) are written under each band.