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PMID: 16723122,10225417 ROS are generated through multiple sources in the cell, such as the electron transport chain in mitochondria, ionizing radiations and through enzymes producing superoxide anion such as phagocytic and non-phagocytic NADPH oxidases , lipoxygenases and cycloxygenases.

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PMID: 16723122,6254151 ROS are generated through multiple sources in the cell, such as the electron transport chain in mitochondria, ionizing radiations and through enzymes producing superoxide anion such as phagocytic and non-phagocytic NADPH oxidases , lipoxygenases and cycloxygenases.

indirect

PMID: 16723122,10029572,10488060,12147646 ROS are generated through multiple sources in the cell, such as the electron transport chain in mitochondria, ionizing radiations and through enzymes producing superoxide anion such as phagocytic and non-phagocytic NADPH oxidases , lipoxygenases and cycloxygenases.

indirect

PMID: 16723122,10029572,10488060,12147646 ROS are generated through multiple sources in the cell, such as the electron transport chain in mitochondria, ionizing radiations and through enzymes producing superoxide anion such as phagocytic and non-phagocytic NADPH oxidases , lipoxygenases and cycloxygenases.

PMID: 16723122 In the resting state, NF-kB is sequestered in the cytoplasm of the cell through its tight associationwith inhibitory proteins called IkBs

PMID; 16723122,12421671,10795740 The classical NF-kB-activating pathway is induced by a variety of innate and adaptative immunity mediators, such as proinflammatory cytokines (TNFa, IL-1b, Toll-like receptors (TLRs) and antigen receptors (TCR, BCR) ligation PMID: 16723122,9915703 The ligation of TNFR1 by trimeric TNFa leads to the aggregation of the receptor and dissociation of silencer of death domain (SODD), an inhibitor of TNFR1 activity, which allows binding of TNFR-associated death domain protein (TRADD protein)

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PMID: 16723122,9657155,9346241 Whereas all these NF-kB inducers signal through different receptors and adaptor proteins, they all converge to the activation of the so called IkB-kinase (IKK) complex, which includes the scaffold protein NF-kB essential modulator (NEMO, also called IKKg, IKKa and IKKb kinases.

PMID; 16723122,12421671,10795740 The classical NF-kB-activating pathway is induced by a variety of innate and adaptative immunity mediators, such as proinflammatory cytokines (TNFa, IL-1b, Toll-like receptors (TLRs) and antigen receptors (TCR, BCR) ligation

PMID; 16723122,16343886 The classical NF-kB-activating pathway is induced by a variety of innate and adaptative immunity mediators, such as proinflammatory cytokines (TNFa, IL-1b, Toll-like receptors (TLRs) and antigen receptors (TCR, BCR) ligation

PMID; 16723122,15134788,15145317,16439988 The classical NF-kB-activating pathway is induced by a variety of innate and adaptative immunity mediators, such as proinflammatory cytokines (TNFa, IL-1b, Toll-like receptors (TLRs) and antigen receptors (TCR, BCR) ligation

PMID; 16723122,12421671,10795740 The classical NF-kB-activating pathway is induced by a variety of innate and adaptative immunity mediators, such as proinflammatory cytokines (TNFa, IL-1b, Toll-like receptors (TLRs) and antigen receptors (TCR, BCR) ligation

indirect

PMID: 16723122,9657155,9346241 Whereas all these NF-kB inducers signal through different receptors and adaptor proteins, they all converge to the activation of the so called IkB-kinase (IKK) complex, which includes the scaffold protein NF-kB essential modulator (NEMO, also called IKKg, IKKa and IKKb kinases.

indirect

PMID: 16723122,9657155,9346241 Whereas all these NF-kB inducers signal through different receptors and adaptor proteins, they all converge to the activation of the so called IkB-kinase (IKK) complex, which includes the scaffold protein NF-kB essential modulator (NEMO, also called IKKg, IKKa and IKKb kinases.

