PMID-sentid Pub_year Sent_text comp_official_name comp_offsetprotein_name organism prot_offset 19411306-13 2009 It appears that knockdown of ERp57 confers cellular protection against hyperoxia- or tunicamycin-induced apoptosis by inhibition of caspase-3 activation and stimulation of BiP/GRP78 induction. Tunicamycin 85-96 heat shock protein family A (Hsp70) member 5 Homo sapiens 172-175 19411306-13 2009 It appears that knockdown of ERp57 confers cellular protection against hyperoxia- or tunicamycin-induced apoptosis by inhibition of caspase-3 activation and stimulation of BiP/GRP78 induction. Tunicamycin 85-96 heat shock protein family A (Hsp70) member 5 Homo sapiens 176-181 18395193-2 2008 We evaluated the effect of a selective inducer of immunoglobulin heavy chain binding protein (BiP) (BiP inducer X; BIX) against both tunicamycin-induced cell death (in SH-SY5Y cells) and the effects of global transient forebrain ischemia (in gerbils). Tunicamycin 133-144 heat shock protein family A (Hsp70) member 5 Homo sapiens 50-92 19302790-3 2009 X-box protein-1 (XBP-1) splicing, GRP78 expression and caspase-12 activation were increased by tunicamycin or IR in Atm-deficient AT5BIVA fibroblasts. Tunicamycin 95-106 heat shock protein family A (Hsp70) member 5 Homo sapiens 34-39 18395193-2 2008 We evaluated the effect of a selective inducer of immunoglobulin heavy chain binding protein (BiP) (BiP inducer X; BIX) against both tunicamycin-induced cell death (in SH-SY5Y cells) and the effects of global transient forebrain ischemia (in gerbils). Tunicamycin 133-144 heat shock protein family A (Hsp70) member 5 Homo sapiens 94-97 18228003-7 2008 Tunicamycin induced a rapid decline of cyclin D1 and cyclin A expression and an early increase of glucose-related protein (GRP) 78 and growth arrest and DNA damage-inducible transcription factor (GADD) 153 levels. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 98-130 18228003-11 2008 The knockdown of GRP78 expression by the siRNA transfection technique moderately increased tunicamycin-induced apoptosis but not the antiproliferative effect by sulforhodamine B assay. Tunicamycin 91-102 heat shock protein family A (Hsp70) member 5 Homo sapiens 17-22 17941056-7 2008 Using SH-SY5Y neuroblastoma cells and primary cerebellar granule neurons as in vitro models, we demonstrated that exposure to ethanol alone had little effect on the expression of markers for ER stress; however, ethanol drastically enhanced the expression of GRP78, CHOP, ATF4, ATF6, and phosphorylated PERK and eIF2 alpha when induced by tunicamycin and thapsigargin. Tunicamycin 338-349 heat shock protein family A (Hsp70) member 5 Homo sapiens 258-263 18029041-2 2008 A time-dependent induction of ER chaperons, glucose regulated protein (GRP)78 and GRP94, was observed after treatment with tunicamycin (TM), and cell death was also induced concomitantly in both cells. Tunicamycin 123-134 heat shock protein family A (Hsp70) member 5 Homo sapiens 71-77 18022401-8 2007 We investigated the effect of exogenous UPR inducers thapsigargin (Tg) and tunicamycin (Tu) on Grp78 and ATF6 expression. Tunicamycin 75-86 heat shock protein family A (Hsp70) member 5 Homo sapiens 95-100 18022401-8 2007 We investigated the effect of exogenous UPR inducers thapsigargin (Tg) and tunicamycin (Tu) on Grp78 and ATF6 expression. Tunicamycin 88-90 heat shock protein family A (Hsp70) member 5 Homo sapiens 95-100 16987996-4 2007 Pharmacological methods such as proteasome inhibition and treatment with brefeldin A and tunicamycin were used to induce ER stress and activate the UPR as monitored by increased levels of spliced XBP1 and BiP mRNA. Tunicamycin 89-100 heat shock protein family A (Hsp70) member 5 Homo sapiens 205-208 17942905-7 2007 Inhibition of MEK/ERK also resulted in down-regulation of GRP78, which was physically associated with caspase-4, before and after treatment with tunicamycin or thapsigargin. Tunicamycin 145-156 heat shock protein family A (Hsp70) member 5 Homo sapiens 58-63 17681378-9 2007 Tunicamycin treatment resulted in upregulation of GRP78/BiP in the neuronal cells. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 50-55 17681378-9 2007 Tunicamycin treatment resulted in upregulation of GRP78/BiP in the neuronal cells. