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KMID : 0613820160260040490
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Journal of Life Science
2016 Volume.26 No. 4 p.490 ~ p.495
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Brefeldin A-induced Endoplasmic Reticulum Stress Leads to Different CHOP Expression in Primary Astrocyte Cells and C6 Glioma Cells
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Park Eun-Jung
Kwon Taeg-Kyu
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Abstract
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Brefeldin A (BFA), a lactone antibiotic isolated from the fungus Eupenicillium brefeldianum, inhibits the transport of secreted and membrane proteins from the endoplasmic reticulum (ER) to the Golgi apparatus. BFA disrupts Golgi function, the accumulation of unfolded proteins in ER, and the induction of ER stress. Prolonged ER stress induces apoptosis at least in part through the transcription factor C/EBP (CCAAT/enhancer binding protein) homologous protein (CHOP),which is activated by the unfolded protein response (UPR). In this paper, we demonstrate that BFA-induced endoplasmic reticulum stress leads to different CHOP expression in primary astrocyte cells and C6 glioma cells. BFA induced lower CHOP expression levels in primary astrocyte cells than in C6 glioma cells; however, other ER stress inducers (thapsigargin and tunicamycin) resulted in similar expression patterns in these two cell types. Interestingly, the three different ER stress inducers (BFA, thapsigargin, and tunicamycin) induced similar levels of CHOP mRNA expression in primary astrocyte cells. The ubiquitin-proteasome inhibitor MG132 also markedly up-regulated the BFA-mediated CHOP protein expression in primary astrocyte cells. BFA also induced higher proteasome activity in primary astrocyte cells than in C6 glioma cells. Taken together, our results suggest that higher proteasomal activity might down-regulate BFA-induced CHOP expression in primary astrocyte cells.
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KEYWORD
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Astocyte cells, Brefeldin A, C6 glioma cells, CHOP, proteasome
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