Browse > Article
http://dx.doi.org/10.5352/JLS.2016.26.4.490

Brefeldin A-induced Endoplasmic Reticulum Stress Leads to Different CHOP Expression in Primary Astrocyte Cells and C6 Glioma Cells  

Park, Eun Jung (Department of Immunology, School of Medicine, Keimyung University)
Kwon, Taeg Kyu (Department of Immunology, School of Medicine, Keimyung University)
Publication Information
Journal of Life Science / v.26, no.4, 2016 , pp. 490-495 More about this Journal
Abstract
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.
Keywords
Astocyte cells; Brefeldin A; C6 glioma cells; CHOP; proteasome;
Citations & Related Records
연도 인용수 순위
  • Reference
1 Boya, P., Cohen, I., Zamzami, N., Vieira, H. L. and Kroemer, G. 2002. Endoplasmic reticulum stress-induced cell death requires mitochondrial membrane permeabilization. Cell Death Differ. 9, 465-467.   DOI
2 Bruhat, A., Jousse, C., Wang, X. Z., Ron, D., Ferrara, M. and Fafournoux, P. 1997. Amino acid limitation induces expression of CHOP, a CCAAT/enhancer binding protein-related gene, at both transcriptional and post-transcriptional levels. J. Biol. Chem. 272, 17588-17593.   DOI
3 Carew, J. S., Nawrocki, S. T., Krupnik, Y. V., Dunner, K., McConkey, D. J. and Keating, M. J. 2006. Targeting endoplasmic reticulum protein transport: a novel strategy to kill malignant B cells and overcome fludarabine resistance in CLL. Blood 107, 222-231.   DOI
4 Donaldson, G., Cassel, D., Kahn, R. A. and Klausner, R. D. 1992. ADP-ribosylation factor, a small GTP-binding protein, is required for binding of the coatomer protein beta-COP to Golgi membranes. Proc. Natl. Acad. Sci. USA 89, 6408-6412.   DOI
5 Giulian, D. and Baker, T. J. 1986. Characterization of ameboid microglia isolated from developing mammalian brain. J. Neurosci. 6, 2163-2178.   DOI
6 Guo, H., Tittle, T. V., Allen, H. and Marziarz, R. T. 1998. Brefeldin A-mediated apoptosis requires the activation of caspases and is inhibited by Bcl-2. Exp. Cell Res. 245, 57-68.   DOI
7 Jeong, K., Kim, H., Kim, K., Kim, S. J., Hahn, B. S., Jahng, G. H., Yoon, K. S., Kim, S. S., Ha, J., Kang, I. and Choe, W. 2014. Cyclophilin B is involved in p300-mediated degradation of CHOP in tumor cell adaptation to hypoxia. Cell Death Differ. 21, 438-450.   DOI
8 Kapoor, A. and Sanyal, A. J. 2009. Endoplasmic reticulum stress and the unfolded protein response. Clin. Liver Dis. 13, 581-590.   DOI
9 Kaufman, R. J. 1999. Stress signaling from the lumen of the endoplasmic reticulum: coordination of gene transcriptional and translational controls. Genes Dev. 13,1211-1233.   DOI
10 Kaufman, R. J., Scheuner, D., Schroder, M., Shen, X., Lee, K., Liu, C. Y. and Arnold, S. M. 2002. The unfolded protein response in nutrient sensing and differentiation. Nat. Rev. Mol. Cell. Biol. 3,411-421.   DOI
11 Klausner, R. D., Donaldson, J. G. and Lippincott-Schwartz, J. 1992. Brefeldin A: insights into the control of membrane traffic and organelle structure. J. Cell. Biol. 116, 1071-1080   DOI
12 Lai, E., Teodoro, T. and Volchuk, A. 2007. Endoplasmic reticulum stress: signaling the unfolded protein response. Physiology 22, 193-201.   DOI
13 McCullough, K. D., Martindale, J. L., Klotz, L. O., Aw, T. Y. and Holbrook, N. J. 2001. Gadd153 sensitizes cells to endoplasmic reticulum stress by down-regulating Bcl2 and perturbing the cellular redox state. Mol. Cell. Biol. 21, 1249-1259.   DOI
14 Mori, K. 2000. Tripartitie management of unfolded proteins in the endoplasmic reticulum. Cell 101, 451-454.   DOI
15 Oyadomari, S., Araki, E. and Mori, M. 2002. Endoplasmic reticulum stress mediated apoptosis in pancreatic β-cell. Apoptosis 7, 335-345.   DOI
16 Sitia, R. and Braakman, I. 2003. Quality control in the endoplasmic reticulum protein factory. Nature 426, 891-894.   DOI
17 Oyadomari, S. and Mori, M. 2004. Roles of CHOP/GADD153 in endoplasmic reticulum stress. Cell Death Differ. 11, 381-389.   DOI
18 Oydomari, S., Takeda, K., Takiguchi, M., Gotoh, T., Matsumoto, M., Wada, I., Akira, S., Araki, E. and Mori, M. 2001. Nitric oxide-induced apoptosis in pancreatic β cells is mediated by the endoplasmic reticulum stress pathway. Proc. Natl. Acad. Sci. USA 98,10845-10850.   DOI
19 Qi, Y. and Xia, P. 2012. Cellular inhibitor of apoptosis protein-1 (cIAP1) plays a critical role in β-cell survival under endoplasmic reticulum stress: promoting ubiquitination and degradation of C/EBP homologous protein (CHOP). J. Biol. Chem. 287, 32236-32245.   DOI
20 Tamura, G., Ando, K., Suzuki, S., Takatsuki, A. and Arima, K. 1968. Antiviral activity of brefeldin A and verrucarin A. J. Antibiot. 21, 160-161.   DOI
21 Ubeda, M., Schmitt-Ney, M., Ferrer, J. and Habener, J. F. 1999. CHOP/GADD153 and methionyl-tRNA synthetase (MetRS) genes overlap in a conserved region that controls mRNA stability. Biochem. Biophys. Res. Commun. 262, 31-38.   DOI
22 Wallen, E., Sellers, R. G. and Peehl, D. M. 2000. Brefeldin A induces p53-independent apoptosis in primary cultures of human prostatic cancer cells. Urology 164, 836-841.   DOI
23 Wang, X. Z., Harding, H. P., Zhang, Y., Jolicoeur, E. M., Kuroda, M. and Ron, D. 1998. Cloning of mammalian Ire1reveals diversity in the ER stress response. EMBO J. 19, 5708-5717.
24 Zinszner, H., Kuroda, M., Wang, X., Batchvarova, N., Lightfoot, R. T., Remotti, H., Stevens, J. L. and Ron, D. 1998. CHOP is implicated in programmed cell death in response to impaired function of the endoplasmic reticulum. Genes Dev. 12, 982-995.   DOI
25 Yoshida, H., Okada, T., Haze, K., Yanagi, H., Yura, T., Negishi, M. and Mori, K. 2000. ATF6 activated by proteolysis binds in the presence of NF-Y (CBF) directly to the cis-acting element responsible for the mammalian unfolded protein response. Mol. Cell. Biol. 20, 6755-6767.   DOI