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 56-59 15572843-9 2004 The tunicamycin-induced up-regulation of GRP78 and GRP94 and phosphorylation of PERK was suppressed by treatment with 4-PBA, indicating that 4-PBA suppresses ER stress responses by decreasing unfolded protein. Tunicamycin 4-15 heat shock protein family A (Hsp70) member 5 Homo sapiens 41-46 16316999-10 2006 Induction of the endoplasmic reticulum stress response by anoxia/recovery or tunicamycin (monitored by induction of Bip or Grp94 expression, phosphorylation of eukaryotic translation initiation factor 2alpha subunit, expression of CHOP, and activation of caspase-12) was attenuated in cells that overexpress SLK. Tunicamycin 77-88 heat shock protein family A (Hsp70) member 5 Homo sapiens 116-119 15760841-5 2005 Sp proteins are constitutively bound to the ERSE; however, activation of GRP78 protein (or reporter gene) by thapsigargin or tunicamycin is inhibited after cotransfection with small inhibitory RNAs for Sp1, Sp3, and Sp4. Tunicamycin 125-136 heat shock protein family A (Hsp70) member 5 Homo sapiens 73-78 16271832-11 2006 Indeed, tunicamycin, known to inhibit N-linked glycosylation in the ER, was found to induce a similar inverse correlation between GRP78 overexpression and HSP72/73 under-expression. Tunicamycin 8-19 heat shock protein family A (Hsp70) member 5 Homo sapiens 130-135 10760948-3 2000 This article characterizes the different biological features associated with GRP78 induction by two kinds of stress agents, calcium ionophore, ionomycin (IM), and glycosylation inhibitor, tunicamycin (TM), focusing on the association with apoptosis in human prostate cancer cells. Tunicamycin 188-199 heat shock protein family A (Hsp70) member 5 Homo sapiens 77-82 10799532-2 2000 In fact, the glycosylation inhibitor tunicamycin induces dephosphorylation of mammalian BiP. Tunicamycin 37-48 heat shock protein family A (Hsp70) member 5 Homo sapiens 88-91 15648788-3 2004 Expression of GRP78 at both protein and mRNA levels was markedly increased in cardiomyocytes pretreated with tunicamycin, when compared to non-treatment controls. Tunicamycin 109-120 heat shock protein family A (Hsp70) member 5 Homo sapiens 14-19 10760948-3 2000 This article characterizes the different biological features associated with GRP78 induction by two kinds of stress agents, calcium ionophore, ionomycin (IM), and glycosylation inhibitor, tunicamycin (TM), focusing on the association with apoptosis in human prostate cancer cells. Tunicamycin 201-203 heat shock protein family A (Hsp70) member 5 Homo sapiens 77-82 9409741-5 1997 The grp78-K8/18 association is induced by culturing cells in the presence of tunicamycin or after glucose starvation. Tunicamycin 77-88 heat shock protein family A (Hsp70) member 5 Homo sapiens 4-9 9755171-7 1998 Over-expression of a dominant-negative form of Ire1 blocks the induction of GRP78/BiP and CHOP in response to the ER stress induced by tunicamycin treatment. Tunicamycin 135-146 heat shock protein family A (Hsp70) member 5 Homo sapiens 76-81 9755171-7 1998 Over-expression of a dominant-negative form of Ire1 blocks the induction of GRP78/BiP and CHOP in response to the ER stress induced by tunicamycin treatment. Tunicamycin 135-146 heat shock protein family A (Hsp70) member 5 Homo sapiens 82-85 9388233-6 1997 The latter results were obtained also when BiP was overexpressed not via transfection but as a response to ER stress by tunicamycin. Tunicamycin 120-131 heat shock protein family A (Hsp70) member 5 Homo sapiens 43-46 10424404-6 1999 Interestingly, while the majority of the breast cancer cell lines can respond to tunicamycin- and thapsigargin-induced stress by increasing the steady state levels of grp94 and grp78 transcripts, the induction at the GRP protein level is variable and does not always correspond with the transcript level. Tunicamycin 81-92 heat shock protein family A (Hsp70) member 5 Homo sapiens 177-182 1506413-2 1992 Expression of the glucose regulated proteins (GRP78 and GRP94) is greatly increased after cells are exposed to stress agents (including A23187 and tunicamycin) which inhibit ER function. Tunicamycin 147-158 heat shock protein family A (Hsp70) member 5 Homo sapiens 46-51 8818631-8 1996 Exposure of cell monolayers to tunicamycin, an inhibitor of protein glycosylation, mimicked the effect of NO2 exposure on expression of GRP-78. Tunicamycin 31-42 heat shock protein family A (Hsp70) member 5 Homo sapiens 136-142 8188375-7 1994 The effects on grp78 expression of heat shock and tunicamycin treatment, the latter of which specifically stimulates mammalian grp78, were investigated. Tunicamycin 50-61 heat shock protein family A (Hsp70) member 5 Homo sapiens 15-20 8188375-8 1994 While the level of the grp78 protein remained constant under all circumstances, grp78 mRNA was unaffected by heat shock but induced fivefold by tunicamycin. Tunicamycin 144-155 heat shock protein family A (Hsp70) member 5 Homo sapiens 80-85 8454000-3 1993 Treatment of the cells with tunicamycin caused a rapid decrease in GRP78 phosphorylation within 2 to 4 h in both cell types prior to GRP78 induction. Tunicamycin 28-39 heat shock protein family A (Hsp70) member 5 Homo sapiens 67-72 8454000-3 1993 Treatment of the cells with tunicamycin caused a rapid decrease in GRP78 phosphorylation within 2 to 4 h in both cell types prior to GRP78 induction. Tunicamycin 28-39 heat shock protein family A (Hsp70) member 5 Homo sapiens 133-138 8454000-4 1993 Following a longer period