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

Shrivastava, Punya; Pantano, Cristen; Watkin, R D; McElhinney, Brian; Guala, Amy S.; Poynter, Matthew E.; Persinger, Rebecca L.; Budd, Ralph C.; Janssen–Heininger, Yvonne M. W.

doi:10.1128/mcb.24.15.6763-6772.2004

Cited by 52 publications

(39 citation statements)

References 70 publications

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“…However, a number of drugs and agents are able to activate a multiprotein complex that promotes the formation of a large channel in the IM, the so-called permeability transition pore (PTP). 25,42,[48][49][50] Changes in mitochondrial membrane potential-∆Ψ m -the energy source of oxphos-are often observed in apoptotic cells and are interpreted to derive from the PTP opening. However, most frequently these changes occur after the initial loss of OM permeability, thereby reflecting a mixture of caspase-mediated and caspase-independent damages, including the opening of the PTP.…”

Section: The Mitochondrial Pathway Of Apoptosismentioning

confidence: 99%

“…25,[44][45][46][47] Oxidative phosphorylation (oxphos) takes place within the IM. 25,48,49 Because of the crucial importance of oxphos in producing cellular ATP, which is also essential for apoptosis signaling (apoptosome formation, see below), genuine apoptotic stimuli normally do not affect the properties of the IM. However, a number of drugs and agents are able to activate a multiprotein complex that promotes the formation of a large channel in the IM, the so-called permeability transition pore (PTP).…”

Section: The Mitochondrial Pathway Of Apoptosismentioning

confidence: 99%

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Death receptor signals to the mitochondria

Khosravi‐Far¹

2004

Cancer Biology & Therapy

175

144

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ACKNOWLEDGEMENTSThe suggestions of R. Shalini are most appreciated. Work in Khosravi-Far laboratory is supported by Public Health Service grant, 1 HL080192 from the National Institute of Health, DAMD, 17-02-10298 and DAMD, 17-02-10299 from the Department of Defense and RSG 03-012-01-CCG from American Cancer Society. Review Death Receptor Signals to Mitochondria ABSTRACTApoptosis is the best-characterized form of programmed cell death (PCD) and is of fundamental importance in tissue homeostasis. In mammalian systems, there are two major pathways that are involved in the initiation of apoptosis: the "extrinsic" death receptor pathway and the "intrinsic" mitochondrial pathway. Although these pathways act independently to initiate the death machinery in some cellular systems, in many cell types, including numerous tumor cells, there is delicate coordination and cross talk between the extrinsic and intrinsic pathways, which leads to the activation of the executioner caspase cascade. Additionally, there appears to be a fine balance between the caspasemediated arm of death receptor signaling that engages mitochondria and the caspaseindependent arm that promotes vacuole proliferation in many cells. Here, we review our current knowledge about the layers of complexity that are posed by the interactions between death receptor-induced pathways and how they influence mitochondria to regulate cellular life and death decisions.

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Section: The Mitochondrial Pathway Of Apoptosismentioning

confidence: 99%

Section: The Mitochondrial Pathway Of Apoptosismentioning

confidence: 99%

Death receptor signals to the mitochondria

Khosravi‐Far¹

2004

Cancer Biology & Therapy

175

144

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“…It has been reported that PARP-1 hyperactivation prompts mitochondria dysfunction, which in turn releases apoptosis-inducing factor (AIF) from the mitochondria to the nucleus (29,30). The involvement of c-Jun N-terminal kinase has recently been demonstrated in caspaseindependent cell death by several groups of investigators (31)(32)(33). Receptor-interacting protein 1 (RIP1) and TNF receptorassociated factor 2 (TRAF2) are known to play important roles in cellular responses to TNF and TNF family members, and both were shown to be required for TNF-induced caspase-independent cell death (24,34).…”

