Butylated hydroxyanisole is more than a reactive oxygen species scavenger

Festjens, Nele; Kalai, Michaël; Smet, J; Meeus, Ann; Coster, Rudy Van; Saelens, Xavier; Vandenabeele, Peter

doi:10.1038/sj.cdd.4401746

Cited by 94 publications

(55 citation statements)

References 12 publications

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“…5,25 As BHA is not only a broad ROS scavenger, but also a cytosolic phospholipase A2 inhibitor, 27 we investigated the lethal contribution of each source by comparing the effects of their specific inhibition. A recent study reported that ROS generation requires recruitment of riboflavin kinase (RFK) and the NADPH oxidases Nox1 and Nox2 to TNFR1.…”

Section: Resultsmentioning

confidence: 99%

cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production

et al. 2010

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Three members of the IAP family (X-linked inhibitor of apoptosis (XIAP), cellular inhibitor of apoptosis proteins-1/-2 (cIAP1 and cIAP2)) are potent suppressors of apoptosis. Recent studies have shown that cIAP1 and cIAP2, unlike XIAP, are not direct caspase inhibitors, but block apoptosis by functioning as E3 ligases for effector caspases and receptor-interacting protein 1 (RIP1). cIAP-mediated polyubiquitination of RIP1 allows it to bind to the pro-survival kinase transforming growth factorb-activated kinase 1 (TAK1) which prevents it from activating caspase-8-dependent death, a process reverted by the deubiquitinase CYLD. RIP1 is also a regulator of necrosis, a caspase-independent type of cell death. Here, we show that cells depleted of the IAPs by treatment with the IAP antagonist BV6 are greatly sensitized to tumor necrosis factor (TNF)-induced necrosis, but not to necrotic death induced by anti-Fas, poly(I:C) oxidative stress. Specific targeting of the IAPs by RNAi revealed that repression of cIAP1 is responsible for the sensitization. Similarly, lowering TAK1 levels or inhibiting its kinase activity sensitized cells to TNF-induced necrosis, whereas repressing CYLD had the opposite effect. We show that this sensitization to death is accompanied by enhanced RIP1 kinase activity, increased recruitment of RIP1 to Fas-associated via death domain and RIP3 (which allows necrosome formation), and elevated RIP1 kinase-dependent accumulation of reactive oxygen species (ROS).In conclusion, our data indicate that cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent ROS production.

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Section: Resultsmentioning

confidence: 99%

cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production

et al. 2010

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“…29 In this respect, there is extensive documentation that mitochondrial complex Imediated ROS production contributes to necroptosis. 22,30,31 The multiple effects of BHA as a mitochondrial complex I inhibitor, oxygen radical scavenger and cPLA 2 inhibitor explain its strong antinecrotic effects on TNF-induced necroptosis. 30 BHA also completely abrogated zVAD-fmkmediated sensitization of mice to TNF lethality.…”

Section: Discussionmentioning

confidence: 99%

“…22,30,31 The multiple effects of BHA as a mitochondrial complex I inhibitor, oxygen radical scavenger and cPLA 2 inhibitor explain its strong antinecrotic effects on TNF-induced necroptosis. 30 BHA also completely abrogated zVAD-fmkmediated sensitization of mice to TNF lethality. 32 In contrast, H 2 O 2 -induced necrosis occurs independently of the abovementioned signaling pathways.…”

Section: Discussionmentioning

confidence: 99%

Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features

et al. 2009

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Necroptosis, necrosis and secondary necrosis following apoptosis represent different modes of cell death that eventually result in similar cellular morphology including rounding of the cell, cytoplasmic swelling, rupture of the plasma membrane and spilling of the intracellular content. Subcellular events during tumor necrosis factor (TNF)-induced necroptosis, H2O2-induced necrosis and anti-Fas-induced secondary necrosis were studied using high-resolution time-lapse microscopy. The cellular disintegration phase of the three types of necrosis is characterized by an identical sequence of subcellular events, including oxidative burst, mitochondrial membrane hyperpolarization, lysosomal membrane permeabilization and plasma membrane permeabilization, although with different kinetics. H2O2-induced necrosis starts immediately by lysosomal permeabilization. In contrast, during TNF-mediated necroptosis and anti-Fas-induced secondary necrosis, this is a late event preceded by a defined signaling phase. TNF-induced necroptosis depends on receptor-interacting protein-1 kinase, mitochondrial complex I and cytosolic phospholipase A(2) activities, whereas H2O2-induced necrosis requires iron-dependent Fenton reactions

