scholarly journals Mitochondrial fusion protein 2 regulates endoplasmic reticulum stress in preeclampsia

2021 ◽  
Vol 22 (2) ◽  
pp. 165-170
Author(s):  
Dandan Sun ◽  
Hui Zhu ◽  
Ling Ai ◽  
Hanbing Wu ◽  
Yanting Wu ◽  
...  
Keyword(s):  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Fusion Protein ◽  
Mitochondrial Fusion

scholarly journals Mdivi-1 Protects CD4+ T Cells against Apoptosis via Balancing Mitochondrial Fusion-Fission and Preventing the Induction of Endoplasmic Reticulum Stress in Sepsis

2019 ◽  
Vol 2019 ◽  
pp. 1-14 ◽  
Author(s):  
You Wu ◽  
Yong-Ming Yao ◽  
He-Liang Ke ◽  
Lan Ying ◽  
Yao Wu ◽  
...  
Keyword(s):  
T Cells ◽  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress ◽  
Protective Effect ◽  
Mitochondrial Fusion ◽  
Mitochondrial Morphology ◽  
Experimental Sepsis ◽  
The Impact

Apoptosis of CD4+ T cells plays a central role in the progression of sepsis because it is associated with subsequent immunosuppression and the lack of specific treatment. Thus, developing therapeutic strategies to attenuate the apoptosis of CD4+ T cells in sepsis is critical. Several studies have demonstrated that Mdivi-1, which is a selective inhibitor of the dynamin-related protein 1 (Drp1), attenuates apoptosis of myocardial cells and neurons during various pathologic states. The present study revealed the impact of Mdivi-1 on the apoptosis of CD4+ T cells in sepsis and the potential underlying mechanisms. We used lipopolysaccharide (LPS) stimulation and cecal ligation and puncture (CLP) surgery as sepsis models in vitro and in vivo, respectively. Our results showed that Mdivi-1 attenuated the apoptosis of CD4+ T cells both in vitro and in vivo. The potential mechanism underlying the protective effect of Mdivi-1 involved Mdivi-1 reestablishing mitochondrial fusion-fission balance in sepsis, as reflected by the expression of the mitofusin 2 (MFN2) and optic atrophy 1 (OPA1) , Drp1 translocation, and mitochondrial morphology, as observed by electron microscopy. Moreover, Mdivi-1 treatment reduced reactive oxygen species (ROS) production and prevented the induction of endoplasmic reticulum stress (ERS) and associated apoptosis. After using tunicamycin to activate ER stress, the protective effect of Mdivi-1 on CD4+ T cells was reversed. Our results suggested that Mdivi-1 ameliorated apoptosis in CD4+ T cells by reestablishing mitochondrial fusion-fission balance and preventing the induction of endoplasmic reticulum stress in experimental sepsis.

Overexpression of calreticulin fails to abolish its induction by perturbation of normal ER function

1998 ◽  
Vol 76 (5) ◽  
pp. 875-880 ◽  
Author(s):  
David H Llewellyn ◽  
H Llewelyn Roderick
Keyword(s):  
Endoplasmic Reticulum ◽  
Stress Response ◽  
Endoplasmic Reticulum Stress ◽  
Fusion Protein ◽  
Er Stress ◽  
Hela Cells ◽  
Mammalian Cells ◽  
Stress Signaling ◽  
Glucose Response ◽  
The Stability

Along with other endoplasmic reticulum (ER) Ca2+-binding proteins, notably the glucose-response proteins grp78 and grp94, expression of calreticulin is induced in response to perturbation of normal ER function. It has yet to be clearly defined how this stress is signaled from the ER to the nucleus in mammalian cells, particularly with regard to its initiation. Using a GFP-calreticulin fusion protein, we have generated and selected stably transfected HeLa cells that overexpress calreticulin to investigate whether the protein might be involved in signaling its own induction. Basal levels of endogenous calreticulin mRNA and protein were unaffected in these cells, indicating that overexpression alone does not induce a stress response. ER stress induced calreticulin expression in response to either thapsigargin or tunicamycin was equivalent in these cells to that seen in control, nontransfected cells, leading us to conclude that calreticulin is unlikely be involved in its own induction. Levels of the mRNA encoding the fusion protein were also increased by tunicamycin, but not thapsigargin, suggesting that, in agreement with our previous observations, inhibition of N-linked glycosylation may increase the stability of calreticulin mRNA. This indicates that in mammalian cells, there is more than one signaling pathway for the ER stress response.Key words: calreticulin, endoplasmic reticulum stress, signaling.

scholarly journals Reduction of endoplasmic reticulum stress attenuates the defects caused by Drosophila mitofusin depletion

2014 ◽  
Vol 204 (3) ◽  
pp. 303-312 ◽  
Author(s):  
Valentina Debattisti ◽  
Diana Pendin ◽  
Elena Ziviani ◽  
Andrea Daga ◽  
Luca Scorrano
Keyword(s):  
Endoplasmic Reticulum ◽  
Drosophila Melanogaster ◽  
Endoplasmic Reticulum Stress ◽  
Fusion Protein ◽  
Er Stress ◽  
Mitochondrial Dysfunction ◽  
Stress Reduction ◽  
Optic Atrophy ◽  
Regulatory Factor ◽  
Developmental Defects

Ablation of the mitochondrial fusion and endoplasmic reticulum (ER)–tethering protein Mfn2 causes ER stress, but whether this is just an epiphenomenon of mitochondrial dysfunction or a contributor to the phenotypes in mitofusin (Mfn)-depleted Drosophila melanogaster is unclear. In this paper, we show that reduction of ER dysfunction ameliorates the functional and developmental defects of flies lacking the single Mfn mitochondrial assembly regulatory factor (Marf). Ubiquitous or neuron- and muscle-specific Marf ablation was lethal, altering mitochondrial and ER morphology and triggering ER stress that was conversely absent in flies lacking the fusion protein optic atrophy 1. Expression of Mfn2 and ER stress reduction in flies lacking Marf corrected ER shape, attenuating the developmental and motor defects. Thus, ER stress is a targetable pathogenetic component of the phenotypes caused by Drosophila Mfn ablation.

Abstract #403: The Glutathione Mimic Ebselen Inhibits Oxidative Stress but not Endoplasmic Reticulum Stress in Endothelial Cells.

2015 ◽  
Vol 21 ◽  
pp. 85-86
Author(s):  
William Kurban ◽  
Salma Makhoul Ahwach ◽  
Melanie Thomas ◽  
Luisa Onsteed-Haas ◽  
Michael Haas
Keyword(s):  
Oxidative Stress ◽  
Endothelial Cells ◽  
Endoplasmic Reticulum ◽  
Endoplasmic Reticulum Stress

CUX1 controls endoplasmic reticulum stress and autophagy related cell death

2016 ◽  
Vol 54 (12) ◽  
pp. 1343-1404
Author(s):  
G Metzger ◽  
P Di Fazio ◽  
DK Bartsch ◽  
T Gress ◽  
TT Wissniowski
Keyword(s):  
Endoplasmic Reticulum ◽  
Cell Death ◽  
Endoplasmic Reticulum Stress ◽  
Related Cell
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