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confidence: 99%

Autophagy Contributes to Caspase-independent Macrophage Cell Death

Kim

et al. 2006

Journal of Biological Chemistry

211

169

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Macrophage cell death plays a role in many physiological and pathophysiological conditions. Previous work has shown that macrophages can undergo caspase-independent cell death, and this process is associated with Nur77 induction, which is involved in inducing chromatin condensation and DNA fragmentation. Here we show that autophagy is a cytosolic event that controls caspase-independent macrophage cell death. Autophagy was induced in macrophages treated with lipopolysaccharides (LPSs) and the pan-caspase inhibitor benzyloxycarbonylVal-Ala-Asp (Z-VAD), and the inhibition of autophagy by either chemical inhibitors or by the RNA interference knockdown of beclin (a protein required for autophagic body formation) inhibited caspase-independent macrophage cell death. We also found an increase in poly(ADP-ribose) (PAR) polymerase (PARP) activation and reactive oxygen species (ROS) production in LPS ؉ Z-VAD-treated macrophages, and both are involved in caspase-independent macrophage cell death. We further determined that the formation of autophagic bodies in macrophages occurs downstream of PARP activation, and PARP activation occurs downstream of ROS production. Using macrophages in which receptor-interacting protein 1 (RIP1) was knocked down by small interfering RNA, and macrophages isolated from Toll/ interleukin-1 receptor-domain-containing adaptor inducing IFN-␤ (TRIF)-deficient mice, we found that TRIF and RIP1 function upstream of ROS production in LPS ؉ Z-VAD-treated macrophages. We also found that Z-VAD inhibits LPS-induced RIP1 cleavage, which may contribute to ROS over-production in macrophages. This paper reveals that TRIF, RIP1, and ROS production, as well as PARP activation, are involved in inducing autophagy, which contributes to caspase-independent macrophage cell death.

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“…Two MAPKKK (MEKK1 and ASK1) and one MAPKK (MKK4) have been implicated in RNS-induced JNK activation. 7,29,30 However, little is known about the signaling mechanism upstream of MAPKKK in RNS-mediated JNK activation. In this study, we provide unequivocal evidence showing the critical role of TRAF2 upstream of ASK1 in RNS-mediated JNK activation.…”

Section: Discussionmentioning

confidence: 99%

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

Zhang

et al. 2007

Cell Death Differ

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At present, the signaling pathways controlling reactive nitrogen species (RNS)-induced non-apoptotic cell death are relatively less understood. In this work, various RNS donors are found to induce caspase-independent non-apoptotic cell death in mouse embryonic fibroblasts (MEF). In search of the molecular mechanisms, we first established the role of c-Jun N-terminal kinase (JNK) in RNS-induced non-apoptotic cell death. RNS readily activate JNK, and the jnk1À/À MEF are resistant to RNS-induced cell death. Moreover, the reconstitution of JNK1 effectively restores the sensitivity to RNS. Next, we identified tumor necrosis factor receptor-associated factor 2 (TRAF2) and apoptosis signal-regulating kinase 1 (ASK1) as the essential upstream molecules for RNS-induced JNK activation and cell death. RNS fail to activate JNK and induce cell death in traf2À/À MEF; and reconstitution of TRAF2 effectively restores the responsiveness of traf2À/À MEF to RNS. Moreover, RNS-induced ASK1 activation is impaired in traf2À/À cells and overexpression of a mutant ASK1 protein suppresses RNS-induced cell death in wild-type MEF cells. Last, we explored the signaling events upstream of TRAF2 and found that translocation of TRAF2 and JNK1 onto membrane lipid rafts is required for RNS-mediated JNK1 activation and cell death. Taken together, data from our study reveal a novel signaling pathway regulating RNS-induced JNK1 activation and non-apoptotic cell death.

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

Cited by 52 publications

References 70 publications

Death receptor signals to the mitochondria

Death receptor signals to the mitochondria

Autophagy Contributes to Caspase-independent Macrophage Cell Death

Signaling pathways from membrane lipid rafts to JNK1 activation in reactive nitrogen species-induced non-apoptotic cell death

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