indirect

PMID: 16723122,9657155,9346241 Whereas all these NF-kB inducers signal through different receptors and adaptor proteins, they all converge to the activation of the so called IkB-kinase (IKK) complex, which includes the scaffold protein NF-kB essential modulator (NEMO, also called IKKg, IKKa and IKKb kinases.

indirect

PMID: 16723122,9657155,9346241 Whereas all these NF-kB inducers signal through different receptors and adaptor proteins, they all converge to the activation of the so called IkB-kinase (IKK) complex, which includes the scaffold protein NF-kB essential modulator (NEMO, also called IKKg, IKKa and IKKb kinases.

indirect

PMID: 16723122 Once activated by phosphorylation, the IKK complex phosphorylates IkBa on Ser32 and Ser36, which is subsequently ubiquitinated and degraded via the proteasome pathway

PMID: 16723122 Once activated by phosphorylation, the IKK complex phosphorylates IkBa on Ser32 and Ser36, which is subsequently ubiquitinated and degraded via the proteasome pathway PMID: 16723122 They showed that, whereas NAC and PDTC efficiently blocked TNF-induced IkBa degradation and NF-kB activation,the more potent antioxidants epigallocatechin-gallate (EGCG) and Vitamin E analog Trolox failed to inhibit TNF-stimulated NF-kB activation, suggesting that the effect of NAC and PDTC on NF-kB signalling does not rely on their antioxidant capacities, but rather acts by inhibiting a crucial step in TNF signalling. PMID: 16723122 PDTC is likely to inhibit IkB-ubiquitin ligase activity.

PMID: 16723122 Once activated by phosphorylation, the IKK complex phosphorylates IkBa on Ser32 and Ser36, which is subsequently ubiquitinated and degraded via the proteasome pathway PMID: 16723122 They showed that, whereas NAC and PDTC efficiently blocked TNF-induced IkBa degradation and NF-kB activation,the more potent antioxidants epigallocatechin-gallate (EGCG) and Vitamin E analog Trolox failed to inhibit TNF-stimulated NF-kB activation, suggesting that the effect of NAC and PDTC on NF-kB signalling does not rely on their antioxidant capacities, but rather acts by inhibiting a crucial step in TNF signalling.

PMID: 16723122 The freed NF-kB then translocates into the nucleus where it activates the transcription of target genes such as cytokines, chemokines, adhesion molecules and inhibitors of apoptosis

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PMID: 16723122 The freed NF-kB then translocates into the nucleus where it activates the transcription of target genes such as cytokines, chemokines, adhesion molecules and inhibitors of apoptosis

indirect

PMID: 16723122 The freed NF-kB then translocates into the nucleus where it activates the transcription of target genes such as cytokines, chemokines, adhesion molecules and inhibitors of apoptosis

indirect

PMID: 16723122 The freed NF-kB then translocates into the nucleus where it activates the transcription of target genes such as cytokines, chemokines, adhesion molecules and inhibitors of apoptosis

indirect

PMID: 16723122 The freed NF-kB then translocates into the nucleus where it activates the transcription of target genes such as cytokines, chemokines, adhesion molecules and inhibitors of apoptosis

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PMID: 16723122,12352969 It is induced by B-cell activating factor (BAFF) , lymphotoxin b (LTb), CD40 ligand and human T cell leukemia (HTLV) and Epstein-Barr (EBV) virus. It enhances NF-kB inducing kinase (NIK)- and IKKa-dependent processing of p100 into p52, which binds DNA in association with its partners, like RelB.

PMID: 16723122,9657155,9346241 Whereas all these NF-kB inducers signal through different receptors and adaptor proteins, they all converge to the activation of the so called IkB-kinase (IKK) complex, which includes the scaffold protein NF-kB essential modulator (NEMO, also called IKKg, IKKa and IKKb kinases.

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PMID: 16723122,12387745 It is induced by B-cell activating factor (BAFF) , lymphotoxin b (LTb), CD40 ligand and human T cell leukemia (HTLV) and Epstein-Barr (EBV) virus. It enhances NF-kB inducing kinase (NIK)- and IKKa-dependent processing of p100 into p52, which binds DNA in association with its partners, like RelB.

indirect

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PMID: 16723122,12374738 It is induced by B-cell activating factor (BAFF) , lymphotoxin b (LTb), CD40 ligand and human T cell leukemia (HTLV) and Epstein-Barr (EBV) virus. It enhances NF-kB inducing kinase (NIK)- and IKKa-dependent processing of p100 into p52, which binds DNA in association with its partners, like RelB.

