scholarly journals Inhibition of Death Receptor Signaling by Flice-Inhibitory Protein as a Mechanism for Immune Escape of Tumors

1999 ◽  
Vol 190 (7) ◽  
pp. 891-894 ◽  
Author(s):  
Lars E. French ◽  
Jürg Tschopp
Keyword(s):  
Immune Escape ◽  
Death Receptor ◽  
Receptor Signaling ◽  
Inhibitory Protein ◽  
Death Receptor Signaling

scholarly journals Superoxide induced inhibition of death receptor signaling is mediated via induced expression of apoptosis inhibitory protein cFLIP

Redox Biology ◽  
2020 ◽  
Vol 30 ◽  
pp. 101403 ◽  
Author(s):  
Jayshree L. Hirpara ◽  
Kothandharaman Subramaniam ◽  
Gregory Bellot ◽  
Jianhua Qu ◽  
Serena Seah ◽  
...  
Keyword(s):  
Death Receptor ◽  
Receptor Signaling ◽  
Inhibitory Protein ◽  
Induced Expression ◽  
Death Receptor Signaling

Beyond apoptosis: nonapoptotic cell death in physiology and disease

2005 ◽  
Vol 83 (5) ◽  
pp. 579-588 ◽  
Author(s):  
Claudio A Hetz ◽  
Vicente Torres ◽  
Andrew F.G Quest
Keyword(s):  
Cell Death ◽  
Programmed Cell Death ◽  
Death Receptor ◽  
Receptor Signaling ◽  
Family Analysis ◽  
Caspase Family ◽  
Death Receptor Signaling ◽  
Apoptotic Pathways ◽  
Nonapoptotic Cell Death ◽  
High Degree

Apoptosis is a morphologically defined form of programmed cell death (PCD) that is mediated by the activation of members of the caspase family. Analysis of death-receptor signaling in lymphocytes has revealed that caspase-dependent signaling pathways are also linked to cell death by nonapoptotic mechanisms, indicating that apoptosis is not the only form of PCD. Under physiological and pathological conditions, cells demonstrate a high degree of flexibility in cell-death responses, as is reflected in the existence of a variety of mechanisms, including necrosis-like PCD, autophagy (or type II PCD), and accidental necrosis. In this review, we discuss recent data suggesting that canonical apoptotic pathways, including death-receptor signaling, control caspase-dependent and -independent cell-death pathways.Key words: apoptosis, necrosis, nonapoptotic programmed cell death, death receptors, ceramides.

scholarly journals Subcellular compartmentalization of FADD as a new level of regulation in death receptor signaling

FEBS Journal ◽  
2009 ◽  
Vol 276 (15) ◽  
pp. 4256-4265 ◽  
Author(s):  
Niko Föger ◽  
Silvia Bulfone-Paus ◽  
Andrew C. Chan ◽  
Kyeong-Hee Lee
Keyword(s):  
Death Receptor ◽  
Receptor Signaling ◽  
Death Receptor Signaling ◽  
Subcellular Compartmentalization

Death Receptor Signaling Giving Life to Ectodermal Organs

2002 ◽  
Vol 2002 (131) ◽  
pp. pe22-pe22 ◽  
Author(s):  
I. Thesleff ◽  
M. L. Mikkola
Keyword(s):  
Death Receptor ◽  
Receptor Signaling ◽  
Death Receptor Signaling

scholarly journals Altered Death Receptor Signaling Promotes Epithelial-to-Mesenchymal Transition and Acquired Chemoresistance

2012 ◽  
Vol 2 (1) ◽  
Author(s):  
James W. Antoon ◽  
Rongye Lai ◽  
Amanda P. Struckhoff ◽  
Ashley M. Nitschke ◽  
Steven Elliott ◽  
...  
Keyword(s):  
Epithelial To Mesenchymal Transition ◽  
Death Receptor ◽  
Receptor Signaling ◽  
Mesenchymal Transition ◽  
Death Receptor Signaling

scholarly journals NF-κB Inducers Upregulate cFLIP, a Cycloheximide-Sensitive Inhibitor of Death Receptor Signaling

2001 ◽  
Vol 21 (12) ◽  
pp. 3964-3973 ◽  
Author(s):  
Sebastian Kreuz ◽  
Daniela Siegmund ◽  
Peter Scheurich ◽  
Harald Wajant
Keyword(s):  
Cell Lines ◽  
Death Receptor ◽  
Jurkat Cells ◽  
Negative Regulator ◽  
Inhibitory Protein ◽  
Iκb Kinase ◽  
Low Concentrations ◽  
Death Receptor Signaling ◽  
Induced Apoptosis ◽  
Necrosis Factor

ABSTRACT The caspase 8 homologue FLICE-inhibitory protein (cFLIP) is a potent negative regulator of death receptor-induced apoptosis. We found that cFLIP can be upregulated in some cell lines under critical involvement of the NF-κB pathway, but NF-κB activation was clearly not sufficient for cFLIP induction in all cell lines. Treatment of SV80 cells with the proteasome inhibitor N-benzoyloxycarbonyl (Z)-Leu-Leu-leucinal (MG-132) or geldanamycin, a drug interfering with tumor necrosis factor (TNF)-induced NF-κB activation, inhibited TNF-induced upregulation of cFLIP. Overexpression of a nondegradable IκBα mutant (IκBα-SR) or lack of IκB kinase γ expression completely prevented phorbol myristate acetate-induced upregulation of cFLIP mRNA in Jurkat cells. These data point to an important role for NF-κB in the regulation of the cFLIP gene. SV80 cells normally show resistance to TNF-related apoptosis-inducing ligand (TRAIL) and TNF, as apoptosis can be induced only in the presence of low concentrations of cycloheximide (CHX). However, overexpression of IκBα-SR rendered SV80 cells sensitive to TRAIL-induced apoptosis in the absence of CHX, and cFLIP expression was able to reverse the proapoptotic effect of NF-κB inhibition. Western blot analysis further revealed that cFLIP, but not TRAF1, A20, and cIAP2, expression levels rapidly decrease upon CHX treatment. In conclusion, these data suggest a key role for cFLIP in the antiapoptotic response of NF-κB activation.

Sign in / Sign up

Export Citation Format

Share Document