Reactive Oxygen Species-Induced Activation of the MAP Kinase Signaling Pathways

McCubrey, James A.; LaHair, Michelle M.; Franklin, Richard A.

doi:10.1089/ars.2006.8.1775

Cited by 680 publications

(502 citation statements)

References 187 publications

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“…In addition, ROS could function as signaling molecules to activate multiple signal transduction cascades and in turn modulate inflammatory responses [9][10][11][12]. Thus, mediators regulating oxidative stress may effectively modulate inflammation responses and improve survival in sepsis.…”

Section: Introductionmentioning

confidence: 99%

Park7 interacts with p47phox to direct NADPH oxidase-dependent ROS production and protect against sepsis

Liu

Chen

et al. 2015

Cell Res

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Inappropriate inflammation responses contribute to mortality during sepsis. Through Toll-like receptors (TLRs), reactive oxygen species (ROS) produced by NADPH oxidase could modulate the inflammation responses. Parkinson disease (autosomal recessive, early onset) 7 (Park7) has a cytoprotective role by eliminating ROS. However, whether Park7 could modulate inflammation responses and mortality in sepsis is unclear. Here, we show that, compared with wild-type mice, Park7 −/− mice had significantly increased mortality and bacterial burdens in sepsis model along with markedly decreased systemic and local inflammation, and drastically impaired macrophage phagocytosis and bacterial killing abilities. Surprisingly, LPS and phorbol-12-myristate-13-acetate stimulation failed to induce ROS and proinflammatory cytokine production in Park7 −/− macrophages and Park7-deficient RAW264.7 cells. Through its C-terminus, Park7 binds to p47 phox , a subunit of the NADPH oxidase, to promote NADPH oxidase-dependent production of ROS. Restoration of Park7 expression rescues ROS production and improves survival in LPS-induced sepsis. Together, our study shows that Park7 has a protective role against sepsis by controlling macrophage activation, NA-DPH oxidase activation and inflammation responses.

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Section: Introductionmentioning

confidence: 99%

Park7 interacts with p47phox to direct NADPH oxidase-dependent ROS production and protect against sepsis

Liu

Chen

et al. 2015

Cell Res

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“…Given that activation of JNK and p38 has been associated with oxidative stress generated by ultraviolet or gamma radiation, or by direct exposure to hydrogen peroxide (Torres and Forman, 2003;McCubrey et al 2006), the present study was aimed at determining whether DomAinduced apoptosis would involve activation of one or both of these two kinases in mouse CGNs.…”

mentioning

confidence: 99%

Apoptosis induced by domoic acid in mouse cerebellar granule neurons involves activation of p38 and JNK MAP kinases

Giordano

Klintworth

Kavanagh

et al. 2008

Neurochemistry International

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In mouse cerebellar granule neurons (CGN) the marine neurotoxin domoic acid (DomA) induces neuronal cell death, either by apoptosis or by necrosis, depending on its concentration, with apoptotic damage predominating in response to low concentrations (100 nM). DomA-induced apoptosis is due to selective activation of AMPA/kainate receptors, and is mediated by DomA-induced oxidative stress, leading to mitochondrial dysfunction and activation of caspase-3. The p38 MAP kinase and the c-Jun NH 2 -terminal protein kinase (JNK) have been shown to be preferentially activated by oxidative stress. Here we report that DomA increases p38 MAP kinase and JNK phosphorylation, and that this effect is more pronounced in CGNs from Gclm (−/−) mice, which lack the modifier subunit of glutamate-cysteine ligase, have very low glutathione (GSH) levels, and are more sensitive to DomA-induced apoptosis than CGNs from wild-type mice. The increased phosphorylation of JNK and p38 kinase was paralleled by a decreased phosphorylation of Erk 1/2. The AMPA/kainate receptor antagonist NBQX, but not the NMDA receptor antagonist MK-801, prevents DomAinduced activation of p38 and JNK kinases. Several antioxidants (GSH ethyl ester, catalase, phenylbutylnitrone) also prevent DomA-induced phosphorylation of JNK and p38 MAP kinases. Inhibitors of p38 (SB203580) and of JNK (SP600125) antagonize DomA-induced apoptosis. These results indicate the importance of oxidative stress-activated JNK and p38 MAP kinase pathways in DomA-induced apoptosis in CGNs.

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“…While inhibition of some kinases blocked or partially inhibited specific parameters related to proliferation or morphology change, our results indicate that ERK1/2 are involved in all aspects related to redox-dependent modifications on such parameters. ERK1/2 are highly sensitive to regulation by reactive species [50] , and previous works from our group indicated that these kinases are involved in the activation of matrix metalloproteinase-2 by retinol in a redoxdependent fashion [51] .…”

Section: Discussionmentioning

confidence: 94%

Retinol induces morphological alterations and proliferative focus formation through free radical-mediated activation of multiple signaling pathways

et al. 2012

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Aim: Toxicity of retinol (vitamin A) has been previously associated with apoptosis and/or cell malignant transformation. Thus, we investigated the pathways involved in the induction of proliferation, deformation and proliferative focus formation by retinol in cultured Sertoli cells of rats. Methods: Sertoli cells were isolated from immature rats and cultured. The cells were subjected to a 24-h treatment with different concentrations of retinol. Parameters of oxidative stress and cytotoxicity were analyzed. The effects of the p38 inhibitor SB203580 (10 μmol/L), the JNK inhibitor SP600125 (10 μmol/L), the Akt inhibitor LY294002 (10 μmol/L), the ERK inhibitor U0126 (10 μmol/L) the pan-PKC inhibitor GÖ6983 (10 μmol/L) and the PKA inhibitor H89 (1 μmol/L) on morphological and proliferative/transformationassociated modifications were studied. Results: Retinol (7 and 14 μmol/L) significantly increases the reactive species production in Sertoli cells. Inhibition of p38, JNK, ERK1/2, Akt, and PKA suppressed retinol-induced [ 3 H]dT incorporation into the cells, while PKC inhibition had no effect. ERK1/2 and p38 inhibition also blocked retinol-induced proliferative focus formation in the cells, while Akt and JNK inhibition partially decreased focus formation. ERK1/2 and p38 inhibition hindered transformation-associated deformation in retinol-treated cells, while other treatments had no effect. Conclusion: Our results suggest that activation of multiple kinases is responsible for morphological and proliferative changes associated to malignancy development in Sertoli cells by retinol at the concentrations higher than physiological level.

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Reactive Oxygen Species-Induced Activation of the MAP Kinase Signaling Pathways

Cited by 680 publications

References 187 publications

Park7 interacts with p47phox to direct NADPH oxidase-dependent ROS production and protect against sepsis

Park7 interacts with p47phox to direct NADPH oxidase-dependent ROS production and protect against sepsis

Apoptosis induced by domoic acid in mouse cerebellar granule neurons involves activation of p38 and JNK MAP kinases

Retinol induces morphological alterations and proliferative focus formation through free radical-mediated activation of multiple signaling pathways

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