PMID: 16723122 It enhances NF-kB inducing kinase (NIK)- and IKKa-dependent processing of p100 into p52, which binds DNA in association with its partners, like RelB.

PMID: 16723122 It enhances NF-kB inducing kinase (NIK)- and IKKa-dependent processing of p100 into p52, which binds DNA in association with its partners, like RelB.

PMID: 16723122 It enhances NF-kB inducing kinase (NIK)- and IKKa-dependent processing of p100 into p52, which binds DNA in association with its partners, like RelB.

indirect

PMID: 16723122,15592513 a recent study in Jurkat leukemic cells has shown that NF-kB activation by H2O2 induces Bfl-1, which, in turn, attenuates Fas-mediated apoptosis

PMID: 16723122,15592513 a recent study in Jurkat leukemic cells has shown that NF-kB activation by H2O2 induces Bfl-1, which, in turn, attenuates Fas-mediated apoptosis

indirect

PMID: 16723122,10754328 Furthermore, the IkBa degradation mechanism appears to be proteasome-independent, but instead relies on a calpain-mediated digestion after phophorylation on S/T in the so-called PEST sequence of the inhibitor

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PMID: 16723122,11231305,8797825 NF-kB activation induced by tyrosine phosphorylation of IkBa was also observed after pervanadate (a potent tyrosine phosphatase inhibitor) and hypoxia/reoxygenation treatment PMID: 16723122,11231305 TCR-associated tyrosine kinases p56Lck and ZAP-70 were required for pervanadate-induced IkBa tyrosine phosphorylation, without showing that these kinases indeed phosphorylate IkBa directly PMID: 16723122,12429743 In that case, the tyrosine kinase c-Src has been reported to be responsible for IkBa tyrosine phosphorylation

indirect

PMID: 16723122,12711606 Recently,Takada et al. reported that Syk tyrosine kinase was required for H2O2-induced IkBa tyrosine phosphorylation and NF-kB activation, and was capable of phosphorylating IkBa in vitro, suggesting that Syk may be the terminal tyrosine kinase responsible for IkBa tyrosine phosphorylation

indirect

PMID: 16723122,16619039 Unexpectedly, micromolar amounts of H2O2 were shown indeed capable of inducing IKK activation in these cell lines, leading to a classical IkBa phosphorylation on Ser32 and 36

PMID: 16723122,16619039 Unexpectedly, micromolar amounts of H2O2 were shown indeed capable of inducing IKK activation in these cell lines, leading to a classical IkBa phosphorylation on Ser32 and 36

indirect

PMID: 16723122,10995586 SHIP-1, a lipid phosphatase, acts by dephosphorylating the membranebound PtdIns(3,4,5)P3, generated by PI3Kinase, and has thus been described as a negative regulator of immune receptor, cytokine and growth factor receptor signalling

indirect

PMID: 16723122,10995586 SHIP-1, a lipid phosphatase, acts by dephosphorylating the membranebound PtdIns(3,4,5)P3, generated by PI3Kinase, and has thus been described as a negative regulator of immune receptor, cytokine and growth factor receptor signalling

indirect

PMID: 16723122 First, activated Src induces Abl-mediated phophorylation of PKD at Y463 in the PH domain.