of tunicamycin treatment, GRP78 phosphorylation recovered gradually in parallel with the accumulation of newly synthesized GRP78. Tunicamycin 29-40 heat shock protein family A (Hsp70) member 5 Homo sapiens 52-57 8454000-4 1993 Following a longer period of tunicamycin treatment, GRP78 phosphorylation recovered gradually in parallel with the accumulation of newly synthesized GRP78. Tunicamycin 29-40 heat shock protein family A (Hsp70) member 5 Homo sapiens 149-154 8454000-5 1993 The half-life of GRP78 was over 24 h and similar in both normal and transformed cells either with or without tunicamycin treatment. Tunicamycin 109-120 heat shock protein family A (Hsp70) member 5 Homo sapiens 17-22 8454000-6 1993 In contrast, the half-life of phosphate groups incorporated into GRP78 was about 120 min in both types of cells in the absence of tunicamycin treatment. Tunicamycin 130-141 heat shock protein family A (Hsp70) member 5 Homo sapiens 65-70 8972186-7 1997 The Y-box proteins can repress the inducibility of the grp78 core element mediated by treatment of cells with A23187, thapsigargin, and tunicamycin. Tunicamycin 136-147 heat shock protein family A (Hsp70) member 5 Homo sapiens 55-60 1506413-6 1992 The increased accumulation of GRP78 mRNA after exposure of cells to either thapsigargin, brefeldin A, AIF4-, A23187, or tunicamycin can be blocked by pre-incubation in cycloheximide. Tunicamycin 120-131 heat shock protein family A (Hsp70) member 5 Homo sapiens 30-35 1344885-5 1992 When newly synthesized storage glycoproteins phaseolin, phytohemagglutinin or alpha-amylase inhibitor were immunoprecipitated from an ER preparation of tunicamycin-treated tissue, the GRP78 homolog was always co-precipitated. Tunicamycin 152-163 heat shock protein family A (Hsp70) member 5 Homo sapiens 184-189 34973349-9 2022 In SIRT4-silenced cells, when treated with 2.5 mug/ml Tunicamycin for 16 hours, the increase in the expressions of ATF6, GRP78 and the ratio of spliced/unspliced XBP1 mRNA were reduced. Tunicamycin 54-65 heat shock protein family A (Hsp70) member 5 Homo sapiens 121-126 33235302-8 2020 ALA pre-treatment significantly reduced the expression of ER stress markers namely, GRP78, XBP1, sXBP1 and ATF4 in response to tunicamycin. Tunicamycin 127-138 heat shock protein family A (Hsp70) member 5 Homo sapiens 84-89 34775235-4 2022 Pre-treatment with DA-9805 (1 mug/ml) attenuated upregulation of glucose-regulated protein 78 (GRP78), C/EBP homologous protein (CHOP) and cleaved caspase-3 in SH-SY5Y neuroblastoma cells treated with thapsigargin (1 microg/ml) or tunicamycin (2 microg/ml). Tunicamycin 231-242 heat shock protein family A (Hsp70) member 5 Homo sapiens 65-93 34775235-4 2022 Pre-treatment with DA-9805 (1 mug/ml) attenuated upregulation of glucose-regulated protein 78 (GRP78), C/EBP homologous protein (CHOP) and cleaved caspase-3 in SH-SY5Y neuroblastoma cells treated with thapsigargin (1 microg/ml) or tunicamycin (2 microg/ml). Tunicamycin 231-242 heat shock protein family A (Hsp70) member 5 Homo sapiens 95-100 35603939-11 2022 In HCT116 cells, tunicamycin increased the expression of Grp78, Gro-alpha and IL-8 in a concentration-dependent manner. Tunicamycin 17-28 heat shock protein family A (Hsp70) member 5 Homo sapiens 57-62 34604209-4 2021 In the current study, we demonstrated that tunicamycin (a novel ERS inducer) can induce the apoptosis of HSCs and increase the concentration of intracellular Ca2+ and the expression of ERS protein GRP78, apoptosis protein caspase-12, and Bax, while it can decrease the antiapoptosis protein expression of Bcl-2. Tunicamycin 43-54 heat shock protein family A (Hsp70) member 5 Homo sapiens 197-202 34079010-6 2021 Hence, although levels of spliced XBP1 and CHOP mRNA and ATF4 protein increase with Ipom-F, the accompanying increase in the levels of ER lumenal BiP and GRP94 seen with tunicamycin are not observed. Tunicamycin 170-181 heat shock protein family A (Hsp70) member 5 Homo sapiens 146-149 35233582-0 2022 The role of GRP78 in oxidative stress induced by tunicamycin in trabecular meshwork cells. Tunicamycin 49-60 heat shock protein family A (Hsp70) member 5 Homo sapiens 12-17 35233582-1 2022 OBJECTIVE: To clarify the regulatory effect of GRP-78 induced by tunicamycin on endoplasmic reticulum (ER) stress. Tunicamycin 65-76 heat shock protein family A (Hsp70) member 5 Homo sapiens 47-53 35233582-6 2022 Tunicamycin can also increase expression levels of GRP78,VDAC1, ATF4, PERK, eIF2a, and CHOP (p<0.01). Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 51-56 35233582-10 2022 CONCLUSION: Tunicamycin induces oxidative stress in trabecular meshwork cells, and the increase in GRP78 expression can protect the cells during ER stress by regulating eIF2. Tunicamycin 12-23 heat shock protein family A (Hsp70) member 5 Homo sapiens 99-104 35165522-8 2022 Moreover in vitro experiments, ER stress induced by tunicamycin (TM) not only significantly increased the expression of GRP78 and CHOP, but also caused the epithelial to myofibroblast transformation (EMT) of renal tubular epithelial cells, evidenced by decreased expression of E-cadherin and increased expression of vimentin, and extracellular matrix (ECM) deposition, evidenced by increased expression of fibronectin (FN). Tunicamycin 52-63 heat shock protein family A (Hsp70) member 5 Homo sapiens 120-125 32608212-7 2020 In addition, H2O2 and TM could increase the levels of PGE2, GRP78, CHOP, caspase-12, and reactive oxygen species (ROS), resulting in the degeneration of CHs. Tunicamycin 22-24 heat shock protein family A (Hsp70) member 5 Homo sapiens 60-65 33014334-0 2020 Tunicamycin promotes metastasis through upregulating endoplasmic reticulum stress induced GRP78 expression in thyroid carcinoma. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 90-95 33014334-8 2020 In addition, tunicamycin-induced ER stress up-regulated the expression of GRP78, PERK and XBP1 as well as reversed the metastatic ability of GRP78 in ATC cells. Tunicamycin 13-24 heat shock protein family A (Hsp70) member 5 Homo sapiens 74-79 33014334-8 2020 In addition, tunicamycin-induced ER stress up-regulated the expression of GRP78, PERK and XBP1 as well as reversed the metastatic ability of GRP78 in ATC cells. Tunicamycin 13-24 heat shock protein family A (Hsp70) member 5 Homo sapiens 141-146 32592208-9 2020 Our study revealed that the tunicamycin-induced persistent UPR expression led to apoptosis of chondrocytes and activation of autophagy incorporation with GRP78. Tunicamycin 28-39 heat shock protein family A (Hsp70) member 5 Homo sapiens 154-159 32040528-4 2020 Treatment with two different ER stress inducers, thapsigargin (TG) and tunicamycin (TM), caused a dose-dependent induction of ER stress as evident from up-regulation of protein kinase RNA-like ER kinase (PERK), heat shock protein family A (Hsp70) member 5 (HSPA5), activating transcription factor (ATF4), ATF6, DNA damage inducible transcript 3 (DDIT3) and spliced X-box binding protein 1 (sXBP1) and impaired cell viability and decreased expression of vitamin D receptor (VDR) in MCF-7 cells (P < 0.05). Tunicamycin 71-82 heat shock protein family A (Hsp70) member 5 Homo sapiens 257-262 32031621-8 2020 Tunicamycin elicited time-dependent increase in GRP78 protein levels, direct interaction with latent TGF-beta1, and activated TGF-beta1 signaling. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 48-53 32086320-9 2020 GRP78 autoantigen expression was upregulated among human aortic endothelial cells (HAECs) stressed by incubation with tunicamycin (an unfolded protein response inducer) or exposure to culture media flow disturbances. Tunicamycin 118-129 heat shock protein family A (Hsp70) member 5 Homo sapiens 0-5 32040528-4 2020 Treatment with two different ER stress inducers, thapsigargin (TG) and tunicamycin (TM), caused a dose-dependent induction of ER stress as evident from up-regulation of protein kinase RNA-like ER kinase (PERK), heat shock protein family A (Hsp70) member 5 (HSPA5), activating transcription factor (ATF4), ATF6, DNA damage inducible transcript 3 (DDIT3) and spliced X-box binding protein 1 (sXBP1) and impaired cell viability and decreased expression of vitamin D receptor (VDR) in MCF-7 cells (P < 0.05). Tunicamycin 84-86 heat shock protein family A (Hsp70) member 5 Homo sapiens 257-262 32040528-5 2020 Treatment with 1,25D3 (100 nM) inhibited TG (10 nM)- and TM (1 mug/mL)-induced mRNA and/or protein levels of ATF4, ATF6, DDIT3 and HSPA5 in MCF-7 cells (P < 0.05). Tunicamycin 57-59 heat shock protein family A (Hsp70) member 5 Homo sapiens 131-136 31888113-6 2019 Simultaneously, induction of ER stress with tunicamycin resulted in an increased expression of Cyclooxygenase 2 (COX-2) and Glucose-regulated protein (GRP78) concomitant with the activation of p38 MAPK/PI3K/Akt in HepG2 cells. Tunicamycin 44-55 heat shock protein family A (Hsp70) member 5 Homo sapiens 151-156 31978676-7 2020 RESULTS: Induction of ER stress in TM treated groups were confirmed by significantly increased mRNA and protein levels of GRP78. Tunicamycin 35-37 heat shock protein family A (Hsp70) member 5 Homo sapiens 122-127 31243264-6 2019 We found that the interaction between GRP78 and SPARC increased during exposure to 5-FU, CPT-11, and tunicamycin, resulting in an attenuation of GRP78"s inhibition of apoptosis. Tunicamycin 101-112 heat shock protein family A (Hsp70) member 5 Homo sapiens 38-43 31243264-6 2019 We found that the interaction between GRP78 and SPARC increased during exposure to 5-FU, CPT-11, and tunicamycin, resulting in an attenuation of GRP78"s inhibition of apoptosis. Tunicamycin 101-112 heat shock protein family A (Hsp70) member 5 Homo sapiens 145-150 30784934-4 2019 Morin downregulated the expression of GRP78, central regulator