Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress

Suyama, Kaori; Watanabe, Masahiko; Sakabe, Kou; Okada, Yoshinori; Matsuyama, Daisuke; Kuroiwa, Masahiro; Mochida, Joji

doi:10.1016/j.neulet.2011.09.045

Cited by 41 publications

(37 citation statements)

References 18 publications

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“…This view was already partially confirmed (53). Furthermore, this notion is consistent with the observations that apoptosis can also be induced in HeLa cells by an inhibitor of CaM (70) and that BIP overexpression can protect cells from ER stressassociated cell death (71). This concept was further strengthened by the observations that the BiP co-chaperones ERj3 and ERj6 support BiP in Sec61 channel closure (Figs.…”

Section: Bip Co-chaperones Erj3 and Erj6 Support Bip-mediatedsupporting

confidence: 84%

Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

Schorr

Klein

Gamayun

et al. 2015

Journal of Biological Chemistry

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Background:The molecular chaperone immunoglobulin heavy-chain-binding protein (BiP) modulates gating of the polypeptide-conducting and calcium-permeable channel (Sec61 complex) in the membrane of the endoplasmic reticulum (ER). Results: Two co-chaperones, ERj3 and ERj6, support BiP in preventing ER calcium leakage via Sec61 complex. Conclusion: ERj3 and ERj6 facilitate Sec61 channel closing. Significance: Different co-chaperones assist BiP in Sec61 channel gating.

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Section: Bip Co-chaperones Erj3 and Erj6 Support Bip-mediatedsupporting

confidence: 84%

Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

Schorr

Klein

Gamayun

et al. 2015

Journal of Biological Chemistry

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“…Bip assists in the folding of newly synthesized proteins and prevents aggregation of unfolded proteins. Previous studies have demonstrated that overexpression of Bip protects cells against extracellular cytotoxic factors and restores cell homeostasis, thus contributing to cell survival following trauma (Suyama et al, 2011). In addition, melatonin treatment also inhibited ER stress through three UPR pathways (PERK, IRE1, and ATF6) by decreasing the expression of p-PERK, p-eIF2α, p-IRE1, spliced XBP-1 and ATF6.…”

Section: Discussionmentioning

confidence: 89%

Melatonin suppresses methamphetamine-triggered endoplasmic reticulum stress in C6 cells glioma cell lines

et al. 2017

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-Methamphetamine (METH) is a neurotoxic drug that causes brain damage by inducing neuronal and glial cell death together with glial cell hyperactivity-mediated progressive neurodegeneration. Previous studies have shown that METH induced glial cell hyperactivity and death via oxidative stress, the inflammatory response, and endoplasmic reticulum stress (ER stress) mechanisms, and melatonin could reverse these effects. However, the exact mechanism of the protective role of melatonin in METH-mediated ER stress has not been understood. This study investigated the protective effect of melatonin against METH toxicity-mediated ER stress in glial cells. Our study demonstrated that METH increased glial cell toxicity related to METH-induced ER stress by stimulating the unfolded protein response (UPR) to activate the expression of ER stress transducers, including phosphorylated doublestranded RNA-activated protein kinase (PKR)-like ER kinase (p-PERK), activating transcription factor (ATF6), and phosphorylated inositol-requiring enzyme 1 (p-IRE1). Moreover, the expression of binding immunoglobulin protein (Bip), CCAAT/enhancer-binding protein homologous protein (CHOP), caspase-12, phosphorylated eukaryotic translation initiation factor 2 alpha (p-eIF2α) and spliced X-box-binding protein-1 (XBP-1) mRNA were also increased. Melatonin reduced ER stress induced by METH toxicity by reducing the expression of ER stress response genes and proteins in a concentration-dependent manner. In addition, melatonin promoted the expression of Bip chaperone in a concentration-dependent manner. Taken together, our findings suggest that melatonin can protect against ER stress-induced glial cell death induced by METH.

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“…1,4 Recently, there has been growing interest in protein-modification disorders related to endoplasmic reticulum (ER) stress during delayed neuronal cell death in various central nervous system conditions, such as cerebral ischemia, Alzheimer's disease, Parkinson's disease, brain injury and SCI. [5][6][7] ER stress causes protein-modification blockage, which spurs the accumulation of abnormal proteins. This accumulation in turn induces the expression of glucose-regulated protein 78 (GRP78), which hydrolyses ATP to promote protein folding.…”

Section: Introductionmentioning

confidence: 99%

“…8 Since the accumulation of unfolded proteins leads to apoptosis, the enhancement of GRP78 is a possible strategy to inhibit apoptotic cell death following neurotrauma and neurodegenerative disease. 5,9,10 Excessive accumulation of abnormal proteins leads to the expression of C/EBP homologous transcription factor protein (CHOP), which is a prominent proapoptotoc protein of the ER stress response. 11,12 Understanding of the precise mechanism of ER stressmediated apoptosis in SCI may lead to the development of novel treatment strategies.…”

Section: Introductionmentioning

confidence: 99%

Endoplasmic reticulum stress response in the rat contusive spinal cord injury model-susceptibility in specific cell types

et al. 2013

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Study design: Focus group study Objective: To investigate cell-specific endoplasmic reticulum (ER) stress reactions in contusive spinal cord by evaluating the expression of the glucose-regulated protein 78 (GRP78) and C/EBP homologous transcription factor protein (CHOP) using immunohistochemical staining. Setting: Data were analysed at Tokai University School of Medicine in Japan. Methods: The authors generated rat spinal cord injury (SCI) models using an IH-Impactor (100 kdyne(LI), 200 kdyne (HI)). Rats were killed at 1, 3, 5, 7 and 14 days post operation (dpo). Spinal cord sections were prepared and the expression ratio of GRP78 and CHOP was evaluated in oligodendrocyte precursor cells (OPCs) (NG2 þ ), oligodendrocytes (OLs) (APC þ ), neurons (NeuN þ ) and astrocytes (GFAP þ ) using double immunohistochemical staining. We examined an area 8 mm distal from SCI-epicenter. Results: Compared with the sham group, both injured groups had higher GRP78 expression ratio in contused spinal cord at 1 dpo. GRP78 expression ratio was highest in GFAP þ cells of both groups, and lowest in NG2 þ cells. Although GRP78 was expressed strongly immediately after SCI in the both groups, increased CHOP expression was observed only in the HI group. The CHOP expression in NG2 þ cells was significantly higher than that observed in GFAP þ cells at 5 dpo. Conclusion: Although the ER stress response contributes to cell survival in the low-stress SCI conditions, the ER stress response induces an apoptotic cascade in high-stress SCI conditions. The ER response varies according to cell type, with the highest observed in astrocytes, and the lowest observed in oligodendrocyte precursor cells.

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Overexpression of GRP78 protects glial cells from endoplasmic reticulum stress

Cited by 41 publications

References 18 publications

Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

Co-chaperone Specificity in Gating of the Polypeptide Conducting Channel in the Membrane of the Human Endoplasmic Reticulum

Melatonin suppresses methamphetamine-triggered endoplasmic reticulum stress in C6 cells glioma cell lines

Endoplasmic reticulum stress response in the rat contusive spinal cord injury model-susceptibility in specific cell types

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