indirect

PMID: 16723122 First, activated Src induces Abl-mediated phophorylation of PKD at Y463 in the PH domain.This facilitates release of the PH domain, which exposes the catalytic domain and activation loop residues to a second phosphorylation by PKCd on S738/S742. This induces a fully activated PKD which, in turn, activates the IKK complex

indirect

PMID: 16723122 First, activated Src induces Abl-mediated phophorylation of PKD at Y463 in the PH domain.This facilitates release of the PH domain, which exposes the catalytic domain and activation loop residues to a second phosphorylation by PKCd on S738/S742. This induces a fully activated PKD which, in turn, activates the IKK complex

indirect

PMID: 16723122 First, activated Src induces Abl-mediated phophorylation of PKD at Y463 in the PH domain.This facilitates release of the PH domain, which exposes the catalytic domain and activation loop residues to a second phosphorylation by PKCd on S738/S742. This induces a fully activated PKD which, in turn, activates the IKK complex

indirect

PMID: 16723122,11479295 Korn et al. reported that, in this case, H2O2 is capable of inhibiting TNF-induced NF-kB activation in lung epithelial cells by reducing IKKb activity through oxidation of cysteine residues in the IKK complex PMID: 16723122,16344117 Other works demonstrated that ammonia monochloramine (NH2Cl) and glycine chloramine (GlyCl), two others neutrophils-derived oxidants, but not TauCl, were capable of inhibiting TNFinduced NF-kB activation via the same molecular mechanism

PMID: 16723122,11479295 Korn et al. reported that, in this case, H2O2 is capable of inhibiting TNF-induced NF-kB activation in lung epithelial cells by reducing IKKb activity through oxidation of cysteine residues in the IKK complex

PMID: 16723122,10333500 HOCl is a strong oxidant that kills phagocytosed bacteria, but can also react with amines to produce chloramines and N-chlorinated derivatives which have long lifetimes PMID: 16723122 Among these chloramines, taurine chloramine (TauCl) is generated in great amount in HOClproducing neutrophils because these cells contain high concentrations of taurine, a free amino acid not incorporated in proteins.

indirect

PMID: 16723122,9787133 HOCl is formed from H2O2 and Cl ion by myeloperoxidase

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PMID: 16723122,11490015 For example, TauCl was shown to decrease LPSinduced NF-kB activation and IKK activity in alveolar macrophages, resulting in inhibition of iNOS and TNFa gene expression

indirect

PMID: 16723122,11490015 For example, TauCl was shown to decrease LPSinduced NF-kB activation and IKK activity in alveolar macrophages, resulting in inhibition of iNOS and TNFa gene expression

indirect

PMID: 16723122,11490015 For example, TauCl was shown to decrease LPSinduced NF-kB activation and IKK activity in alveolar macrophages, resulting in inhibition of iNOS and TNFa gene expression

indirect

PMID: 16723122,11490015 For example, TauCl was shown to decrease LPSinduced NF-kB activation and IKK activity in alveolar macrophages, resulting in inhibition of iNOS and TNFa gene expression

PMID: 16723122,11983684 The molecular mechanism of this inhibition relied on oxidation of IkBa methionine 45, which renders the inhibitor resistant to TNF-induced degradation

indirect

PMID: 16723122,11983684 The molecular mechanism of this inhibition relied on oxidation of IkBa methionine 45, which renders the inhibitor resistant to TNF-induced degradation

PMID: 16723122,2154753 Peroxinitrite is formed by the reaction of nitric oxide (NO) with superoxide

PMID: 16723122,9374458,9371760,10854325 IL-1b is a potent pro-inflammatory cytokine that exerts its effects by binding to its receptor (IL1-R1) on the plasma membrane. This binding induces the recruitment to the receptor cytoplasmic tail of adaptator and effector proteins, including IL-1RacP, MyD88 and Tollip

PMID: 16723122,9374458,9371760,10854325 IL-1b is a potent pro-inflammatory cytokine that exerts its effects by binding to its receptor (IL1-R1) on the plasma membrane. This binding induces the recruitment to the receptor cytoplasmic tail of adaptator and effector proteins, including IL-1RacP, MyD88 and Tollip

PMID: 16723122,9374458,9371760,10854325 IL-1b is a potent pro-inflammatory cytokine that exerts its effects by binding to its receptor (IL1-R1) on the plasma membrane. This binding induces the recruitment to the receptor cytoplasmic tail of adaptator and effector proteins, including IL-1RacP, MyD88 and Tollip

