scholarly journals Angiotensin II type I receptor agonistic autoantibody-induced apoptosis in neonatal rat cardiomyocytes is dependent on the generation of tumor necrosis factor- 

2012 ◽  
Vol 44 (12) ◽  
pp. 984-990 ◽  
Author(s):  
W. Chai ◽  
W. Zhang ◽  
Z. Jin ◽  
Y. Feng ◽  
Y. Kuang ◽  
...  
Keyword(s):  
Angiotensin Ii ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Neonatal Rat ◽  
Type I ◽  
Rat Cardiomyocytes ◽  
Neonatal Rat Cardiomyocytes ◽  
Induced Apoptosis ◽  
Necrosis Factor

scholarly journals Tumor Necrosis Factor-α Downregulates the Voltage Gated Outward K+ Current in Cultured Neonatal Rat Cardiomyocytes

2006 ◽  
Vol 70 (5) ◽  
pp. 605-609 ◽  
Author(s):  
Hideaki Kawada ◽  
Shinichi Niwano ◽  
Hiroe Niwano ◽  
Yoshihiro Yumoto ◽  
Yuko Wakisaka ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Α ◽  
Neonatal Rat ◽  
Rat Cardiomyocytes ◽  
Voltage Gated ◽  
Neonatal Rat Cardiomyocytes ◽  
K Current ◽  
Factor Α ◽  
Necrosis Factor

scholarly journals Keratin attenuates tumor necrosis factor–induced cytotoxicity through association with TRADD

2001 ◽  
Vol 155 (3) ◽  
pp. 415-426 ◽  
Author(s):  
Hiroyasu Inada ◽  
Ichiro Izawa ◽  
Miwako Nishizawa ◽  
Eriko Fujita ◽  
Tohru Kiyono ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Epithelial Cells ◽  
Tumor Necrosis ◽  
Mammary Epithelial Cells ◽  
Mammary Epithelial ◽  
Type I ◽  
Death Domain ◽  
Interacting Protein ◽  
Induced Apoptosis ◽  
Necrosis Factor

Keratin 8 and 18 (K8/18) are the major components of intermediate filament (IF) proteins of simple or single-layered epithelia. Recent data show that normal and malignant epithelial cells deficient in K8/18 are nearly 100 times more sensitive to tumor necrosis factor (TNF)–induced cell death. We have now identified human TNF receptor type 1 (TNFR1)–associated death domain protein (TRADD) to be the K18-interacting protein. Among IF proteins tested in two-hybrid systems, TRADD specifically bound K18 and K14, type I (acidic) keratins. The COOH-terminal region of TRADD interacted with the coil Ia of the rod domain of K18. Endogenous TRADD coimmunoprecipitated with K18, and colocalized with K8/18 filaments in human mammary epithelial cells. Overexpression of the NH2 terminus (amino acids 1–270) of K18 containing the TRADD-binding domain as well as overexpression of K8/18 in SW13 cells, which are devoid of keratins, rendered the cells more resistant to killing by TNF. We also showed that overexpressed NH2 termini of K18 and K8/18 were associated with endogenous TRADD in SW13 cells, resulting in the inhibition of caspase-8 activation. These results indicate that K18 may sequester TRADD to attenuate interactions between TRADD and activated TNFR1 and moderate TNF-induced apoptosis in simple epithelial cells.

scholarly journals SARS-CoV-2 Accessory Protein ORF7b Mediates Tumor Necrosis Factor-α-Induced Apoptosis in Cells

2021 ◽  
Vol 12 ◽  
Author(s):  
Ruiping Yang ◽  
Qiong Zhao ◽  
Jingjing Rao ◽  
Feng Zeng ◽  
Shengren Yuan ◽  
...  
Keyword(s):  
Tumor Necrosis Factor ◽  
Immune Responses ◽  
Tumor Necrosis ◽  
Accessory Protein ◽  
Type I ◽  
Host Immune Responses ◽  
Tnf Α ◽  
Induced Apoptosis ◽  
Necrosis Factor ◽  
In Cells

The accessory proteins of coronaviruses are essential for virus–host interactions and the modulation of host immune responses. It has been reported that accessory protein ORF3a encoded by severe acute respiratory syndrome coronavirus 2 (SARS-CoV-2) can induce apoptosis, and accessory protein ORF6 and ORF8 could be inhibitors of the type-I interferon (IFN) signaling pathway. However, the function of accessory protein ORF7b is largely unknown. We investigated the apoptosis-inducing activity of ORF7b in cells. Cytokine levels and host innate immune responses, including expression of interferon regulatory transcription factor (IRF)-3, signal transducer and activator of transcription (STAT)-1, interferon (IFN)-β, tumor necrosis factor (TNF)-α, and interleukin (IL)-6, were also investigated. We found that ORF7b promoted expression of IFN-β, TNF-α, and IL-6, activated type-I IFN signaling through IRF3 phosphorylation, and activated TNFα-induced apoptosis in HEK293T cells and Vero E6 cells. These results could provide deeper understanding about the pathogenicity of SARS-CoV-2 as well as the interaction between the accessory protein ORF7b with host immune responses.

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