scholarly journals Tumor Necrosis Factor Receptor 1-Associated DEATH Domain Protein

2020 ◽  
Author(s):  
Keyword(s):  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Death Domain ◽  
Domain Protein ◽  
Necrosis Factor

scholarly journals Reduced Tumor Necrosis Factor Receptor–Associated Death Domain Expression Is Associated with Prostate Cancer Progression

2009 ◽  
Vol 69 (24) ◽  
pp. 9448-9456 ◽  
Author(s):  
Diping Wang ◽  
R. Bruce Montgomery ◽  
Lucy J. Schmidt ◽  
Elahe A. Mostaghel ◽  
Haojie Huang ◽  
...  
Keyword(s):  
Prostate Cancer ◽  
Tumor Necrosis Factor ◽  
Cancer Progression ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Death Domain ◽  
Prostate Cancer Progression ◽  
Necrosis Factor

Expression in Escherichia coli of the Death Domain of the Human p55 Tumor Necrosis Factor Receptor

2001 ◽  
Vol 23 (2) ◽  
pp. 226-232 ◽  
Author(s):  
Gert De Wilde ◽  
Nico Mertens ◽  
Elke Boone ◽  
Bart De Vreese ◽  
Jozef Van Beeumen ◽  
...  
Keyword(s):  
Escherichia Coli ◽  
Tumor Necrosis Factor ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Death Domain ◽  
Expression In Escherichia Coli ◽  
Necrosis Factor

scholarly journals Reactive Nitrogen Species-Induced Cell Death Requires Fas-Dependent Activation of c-Jun N-Terminal Kinase

2004 ◽  
Vol 24 (15) ◽  
pp. 6763-6772 ◽  
Author(s):  
Punya Shrivastava ◽  
Cristen Pantano ◽  
Richard Watkin ◽  
Brian McElhinney ◽  
Amy Guala ◽  
...  
Keyword(s):  
Cell Death ◽  
Tumor Necrosis Factor ◽  
Reactive Nitrogen Species ◽  
Tumor Necrosis ◽  
Tumor Necrosis Factor Receptor ◽  
Reactive Nitrogen ◽  
Death Domain ◽  
Nitrogen Species ◽  
Jnk Activation ◽  
Necrosis Factor

ABSTRACT Nitrogen dioxide is a highly toxic reactive nitrogen species (RNS) recently discovered as an inflammatory oxidant with great potential to damage tissues. We demonstrate here that cell death by RNS was caused by c-Jun N-terminal kinase (JNK). Activation of JNK by RNS was density dependent and caused mitochondrial depolarization and nuclear condensation. JNK activation by RNS was abolished in cells lacking functional Fas or following expression of a truncated version of Fas lacking the intracellular death domain. In contrast, RNS induced JNK potently in cells expressing a truncated version of tumor necrosis factor receptor 1 or cells lacking tumor necrosis factor receptor 1 (TNF-R1), illustrating a dependence of Fas but not TNF-R1 in RNS-induced signaling to JNK. Furthermore, Fas was oxidized, redistributed, and colocalized with Fas-associated death domain (FADD) in RNS-exposed cells, illustrating that RNS directly targeted Fas. JNK activation and cell death by RNS occurred in a Fas ligand- and caspase-independent manner. While the activation of JNK by RNS or FasL required FADD, the cysteine-rich domain 1 containing preligand assembly domain required for FasL signaling was not involved in JNK activation by RNS. These findings illustrate that RNS cause cell death in a Fas- and JNK-dependent manner and that this occurs through a pathway distinct from FasL. Thus, avenues aimed at preventing the interaction of RNS with Fas may attenuate tissue damage characteristic of chronic inflammatory diseases that are accompanied by high levels of RNS.

Sign in / Sign up

Export Citation Format

Share Document