PMID: 16723122,9430229,11518704 MyD88 then mediates the recruitment of the interleukin-1 receptorassociated kinase (IRAK) family members to the IL-1R, which, in turn, recruit TRAF6

PMID: 16723122,9430229,11518704 MyD88 then mediates the recruitment of the interleukin-1 receptorassociated kinase (IRAK) family members to the IL-1R, which, in turn, recruit TRAF6

PMID: 16723122,11460167 Then, TRAF6 recruits TAK1 that mediates phosphorylation of the IKK complex, a crucial step in NF-kB activation

indirect

PMID: 16723122,11460167 Then, TRAF6 recruits TAK1 that mediates phosphorylation of the IKK complex, a crucial step in NF-kB activation

PMID: 16723122 It binds to its cellular TNFR1 receptor, which triggers signalling cascades that activate NF-kB and AP-1 transcription factors.

PMID: 16723122,9915703 The ligation of TNFR1 by trimeric TNFa leads to the aggregation of the receptor and dissociation of silencer of death domain (SODD), an inhibitor of TNFR1 activity, which allows binding of TNFR-associated death domain protein (TRADD protein)

PMID: 16723122,9915703 The ligation of TNFR1 by trimeric TNFa leads to the aggregation of the receptor and dissociation of silencer of death domain (SODD), an inhibitor of TNFR1 activity, which allows binding of TNFR-associated death domain protein (TRADD protein)

PMID: 16723122,12787559 Although many members of the TRAF family have been implicated in TNF signalling, it appears that both TRAF2 and TRAF5 have a role in NF-kB activation by TNFa

PMID: 16723122,10755617 RIP1 functions as a scaffold protein notably through its direct binding to NEMO, which allows the recruitment of the IKK complex in TNF signalling

PMID: 16723122,10755617 RIP1 functions as a scaffold protein notably through its direct binding to NEMO, which allows the recruitment of the IKK complex in TNF signalling

indirect

PMID: 16723122 These results are reinforced by the observation that, whereas NAC does not inhibit IL-1 or TPA-induced IkBa degradation, PDTC does

PMID: 16723122 These results are reinforced by the observation that, whereas NAC does not inhibit IL-1 or TPA-induced IkBa degradation, PDTC does

indirect

PMID: 16723122 These results are reinforced by the observation that, whereas NAC does not inhibit IL-1 or TPA-induced IkBa degradation, PDTC does

PMID:16723122 They showed that ROS (induced by cigarette smoke or H2O2 treatment) reduce HDAC2 expression

PMID: 16723122,12368228 Finally, it should also be noted that NAC was shown to inhibit p65 ser536 phosphorylation, suggesting that post-translationalmodifications affecting p65 are also redox-sensitive

indirect

PMID: 16723122,14743220 In that respect, they identified growth arrest and DNA damage-inducing protein 45b (GADD45b) and X chromosome-linked IAP (XIAP) as capable of inhibiting JNK signalling by inactivating MEKK7

PMID: 16723122 They showed that TNFinduced ROS production is responsible for sustained JNK activation in NF-kB-activation deficient cells,whereas wildtype cells exhibited neither ROS production nor sustained JNK activation upon TNF challenge.

indirect

PMID: 16723122 In fact, several laboratories have independently reported that NF-kB down-regulates JNK activation by suppressing TNF-induced ROS accumulation PMID: 16723122 Moreover, prolonged JNK activation is inhibited by pre-treatment of NF-kB-defective cells with the antioxidants BHA or NAC, suggesting that ROS are key messengers of prolonged JNK activation after TNF induction.