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“…Besides, RIP1 has also been shown to be essential for TNFa-induced production of ceramide, the latter mediating TNFa-induced caspase-independent cell death. 39 As cPLA 2 contributes to TNFa-induced necrosis, 40 it is conceivable that a RIP1-cPLA 2 -acid sphingomyelinase pathway may lead to necrotic cell death. Indeed, cPLA 2 -mediated production of arachidonic acid activates acid sphingomyelinase, 41 promoting enhanced levels of ceramide.…”

Section: Role Of Rip1 In Death Receptor Signallingmentioning

confidence: 99%

RIP1, a kinase on the crossroads of a cell's decision to live or die

et al. 2007

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Binding of inflammatory cytokines to their receptors, stimulation of pathogen recognition receptors by pathogen-associated molecular patterns, and DNA damage induce specific signalling events. A cell that is exposed to these signals can respond by activation of NF-jB, mitogen-activated protein kinases and interferon regulatory factors, resulting in the upregulation of antiapoptotic proteins and of several cytokines. The consequent survival may or may not be accompanied by an inflammatory response. Alternatively, a cell can also activate death-signalling pathways, resulting in apoptosis or alternative cell death such as necrosis or autophagic cell death. Interplay between survival and death-promoting complexes continues as they compete with each other until one eventually dominates and determines the cell's fate. RIP1 is a crucial adaptor kinase on the crossroad of these stress-induced signalling pathways and a cell's decision to live or die. Following different upstream signals, particular RIP1-containing complexes are formed; these initiate only a limited number of cellular responses. In this review, we describe how RIP1 acts as a key integrator of signalling pathways initiated by stimulation of death receptors, bacterial or viral infection, genotoxic stress and T-cell homeostasis. Cell Death and Differentiation (2007) 14, 400-410. doi:10.1038/sj.cdd.4402085Receptor interacting protein (RIP) kinases constitute a family of seven members, all of which contain a kinase domain (KD) (Figure 1a). They are crucial regulators of cell survival and death 1 (Figure 2). Based on sequence similarities, mode of regulation and substrate specificities of their catalytic domain, RIP kinases are classified as serine/threonine kinases and are closely related to members of the interleukin-1-receptorassociated kinase (IRAK) family. RIP1 and RIP2 (CARDIAK/ RICK) also bear a C-terminal domain belonging to the death domain (DD) superfamily, namely, a DD and a caspase recruitment domain (CARD), respectively, allowing recruitment to large protein complexes initiating different signalling pathways. The unique C-terminus of RIP3 bears a RIP homotypic interaction motif (RHIM), which is also present in the intermediate domain (ID) of RIP1. This RHIM domain is sufficient for interaction of RIP1 with RIP3. 1 RIP4 (DIK/PKK) and RIP5 (SgK288) are characterized by the presence of ankyrin repeats in their C-terminal domains. 1 RIP6 (LRRK1) and RIP7 (LRRK2) are RIP members containing a leucine-rich repeat (LRR) motif 1 that may be involved in recognition of pathogen-, damage-or stress-associated molecular patterns (PAMP, DAMP, SAMP). In addition, they harbor Roc/COR domains (Ras of complex proteins/C-terminal of Roc). Binding of GTP to the GTPase-like Roc domain leads to the stimulation of LRRK1 kinase activity. 2 Mutation analysis indicated that the COR domain might be important for transmitting the stimulating signal to the KD. 2 The function of RIP6 and RIP7 is yet unknown; however, mutations in the human LRRK2 gene are associated with both fam...

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Butylated hydroxyanisole is more than a reactive oxygen species scavenger

Cited by 94 publications

References 12 publications

cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production

cIAP1 and TAK1 protect cells from TNF-induced necrosis by preventing RIP1/RIP3-dependent reactive oxygen species production

Necroptosis, necrosis and secondary necrosis converge on similar cellular disintegration features

RIP1, a kinase on the crossroads of a cell's decision to live or die

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