scholarly journals The E3 Ubiquitin Ligase MARCH8 Regulates TNF‐α‐Induced Apoptosis in Hippocampal Neurons by Targeting Myosin Light Chain 2 for Degradation

2019 ◽  
Vol 302 (12) ◽  
pp. 2271-2278
Author(s):  
Shanglin Guo ◽  
Yongqing Zhang ◽  
Chaoping Wei ◽  
Lu Shi ◽  
Yugong Feng
Keyword(s):  
Ubiquitin Ligase ◽  
Light Chain ◽  
Hippocampal Neurons ◽  
Myosin Light Chain ◽  
E3 Ubiquitin Ligase ◽  
Myosin Light Chain 2 ◽  
Tnf Α ◽  
Induced Apoptosis

scholarly journals LncTRPM2-AS inhibits TRIM21-mediated TRPM2 ubiquitination and prevents autophagy-induced apoptosis of macrophages in asthma

2021 ◽  
Vol 12 (12) ◽  
Author(s):  
Xiaoping Li ◽  
Wenwen Wang ◽  
Yu Shao ◽  
Ji Zhou ◽  
Jiaqi Huang ◽  
...  
Keyword(s):  
Mass Spectrometry ◽  
Ubiquitin Ligase ◽  
Crucial Role ◽  
Cytokine Production ◽  
E3 Ubiquitin Ligase ◽  
Tnf Α ◽  
Rna Immunoprecipitation ◽  
Non Coding Rnas ◽  
Induced Apoptosis

AbstractLong non-coding RNAs (lncRNAs) play a crucial role in macrophage development but little is known about their role in asthma. Here, we investigated the role of lncRNA lncTRPM2-AS in asthma and found that lncTRPM2-AS participates in the promotion of macrophage inflammation. Downregulation of lncTRPM2-AS promoted apoptosis and inhibited proliferation and production of cytokines including IL-1β, IL-4, IL-6, IL-10, TNF-α, and TGF-β. RNA-immunoprecipitation and mass spectrometry indicated that the protein TRPM2 interacted with both lncTRPM2-AS and the E3 ubiquitin ligase TRIM21. LncTRPM2-AS silencing enhanced the interaction between TRIM21 and TRPM2, resulting in elevated levels of ubiquitin-related degradation of TRPM2. Mutation analysis indicated that TRPM2 K1218 is a key site for TRIM21-dependent ubiquitination. Downregulation of lncTRPM2-AS significantly decreased intracellular calcium levels by restraining TRPM2 protein expression, which in turn decreased ROS levels and increased autophagy to promote macrophage apoptosis and reduce cytokine production, together inhibiting macrophage inflammation. Taken together, our findings demonstrate that lncTRPM2-AS blocks the ubiquitination of TRPM2 via TRIM21 and inhibits autophagy-induced apoptosis which may contribute to macrophage inflammation in asthma.

scholarly journals Chamber specification of atrial myosin light chain-2 expression precedes septation during murine cardiogenesis

1994 ◽  
Vol 269 (24) ◽  
pp. 16961-16970
Author(s):  
S.W. Kubalak ◽  
W.C. Miller-Hance ◽  
T.X. O'Brien ◽  
E. Dyson ◽  
K.R. Chien
Keyword(s):  
Light Chain ◽  
Myosin Light Chain ◽  
Myosin Light Chain 2 ◽  
Atrial Myosin

scholarly journals Herpes Simplex Virus 1 E3 Ubiquitin Ligase ICP0 Protein Inhibits Tumor Necrosis Factor Alpha-Induced NF-κB Activation by Interacting with p65/RelA and p50/NF-κB1

2013 ◽  
Vol 87 (23) ◽  
pp. 12935-12948 ◽  
Author(s):  
Jie Zhang ◽  
Kezhen Wang ◽  
Shuai Wang ◽  
Chunfu Zheng
Keyword(s):  
Tumor Necrosis Factor ◽  
Ubiquitin Ligase ◽  
Tumor Necrosis ◽  
Nuclear Translocation ◽  
E3 Ubiquitin Ligase ◽  
Necrosis Factor Alpha ◽  
Tnf Α ◽  
Factor Alpha ◽  
Necrosis Factor ◽  
Hsv 1

NF-κB plays central roles in regulation of diverse biological processes, including innate and adaptive immunity and inflammation. HSV-1 is the archetypal member of the alphaherpesviruses, with a large genome encoding over 80 viral proteins, many of which are involved in virus-host interactions and show immune modulatory capabilities. In this study, we demonstrated that the HSV-1 ICP0 protein, a viral E3 ubiquitin ligase, was shown to significantly suppress tumor necrosis factor alpha (TNF-α)-mediated NF-κB activation. ICP0 was demonstrated to bind to the NF-κB subunits p65 and p50 by coimmunoprecipitation analysis. ICP0 bound to the Rel homology domain (RHD) of p65. Fluorescence microscopy demonstrated that ICP0 abolished nuclear translocation of p65 upon TNF-α stimulation. Also, ICP0 degraded p50 via its E3 ubiquitin ligase activity. The RING finger (RF) domain mutant ICP0 (ICP0-RF) lost its ability to inhibit TNF-α-mediated NF-κB activation and p65 nuclear translocation and degrade p50. Notably, the RF domain of ICP0 was sufficient to interact with p50 and abolish NF-κB reporter gene activity. Here, it is for the first time shown that HSV-1 ICP0 interacts with p65 and p50, degrades p50 through the ubiquitin-proteasome pathway, and prevents NF-κB-dependent gene expression, which may contribute to immune evasion and pathogenesis of HSV-1.

scholarly journals The protective mechanism of Ginkgolides and Ginkgo flavonoids on the TNF-α induced apoptosis of rat hippocampal neurons and its mechanisms in vitro

Heliyon ◽  
2015 ◽  
Vol 1 (1) ◽  
pp. e00020 ◽  
Author(s):  
Maojuan Guo ◽  
Yanrong Suo ◽  
Qing Gao ◽  
Huan Du ◽  
Wenyun Zeng ◽  
...  
Keyword(s):  
Hippocampal Neurons ◽  
Protective Mechanism ◽  
Tnf Α ◽  
Induced Apoptosis
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