of ER stress response, induced by ER stress inducer tunicamycin. Tunicamycin 115-126 heat shock protein family A (Hsp70) member 5 Homo sapiens 38-43 30770792-7 2019 BV6 consistently abolishes TM-stimulated accumulation of ER stress markers such as glucose-regulated protein 78 (GRP78) and C/EBP homologous protein (CHOP) and reduces protein kinase RNA-like ER kinase (PERK) phosphorylation and X box-binding protein 1 (XBP1) splicing upon TM treatment. Tunicamycin 27-29 heat shock protein family A (Hsp70) member 5 Homo sapiens 83-111 30893871-7 2019 Molecular modulation of endoplasmic reticulum (ER) stress induced by tunicamycin was studied by western blot analysis of the ER stress markers GRP78, CHOP and p-IRE1. Tunicamycin 69-80 heat shock protein family A (Hsp70) member 5 Homo sapiens 143-148 30820153-4 2019 The effect of tunicamycin on the expression of the unfolded protein response (UPR)-related proteins BiP and CHOP was assayed by western blotting with or without inhibition of Orai1. Tunicamycin 14-25 heat shock protein family A (Hsp70) member 5 Homo sapiens 100-103 30657961-6 2019 We found that ER stress marker GRP78 expression increased with CHOP and TRIB3 expression in normal endometrial stromal cells (NESCs) treated with tunicamycin, and this increase was accompanied by decreased AKT and mTOR activity and cellular invasiveness. Tunicamycin 146-157 heat shock protein family A (Hsp70) member 5 Homo sapiens 31-36 30770792-7 2019 BV6 consistently abolishes TM-stimulated accumulation of ER stress markers such as glucose-regulated protein 78 (GRP78) and C/EBP homologous protein (CHOP) and reduces protein kinase RNA-like ER kinase (PERK) phosphorylation and X box-binding protein 1 (XBP1) splicing upon TM treatment. Tunicamycin 27-29 heat shock protein family A (Hsp70) member 5 Homo sapiens 113-118 30567393-3 2018 Tunicamycin (TM) treatment significantly increased mRNA levels of CHOP and GRP78, and induced lipid accumulation in the liver. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 75-80 30567393-3 2018 Tunicamycin (TM) treatment significantly increased mRNA levels of CHOP and GRP78, and induced lipid accumulation in the liver. Tunicamycin 13-15 heat shock protein family A (Hsp70) member 5 Homo sapiens 75-80 30096296-7 2018 Moreover, 25-OCH3-PPD significantly inhibited glucose-regulated protein 78 (GRP78; the major ER stress marker) expression in TM-induced ER stress in HepG2 and HEK293T cells, suggesting that 25-OCH3-PPD could attenuate ER stress in these cells. Tunicamycin 125-127 heat shock protein family A (Hsp70) member 5 Homo sapiens 46-74 30096296-7 2018 Moreover, 25-OCH3-PPD significantly inhibited glucose-regulated protein 78 (GRP78; the major ER stress marker) expression in TM-induced ER stress in HepG2 and HEK293T cells, suggesting that 25-OCH3-PPD could attenuate ER stress in these cells. Tunicamycin 125-127 heat shock protein family A (Hsp70) member 5 Homo sapiens 76-81 29620275-7 2018 Compared with in cells prior to treatment, human leukemia cells treated with tunicamycin exhibited increased expression of p-PERK, p-eIF2alpha and GRP78 after 72 h (P<0.05). Tunicamycin 77-88 heat shock protein family A (Hsp70) member 5 Homo sapiens 147-152 29764928-6 2018 Our results show that ER stress maker GRP78 expression was increased in human endometrial Ishikawa and endometrial stromal cells (ESCs) treated with tunicamycin. Tunicamycin 149-160 heat shock protein family A (Hsp70) member 5 Homo sapiens 38-43 29764928-7 2018 Addition of estrogen decreased tunicamycin-induced GRP78 expression. Tunicamycin 31-42 heat shock protein family A (Hsp70) member 5 Homo sapiens 51-56 30146638-7 2018 Treatment with tunicamycin resulted in up-regulation of ER stress genes, such as splicing x-box binding protein-1(sXBP1), activating transcription factor 4(ATF4), glucose-regulated protein 78(GRP78) and C/EBP homologous protein (CHOP). Tunicamycin 15-26 heat shock protein family A (Hsp70) member 5 Homo sapiens 192-197 29705800-8 2018 Meanwhile, GRP78 was upregulated in A549 cells exposed to tunicamycin or bleomycin. Tunicamycin 58-69 heat shock protein family A (Hsp70) member 5 Homo sapiens 11-16 29206917-4 2018 We have evaluated the effect of tunicamycin on cellular localization of GRP78 in metastatic human breast cancer cells MDA-MB-231 (ER-/PR-/HER2-). Tunicamycin 32-43 heat shock protein family A (Hsp70) member 5 Homo sapiens 72-77 29206917-7 2018 GRP78 expression (protein and mRNA) was higher in tunicamycin (1.0 mug/mL) treated MCF-7 and MDA-MB-231 cells. Tunicamycin 50-61 heat shock protein family A (Hsp70) member 5 Homo sapiens 0-5 29206917-12 2018 The conclusion, GRP78 is expressed neither on the outer-leaflet of the (ER-/PR-/HER2-) human breast cancer cells nor it is secreted into the culture media during tunicamycin-induced ER stress. Tunicamycin 162-173 heat shock protein family A (Hsp70) member 5 Homo sapiens 16-21 26796921-4 2016 Tunicamycin (TM), an ER stress inducer, constitutively activates the mitogen-activated protein kinase (MAPK)/extracellular signal regulated kinase (ERK), and (MEK)/ERK pathway which plays a role in upregulation of GRP78 by ER stress in that inhibition of MEK by U0126 reduces the levels of GRP78 and blocks its upregulation by TM. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 214-219 28841673-2 2017 We demonstrated the induction of ER stress in response to tunicamycin stimulation, as evidenced by increased expression of chaperone proteins Grp78, Grp94, and enhanced eukaryotic initiation factor 2 subunit 1 (eIF2alpha) phosphorylation in hepatocellular carcinoma cells. Tunicamycin 58-69 heat shock protein family A (Hsp70) member 5 Homo sapiens 142-147 28978049-4 2017 We showed GRP78/BiP translocation to PC3 cell surface in the presence of tunicamycin, an ER stress inductor, and demonstrated the existence of a GRP78/BiP-dependent non-canonical Nrf2 activation, responsible for increased resistance to ER-stress induced apoptosis. Tunicamycin 73-84 heat shock protein family A (Hsp70) member 5 Homo sapiens 10-15 28978049-4 2017 We showed GRP78/BiP translocation to PC3 cell surface in the presence of tunicamycin, an ER stress inductor, and demonstrated the existence of a GRP78/BiP-dependent non-canonical Nrf2 activation, responsible for increased resistance to ER-stress induced apoptosis. Tunicamycin 73-84 heat shock protein family A (Hsp70) member 5 Homo sapiens 16-19 28978049-5 2017 We found that, even in the absence of ROS production, tunicamycin causes Nrf2 activation, and activates Akt signaling, events bulnted by anti-GRP78/BiP antibody treatment. Tunicamycin 54-65 heat shock protein family A (Hsp70) member 5 Homo sapiens 142-147 28978049-5 2017 We found that, even in the absence of ROS production, tunicamycin causes Nrf2 activation, and activates Akt signaling, events bulnted by anti-GRP78/BiP antibody treatment. Tunicamycin 54-65 heat shock protein family A (Hsp70) member 5 Homo sapiens 148-151 28631572-7 2017 Tunicamycin led to increased expression of GRP78. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 43-48 28024901-6 2017 The ER stress inducer, tunicamycin, also up-regulated the kinase activity and protein expression of Cdk5 in podocytes accompanied with the increasing of GRP78. Tunicamycin 23-34 heat shock protein family A (Hsp70) member 5 Homo sapiens 153-158 26796921-4 2016 Tunicamycin (TM), an ER stress inducer, constitutively activates the mitogen-activated protein kinase (MAPK)/extracellular signal regulated kinase (ERK), and (MEK)/ERK pathway which plays a role in upregulation of GRP78 by ER stress in that inhibition of MEK by U0126 reduces the levels of GRP78 and blocks its upregulation by TM. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 290-295 26796921-7 2016 This sensitization of breast cancer cells to TM-induced apoptosis by inhibition of MEK/ERK and GRP78 is caspase-dependent, at least in part, by activation of caspase-4. Tunicamycin 45-47 heat shock protein family A (Hsp70) member 5 Homo sapiens 95-100 23755268-6 2013 We show that VCD was highly cytotoxic only under hypoglycemic conditions, but not in the presence of normal glucose levels, and VCD blocked GRP78 expression only when glycolysis was impaired (due to hypoglycemia or the presence of the glycolysis inhibitor 2-deoxyglucose), but not when GRP78 was induced by other means (hypoxia, thapsigargin, tunicamycin). Tunicamycin 343-354 heat shock protein family A (Hsp70) member 5 Homo sapiens 140-145 24982359-4 2014 MATERIALS AND METHODS: GRP78 was over-expressed in A549 cells with 2-deoxyglucose (2-dG) or tunicamycin (TM) treatments for 48 h and subsequently exposed to cisplatin for 2 h. Viability of these cells was determined at 0, 12, 24, 36 and 48 h afterwards. Tunicamycin 92-103 heat shock protein family A (Hsp70) member 5 Homo sapiens 23-28 24982359-4 2014 MATERIALS AND METHODS: GRP78 was over-expressed in A549 cells with 2-deoxyglucose (2-dG) or tunicamycin (TM) treatments for 48 h and subsequently exposed to cisplatin for 2 h. Viability of these cells was determined at 0, 12, 24, 36 and 48 h afterwards. Tunicamycin 105-107 heat shock protein family A (Hsp70) member 5 Homo sapiens 23-28 26540043-5 2015 MEAO significantly inhibited tunicamycin-induced ER stress marker expression including GRP78, CHOP, and XBP-1 in tunicamycin-treated Human hepatocellular carcinoma (HepG2) cells and the livers of tunicamycin-injected mice. Tunicamycin 29-40 heat shock protein family A (Hsp70) member 5 Homo sapiens 87-92 26540043-10 2015 Alismol, a guaiane-type sesquiterpenes in Alisma orientale, inhibited GRP78 expression in tunicamycin-treated HepG2 cells. Tunicamycin 90-101 heat shock protein family A (Hsp70) member 5 Homo sapiens 70-75 25881988-7 2015 Tunicamycin treatment increased (P < 0.01) and TUDCA treatment decreased (P < 0.01) the expression level of ER chaperones, GRP78 and GRP94. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 129-134 25322957-5 2015 Thapsigargin/tunicamycin treatment induced a significant increase in endoplasmic reticulum stress and of cell death, represented by higher GADD153 and GRP78 expression and propidium iodide flow cytometry, respectively. Tunicamycin 13-24 heat shock protein family A (Hsp70) member 5 Homo sapiens 151-156 25428129-4 2015 Tunicamycin induced the phosphorylation and activation of PERK and eIF2alpha within 2 h in RPTC, which was followed by the induction of GRP78 and CHOP. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 136-141 25428129-7 2015 Inhibition of mTOR with rapamycin partially suppressed the phosphorylation of PERK and eIF2a and the induction of CHOP and GRP78 induction during tunicamycin treatment. Tunicamycin 146-157 heat shock protein family A (Hsp70) member 5 Homo sapiens 123-128 25360516-2 2014 Here, we show that induction in cell surface GRP78 by doxorubicin and tunicamycin was associated with CHOP/GADD153 upregulation and increase in apoptosis in triple negative breast cancer tumor cells. Tunicamycin 70-81 heat shock protein family A (Hsp70) member 5 Homo sapiens 45-50 25360516-4 2014 The blocking of cell surface GRP78 by anti-GRP78 antibody prevented apoptosis, suggesting that induction of cell surface GRP78 by doxorubicin and tunicamycin is required for apoptosis. Tunicamycin 146-157 heat shock protein family A (Hsp70) member 5 Homo sapiens 29-34 25360516-4 2014 The blocking of cell surface GRP78 by anti-GRP78 antibody prevented apoptosis, suggesting that induction of cell surface GRP78 by doxorubicin and tunicamycin is required for apoptosis. Tunicamycin 146-157 heat shock protein family A (Hsp70) member 5 Homo sapiens 43-48 25360516-4 2014 The blocking of cell surface GRP78 by anti-GRP78 antibody prevented apoptosis, suggesting that induction of cell surface GRP78 by doxorubicin and tunicamycin is required for apoptosis. Tunicamycin 146-157 heat shock protein family A (Hsp70) member 5 Homo sapiens 43-48 25026174-5 2014 Tunicamycin or brefeldin A, two ER stress inducers, increased APE1 and GRP78, an ER stress marker, expression in HepG2 and Huh-7 cells. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 71-76 24604564-5 2014 GRP78 protein levels were similar in the tunicamycin (Tm), salubrinal, and SP600125 groups, but were lower in cells treated with SN50. Tunicamycin 41-52 heat shock protein family A (Hsp70) member 5 Homo sapiens 0-5 22740470-5 2012 The important ER stress regulator 78 kDa glucose-regulated protein (GRP-78 or BiP) was highly upregulated together with several proteins that have been found to form a multiprotein complex with BiP including cyclophilin B, DnaJ homolog subfamily B member 11, endoplasmin, hypoxia upregulated protein 1, protein disulfide isomerase and protein disulfide isomerase A4 upon tunicamycin-induced ER stress. Tunicamycin 371-382 heat shock protein family A (Hsp70) member 5 Homo sapiens 68-74 23171849-3 2012 Here we show in U937 cells that the ER stressors tunicamycin and thapsigargin cause increased expression of c-Jun N-terminal kinase 2 (JNK2), which allows regulation of the UPR, whose silencing or pharmacological inhibition delays BiP (immunoglobulin heavy-chain binding protein) upregulation, and causes earlier and greater expression of CCAAT/enhancer-binding protein-homologous protein (CHOP). Tunicamycin 49-60 heat shock protein family A (Hsp70) member 5 Homo sapiens 231-234 22740470-5 2012 The important ER stress regulator 78 kDa glucose-regulated protein (GRP-78 or BiP) was highly upregulated together with several proteins that have been found to form a multiprotein complex with BiP including cyclophilin B, DnaJ homolog subfamily B member 11, endoplasmin, hypoxia upregulated protein 1, protein disulfide isomerase and protein disulfide isomerase A4 upon tunicamycin-induced ER stress. Tunicamycin 371-382 heat shock protein family A (Hsp70) member 5 Homo sapiens 78-81 22740470-5 2012 The important ER stress regulator 78 kDa glucose-regulated protein (GRP-78 or BiP) was highly upregulated together with several proteins that have been found to form a multiprotein complex with BiP including cyclophilin B, DnaJ homolog subfamily B member 11, endoplasmin, hypoxia upregulated protein 1, protein disulfide isomerase and protein disulfide isomerase A4 upon tunicamycin-induced ER stress. Tunicamycin 371-382 heat shock protein family A (Hsp70) member 5 Homo sapiens 194-197 22550476-5 2012 Cells subjected to either glucolipotoxicity or tunicamycin exhibited increased ROS generation, gene and protein (PERK, GRP-78, IRE1alpha, and CHOP) expression of ER stress markers. Tunicamycin 47-58 heat shock protein family A (Hsp70) member 5 Homo sapiens 119-125 21922249-11 2012 GRP78 expression and xbp-1 mRNA splicing were