PMID: 16723122,14751757,: 1475175 Upon binding of TLR4 to LPS, the cytoplasmic region of TLR4 recruits MyD88, which links TLR4 to IRAK and TRAF6 that mediates NF-kB activation

PMID: 16723122 Upon binding of TLR4 to LPS, the cytoplasmic region of TLR4 recruits MyD88, which links TLR4 to IRAK and TRAF6 that mediates NF-kB activation

PMID: 16723122 Upon binding of TLR4 to LPS, the cytoplasmic region of TLR4 recruits MyD88, which links TLR4 to IRAK and TRAF6 that mediates NF-kB activation

indirect

PMID: 16723122 Upon binding of TLR4 to LPS, the cytoplasmic region of TLR4 recruits MyD88, which links TLR4 to IRAK and TRAF6 that mediates NF-kB activation PMID: 16723122,14764725,15039334 Pre-treatment of neutrophils with NAC or atocopherol prevented LPS-induced NF-kB activation and the production of pro-inflammatory cytokines, and NAC and DMSO were reported to block NF-kB activation and IL-8 secretion in monocyte-like THP-1 cells challenged with LPS

PMID:16723122,1698311,7681082,2402637 CD14, which is expressed on the surface and in the cytoplasm (sCD14) of monocytes/macrophages and neutrophils, has also been reported to play a key role in the recognition of LPS and in downstream cytokine release, notably through its interaction with LPS-binding protein (LBP), which binds the lipid A region of LPS and aids LPS to dock at the TLR4

PMID:16723122,1698311,7681082,2402637 CD14, which is expressed on the surface and in the cytoplasm (sCD14) of monocytes/macrophages and neutrophils, has also been reported to play a key role in the recognition of LPS and in downstream cytokine release, notably through its interaction with LPS-binding protein (LBP), which binds the lipid A region of LPS and aids LPS to dock at the TLR4

PMID:16723122,1698311,7681082,2402637 CD14, which is expressed on the surface and in the cytoplasm (sCD14) of monocytes/macrophages and neutrophils, has also been reported to play a key role in the recognition of LPS and in downstream cytokine release, notably through its interaction with LPS-binding protein (LBP), which binds the lipid A region of LPS and aids LPS to dock at the TLR4

PMID: 16723122 They showed that, in HEK293T cells, LPS-induced ROS generation and NF-kB activation are mediated by direct interaction of TLR4 with NADPH oxidase 4 (Nox4

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PMID: 16723122,14743220 In that respect, they identified growth arrest and DNA damage-inducing protein 45b (GADD45b) and X chromosome-linked IAP (XIAP) as capable of inhibiting JNK signalling by inactivating MEKK7

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PMID: 16723122 Indeed, ROS inactivate MAP kinase phosphatases (MKPs, which are known to suppress JNK activation) by oxidizing critical residues in their phosphatase domain, which leads to prolonged JNK activation (Fig. 5). Moreover, oxidized MKPs are rapidly degraded by the ubiquitin-proteasome pathway

PMID: 16723122 Indeed, ROS inactivate MAP kinase phosphatases (MKPs, which are known to suppress JNK activation) by oxidizing critical residues in their phosphatase domain, which leads to prolonged JNK activation (Fig. 5). Moreover, oxidized MKPs are rapidly degraded by the ubiquitin-proteasome pathway

PMID: 16723122 Indeed, ROS inactivate MAP kinase phosphatases (MKPs, which are known to suppress JNK activation) by oxidizing critical residues in their phosphatase domain, which leads to prolonged JNK activation (Fig. 5). Moreover, oxidized MKPs are rapidly degraded by the ubiquitin-proteasome pathway

indirect

PMID: 16723122,15864310 It should, however, be noted that ROS production after LPS challenge has been showed to mediate the formation of a complex between TRAF6 and the redox-sensitive ASK1, which, in turn, triggers p38 activation, another downstream target of LPS signalling

indirect

PMID: 16723122,15864310 It should, however, be noted that ROS production after LPS challenge has been showed to mediate the formation of a complex between TRAF6 and the redox-sensitive ASK1, which, in turn, triggers p38 activation, another downstream target of LPS signalling

indirect

PMID: 16723122,15864310 It should, however, be noted that ROS production after LPS challenge has been showed to mediate the formation of a complex between TRAF6 and the redox-sensitive ASK1, which, in turn, triggers p38 activation, another downstream target of LPS signalling

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PMID: 16723122 Using blocking antibodies, they also reported that the ROS-dependent Rac1 activation is independent of the CD14 receptor, suggesting that alternative pathways contribute to NF-kB activation by LPS