Oxygen–Glucose Deprivation (OGD) Modulates the Unfolded Protein Response (UPR) and Inflicts Autophagy in a PC12 Hypoxia Cell Line Model

2015 ◽  
Vol 36 (5) ◽  
pp. 701-712 ◽  
Author(s):  
Theofanis Vavilis ◽  
Nikoleta Delivanoglou ◽  
Eleni Aggelidou ◽  
Eleni Stamoula ◽  
Kyriakos Mellidis ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Cell Line ◽  
Glucose Deprivation ◽  
Oxygen Glucose Deprivation ◽  
Line Model ◽  
Unfolded Protein ◽  
Cell Line Model ◽  
The Unfolded Protein Response ◽  
Protein Response

The unfolded protein response in a dolichyl phosphate mannose-deficient Chinese hamster ovary cell line points out the key role of a demannosylation step in the quality-control mechanism of N-glycoproteins

2002 ◽  
Vol 362 (2) ◽  
pp. 491-498 ◽  
Author(s):  
François FOULQUIER ◽  
Anne HARDUIN-LEPERS ◽  
Sandrine DUVET ◽  
Ingrid MARCHAL ◽  
Anne Marie MIR ◽  
...  
Keyword(s):  
Quality Control ◽  
Control System ◽  
Unfolded Protein Response ◽  
Cell Line ◽  
Chinese Hamster Ovary ◽  
Chinese Hamster ◽  
Quality Control System ◽  
Unfolded Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

The CHO (Chinese hamster ovary) glycosylation mutant cell line, B3F7, transfers the truncated glycan Glc3Man5GlcNAc2 on to nascent proteins. After deglucosylation, the resulting Man5GlcNAc2 glycan is subjected to two reciprocal enzymic processes: the action of an endoplasmic-reticulum (ER) kifunensine-sensitive α1,2-mannosidase activity to yield a Man4GlcNAc2 glycan, and the reglucosylation involved in the quality-control system which ensures that only correctly folded glycoproteins leave the ER. We show that the recombinant secreted alkaline phosphatase (SeAP) produced in stably transfected B3F7 cells, is co-immunoprecipitated with the GRP78 (glucose-regulated protein 78), a protein marker of the unfolded protein response (UPR). The level of GRP78 transcription has been evaluated by reverse transcription-PCR (RT-PCR) and we demonstrate that B3F7 cells present a constitutively higher level of UPR in the absence of inductors, compared with Pro−5 cells. Interestingly, a decrease was observed in the UPR and an increase in SeAP secretion in the kifunensine-treated B3F7 cells. Altogether, these data highlight the relationships between the glycan structure, the quality control system and the UPR. Moreover, they support the idea that a specific demannosylation step is a key event of the glycoprotein quality control in B3F7 cells.

Glucose, dexamethasone, and the unfolded protein response regulate TRB3 mRNA expression in 3T3-L1 adipocytes and L6 myotubes

2006 ◽  
Vol 291 (6) ◽  
pp. E1274-E1280 ◽  
Author(s):  
Sherif Z. Yacoub Wasef ◽  
Katherine A. Robinson ◽  
Mary N. Berkaw ◽  
Maria G. Buse
Keyword(s):  
Insulin Resistance ◽  
Cell Survival ◽  
Mrna Expression ◽  
Unfolded Protein Response ◽  
High Glucose ◽  
Glucose Deprivation ◽  
Unfolded Protein ◽  
L6 Myotubes ◽  
The Unfolded Protein Response ◽  
Protein Response

Tribbles 3 (TRB3) is a recently recognized atypical inactive kinase that negatively regulates Akt activity in hepatocytes, resulting in insulin resistance. Recent reports link TRB3 to nutrient sensing and regulation of cell survival under stressful conditions. We studied the regulation of TRB3 by glucose, insulin, dexamethasone (Dex), and the unfolded protein response (UPR) in 3T3-L1 adipocytes and in L6 myotubes. In 3T3-L1 adipocytes, incubation in high glucose with insulin did not increase TRB3 mRNA expression. Rather, TRB3 mRNA increased fourfold with glucose deprivation and two- to threefold after incubation with tunicamcyin (an inducer of the UPR). Incubation of cells in no glucose or in tunicamcyin stimulated the expression of CCAAT/enhancer-binding protein homologous protein. In L6 myotubes, absent or low glucose induced TRB3 mRNA expression by six- and twofold, respectively. The addition of Dex to 5 mM glucose increased TRB3 mRNA expression twofold in 3T3-L1 adipocytes but decreased it 16% in L6 cells. In conclusion, TRB3 is not the mediator of high glucose or glucocorticoid-induced insulin resistance in 3T3-L1 adipocytes or L6 myotubes. TRB3 is induced by glucose deprivation in both cell types as a part of the UPR, where it may be involved in regulation of cell survival in response to glucose depletion.

The flavonoid tangeretin activates the unfolded protein response and synergizes with imatinib in the erythroleukemia cell line K562

2010 ◽  
Vol 54 (6) ◽  
pp. 823-832 ◽  
Author(s):  
Sofie Lust ◽  
Barbara Vanhoecke ◽  
Mireille Van Gele ◽  
Jan Philippé ◽  
Marc Bracke ◽  
...  
Keyword(s):  
Unfolded Protein Response ◽  
Cell Line ◽  
Unfolded Protein ◽  
Erythroleukemia Cell ◽  
The Unfolded Protein Response ◽  
Protein Response

scholarly journals Cullin3-RING ubiquitin ligases are intimately linked to the unfolded protein response of the endoplasmic reticulum

2018 ◽  
Author(s):  
Kyungho Kim ◽  
Tamara Moretti ◽  
Sujin Park ◽  
Jinoh Kim
Keyword(s):  
Endoplasmic Reticulum ◽  
Unfolded Protein Response ◽  
Cell Line ◽  
Ubiquitin Ligases ◽  
C2c12 Myotubes ◽  
Unfolded Protein ◽  
Btb Domain ◽  
Domain Protein ◽  
The Unfolded Protein Response ◽  
Protein Response

ABSTRACTCUL3-RING ubiquitin ligases (CRL3s) are involved in various cellular processes through different Bric a brac, Tramtrack and Broad-Complex (BTB)-domain proteins. KLHL12, a BTB-domain protein, appears to play an essential role in export of large cargo molecules like procollagen from the endoplasmic reticulum (ER). It has been suggested that CRL3KLHL12 mono-ubiquitinates SEC31 and mono-ubiquitinated SEC31 increases the dimension of a COPII coat to accommodate the large cargo molecules. As we examined this model, we found that functional CRL3KLHL12 was indeed critical for the assembly of large COPII structures. Interestingly, we noticed that CRL3KLHL12 influences collagen synthesis in human skin fibroblasts (HSFs). Our results also suggest that there is a CRL3KLHL12–independent collagen secretion route in HSFs. In addition, we found that CRL3KLHL12 strongly influences levels of sensors of the unfolded protein response (UPR). Different cell lines reacted differently to CUL3 depletion with respect to UPR regulation. This cell line-dependency appears to rely on a cell line-specific BTB-domain protein(s). Consistent with this idea, depletion of a muscle-specific BTB-domain protein KLHL41 recapitulated the effects of CUL3 depletion in C2C12 myotubes in UPR regulation. Based on these results we propose that CRL3KLHL12 and CRL3KLHL41 are regulators of the UPR.

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