enhanced significantly in the presence of IFN-gamma/TNF-alpha and tunicamycin, and they could be dampened by BBR. Tunicamycin 112-123 heat shock protein family A (Hsp70) member 5 Homo sapiens 0-5 22699051-4 2012 The expressions of Bax, Bcl-2, and GRP78 in cells treated with 3 micromol/L tunicamycin with or without 6.00 micromol/L cisplatin were measured with Western blotting. Tunicamycin 76-87 heat shock protein family A (Hsp70) member 5 Homo sapiens 35-40 22699051-9 2012 Compared with tunicamycin and cisplatin alone, the combined treatment significantly increased Bax expression and decreased Bcl-2 expression in the cells; tunicamycin up-regulated the expression of GRP-78 and enhanced the activity of caspase-3. Tunicamycin 154-165 heat shock protein family A (Hsp70) member 5 Homo sapiens 197-203 21896647-7 2011 Treatment with ER stressors, tunicamycin or DTT, rapidly decreased BiP-GFP mobility in mHtt striatal cells and accelerated UPR activation compared with wild-type cells. Tunicamycin 29-40 heat shock protein family A (Hsp70) member 5 Homo sapiens 67-70 21527262-4 2011 Time-dependent induction of the ER chaperones, glucose-regulated protein (GRP) 78 and GRP94, was observed after treatment with tunicamycin (TM) (80 mug/mL). Tunicamycin 127-138 heat shock protein family A (Hsp70) member 5 Homo sapiens 47-81 21389343-8 2011 However, tunicamycin-induced HSPA5 expression was significantly lowered in these cells when pretreated with E(2) (P < 0.01 and P < 0.05, respectively). Tunicamycin 9-20 heat shock protein family A (Hsp70) member 5 Homo sapiens 29-34 21527262-4 2011 Time-dependent induction of the ER chaperones, glucose-regulated protein (GRP) 78 and GRP94, was observed after treatment with tunicamycin (TM) (80 mug/mL). Tunicamycin 140-142 heat shock protein family A (Hsp70) member 5 Homo sapiens 47-81 21605547-5 2011 TUDCA efficiently inhibited the expression of UPR dependent genes like GRP78 triggered by the ER stressor tunicamycin in the small intestinal epithelial cell line Mode-K. TUDCA inhibited upstream signaling events in all three branches of the UPR cascade and diminished binding of UPR activated transcription factors to the grp78 promoter. Tunicamycin 106-117 heat shock protein family A (Hsp70) member 5 Homo sapiens 71-76 21605547-5 2011 TUDCA efficiently inhibited the expression of UPR dependent genes like GRP78 triggered by the ER stressor tunicamycin in the small intestinal epithelial cell line Mode-K. TUDCA inhibited upstream signaling events in all three branches of the UPR cascade and diminished binding of UPR activated transcription factors to the grp78 promoter. Tunicamycin 106-117 heat shock protein family A (Hsp70) member 5 Homo sapiens 323-328 20628148-8 2010 Manipulating ER signaling by siRNA down-regulation of BiP/GRP78 or treating B-CLL cells with 2 well-known ER stress-inducers, tunicamycin and thapsigargin, increases their apoptosis. Tunicamycin 126-137 heat shock protein family A (Hsp70) member 5 Homo sapiens 58-63 20974203-5 2011 Pretreatment with ER stress inducers, thapsigargin (Tg) and tunicamycin (Tm), promoted GRP78 mRNA induction and ATF4 translation, which are ER stress markers, under our experimental conditions and protected against the cytotoxicity. Tunicamycin 60-71 heat shock protein family A (Hsp70) member 5 Homo sapiens 87-92 20974203-5 2011 Pretreatment with ER stress inducers, thapsigargin (Tg) and tunicamycin (Tm), promoted GRP78 mRNA induction and ATF4 translation, which are ER stress markers, under our experimental conditions and protected against the cytotoxicity. Tunicamycin 73-75 heat shock protein family A (Hsp70) member 5 Homo sapiens 87-92 19777212-0 2009 Tunicamycin induces resistance to camptothecin and etoposide in human hepatocellular carcinoma cells: role of cell-cycle arrest and GRP78. Tunicamycin 0-11 heat shock protein family A (Hsp70) member 5 Homo sapiens 132-137 19777212-11 2009 Furthermore, the cells transfected with GRP78 siRNA were partly resistant to tunicamycin-induced apoptosis but not the inhibitory effect on cell-cycle regulators indicating that GRP78 and G1 arrest are two independent factors to tunicamycin-induced resistance mechanism. Tunicamycin 77-88 heat shock protein family A (Hsp70) member 5 Homo sapiens 40-45 19777212-11 2009 Furthermore, the cells transfected with GRP78 siRNA were partly resistant to tunicamycin-induced apoptosis but not the inhibitory effect on cell-cycle regulators indicating that GRP78 and G1 arrest are two independent factors to tunicamycin-induced resistance mechanism. Tunicamycin 229-240 heat shock protein family A (Hsp70) member 5 Homo sapiens 40-45 19777212-12 2009 In conclusion, the data suggest that tunicamycin induces the resistance to topoisomerase inhibitors through GRP78 up-regulation and G1 arrest of the cell cycle. Tunicamycin 37-48 heat shock protein family A (Hsp70) member 5 Homo sapiens 108-113