GSH-Mediated <i>S</i>-Transarylation of a Quinone Glyceraldehyde-3-Phosphate Dehydrogenase Conjugate

Miura, Takashi; Kakehashi, Hidenao; Shinkai, Yasuhiro; Egara, Yuko; Hirose, Ryoji; Cho, Arthur K.; Kumagai, Yoshito

doi:10.1021/tx200025y

Cited by 31 publications

(35 citation statements)

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“…1) (Kumagai et al, 2012;Miura et al, 2011a). For example, sensor proteins containing reactive nucleophiles undergo arylation by 1,2-NQ, thereby disrupting their function (Endo et al, 2011(Endo et al, , 2007Iwamoto et al, 2007;Miura et al, 2011aMiura et al, , 2011bSumi et al, 2010). In a previous study, we found that several unidentified proteins expressed by human pulmonary epithelial A549 cells are modified after exposure to 1,2-NQ (Miura et al, 2011b).…”

Section: Introductionmentioning

confidence: 94%

“…SDS-PAGE and subsequent immunoblot analysis were performed as reported previously (Miura et al, 2011a). The protein concentrations were determined using the Bio-Rad Protein assay kit (Bio-Rad, Richmond, CA, USA) or the bicinchoninic acid (BCA) protein assay reagent (Pierce Biotechnology Inc., Rockford, IL, USA), incorporating bovine serum albumin as a standard.…”

Section: Western Blottingmentioning

confidence: 99%

“…Accumulating evidence indicates that 1,2-NQ reacts with protein thiols via the Michael reaction to form 1,2-dihydroxynaphthalene-protein adducts, which are rapidly auto-oxidized to 1,2-NQ-protein adducts ( Fig. 1) (Kumagai et al, 2012;Miura et al, 2011a). For example, sensor proteins containing reactive nucleophiles undergo arylation by 1,2-NQ, thereby disrupting their function (Endo et al, 2011(Endo et al, , 2007Iwamoto et al, 2007;Miura et al, 2011aMiura et al, , 2011bSumi et al, 2010).…”

Section: Introductionmentioning

confidence: 99%

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Peroxiredoxin 6 is a molecular target for 1,2-naphthoquinone, an atmospheric electrophile, in human pulmonary epithelial A549 cells

et al. 2011

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-1,2-Naphthoquinone (1,2-NQ) is an electrophile found in the atmosphere, which reacts readily with protein nucleophiles to form a stable protein adduct. Peroxiredoxin 6 (Prdx6) is predominantly expressed in lung tissue and functions in antioxidant defense by facilitating the repair of damaged cell membranes via reduction of peroxidized phospholipids. In the present study, human A549 pulmonary epithelial cells were exposed to 1,2-NQ to explore whether 1,2-NQ can bind covalently to Prdx6, thereby disrupting its catalytic activity. Two-dimensional SDS/PAGE followed by western blot analysis with a specific antibody against 1,2-NQ showed that Prdx6 was covalently modified by 1,2-NQ. Using purified human Prdx6, it was found that 1,2-NQ bound covalently to Prdx6 through Cys47, Lys144 and Cys91, resulting in a significant reduction in phospholipase A 2 activity. These results suggest that arylation of Prdx6 by 1,2-NQ may, at least in part, be involved in the cellular toxicity induced by 1,2-NQ.

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Section: Introductionmentioning

confidence: 94%

Section: Western Blottingmentioning

confidence: 99%

Section: Introductionmentioning

confidence: 99%

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Peroxiredoxin 6 is a molecular target for 1,2-naphthoquinone, an atmospheric electrophile, in human pulmonary epithelial A549 cells

et al. 2011

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“…Using anti-1,2-NQ, it has been demonstrated that protein tyrosine phosphatase 1B (PTP1B) (Iwamoto et al, 2007), cAMP response element-binding protein (Endo et al, 2007), inhibitory κB kinase β (Sumi et al, 2010), Kelch-like ECH-associated protein 1 (Keap1) (Miura et al, 2011c), glyceraldehyde-3-phosphate dehydrogenase (Miura et al, 2011a(Miura et al, , 2011b, peroxiredoxin 6 (Takayama et al, 2011) and thioredoxin1 are molecular targets of 1,2-NQ for covalent modification. More importantly, it has been shown that activations of epidermal growth factor receptor and NF-E2-related factor 2 (Nrf2) are attributable to S-arylation of PTP1B through Cys121 and of Keap1 through Cys151 by 1,2-NQ, respectively (Iwamoto et al, 2007;Kobayashi et al, 2009).…”

Section: Introductionmentioning

confidence: 99%

A method for detecting covalent modification of sensor proteins associated with 1,4-naphthoquinone-induced activation of electrophilic signal transduction pathways

et al. 2012

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-While metabolic activation of naphthalene, yielding 1,2-naphthoquinone (1,2-NQ) and 1,4-NQ that can covalently bind to cellular proteins, has been recognized to be associated with its toxicity, the current consensus is that such electrophile-mediated covalent modification of sensor proteins with thiolate ions is also involved in activation of cellular signal transduction pathways for cellular protection against reactive materials. In the present study, we developed an immunochemical assay to detect cellular proteins adducted by 1,4-NQ. Dot blot analysis indicated that the antibody prepared against 1,4-NQ recognized the naphthalene moiety with the para-dicarbonyl group, rather than with the ortho-dicarbonyl group. Furthermore, little cross-reactivity of para-quinones with either a different number of aromatic rings (n = 1) or substituent groups was observed. With this specific antibody against 1,4-NQ, we identified nine target proteins of 1,4-NQ following exposure of human epithelial carcinoma cell line A431 to 1,4-NQ. Among them, heat shock protein 90 (HSP90) and HSP70 are of interest because covalent modification of these chaperones causes activation of heat shock factor-1, which plays a role in the cellular response against electrophiles such as 1,4-NQ. Thus, our method, which does not use radiolabeled compounds, would be applicable for exploring activation of electrophilic signal transduction pathways coupled to covalent modification of sensor proteins during exposure to naphthalene as well as 1,4-NQ.

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“…NRF2 binds to a cognate DNA regulatory element termed the antioxidant response element and up-regulates its target genes. Of interest, 1,2-NQ also activates NRF2 through covalent modification of Keap1 (10). Collectively, it seems likely that there are different adaptive responses against environmental electrophiles, such as 1,2-NQ, via activating signal transduction pathways.…”

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confidence: 99%

Critical Contribution of Nuclear Factor Erythroid 2-related Factor 2 (NRF2) to Electrophile-induced Interleukin-11 Production

Nishina

Deguchi

Miura

et al. 2017

Journal of Biological Chemistry

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Edited by Joel GottesfeldNuclear factor erythroid 2-related factor 2 (NRF2) is a transcription factor that plays a crucial role in protection of cells from electrophile-induced toxicity through up-regulating phase II detoxifying enzymes and phase III transporters. We previously reported that oxidative stress induces up-regulation of interleukin-11 (IL-11), a member of the IL-6 family that ameliorates acetaminophen-induced liver toxicity. However, a role for IL-11 in protection of cells from electrophile-induced toxicity remains unclear. Here we show that an environmental electrophile, 1,2-naphthoquinone (1,2-NQ), but not 15d-prostaglandin J 2 (PGJ 2 ) or tert-butylhydroxyquinone (tBHQ), induced IL-11 production. Consistent with a crucial role for prolonged ERK activation in H 2 O 2 -induced IL-11 production, 1,2-NQ, but not 15d-PGJ 2 or tBHQ, elicited prolonged ERK activation. Conversely, inhibition of the ERK pathway by a MEK inhibitor completely blocked 1,2-NQ-induced IL-11 production at both protein and mRNA levels, further substantiating an intimate cross-talk between ERK activation and 1,2-NQ-induced IL-11 production. Promoter analysis of the Il11 gene revealed that two AP-1 sites were essential for 1,2-NQ-induced promoter activities. Among various members of the AP-1 family, Fra-1 was upregulated by 1,2-NQ, and its up-regulation was blocked by a MEK inhibitor. Although NRF2 was not required for H 2 O 2 -induced IL11 up-regulation, NRF2 was essential for 1,2-NQ-induced IL11 up-regulation by increasing Fra-1 proteins possibly through promoting mRNA translation of FOSL1. Finally, intraperitoneal administration of 1,2-NQ induced body weight loss in wild-type mice, which was further exacerbated in Il11ra1 ؊/؊ mice compared with Il11ra1 ؉/؊ mice. Together, both Fra-1 and NRF2 play crucial roles in IL-11 production that protects cells from 1,2-NQ intestinal toxicity.Electrophiles are electron-deficient compounds that can accept an electron pair to form a covalent bond with its reaction partner (nucleophile), resulting in adducts of macromolecules (e.g. proteins, lipids, and DNA) (1). Such reactive species have been shown to be involved in stress, aging, and cancer through modification of various signaling molecules. It is well recognized that endogenous electrophiles, such as 8-nitro-cGMP, 15-deoxy-prostaglandin J 2 (15d-PGJ 2 ), 3 and nitrated fatty acids, are produced during oxidative stress and inflammation (2, 3) and then activate redox signal transduction pathways associated with up-regulation of antioxidant and anti-inflammation genes (1-3). In addition, there are a variety of electrophiles in the environment (4, 5). For example, particles with an aerodynamic diameter of 2.5 m or less (PM2.5) and tobacco smoke (6) contain an atmospheric electrophile, 1,2-naphtoquinone (1,2-NQ), that activates epidermal growth factor receptor (EGFR) through S-arylation of Cys-121 of protein-tyrosine phosphatase 1B (PTP1B) (7). A transcription factor, NF-E2-related factor 2 (NRF2), is activated and attenuates electrophile-ind...

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GSH-Mediated S-Transarylation of a Quinone Glyceraldehyde-3-Phosphate Dehydrogenase Conjugate

Cited by 31 publications

References 39 publications

Peroxiredoxin 6 is a molecular target for 1,2-naphthoquinone, an atmospheric electrophile, in human pulmonary epithelial A549 cells

Peroxiredoxin 6 is a molecular target for 1,2-naphthoquinone, an atmospheric electrophile, in human pulmonary epithelial A549 cells

A method for detecting covalent modification of sensor proteins associated with 1,4-naphthoquinone-induced activation of electrophilic signal transduction pathways

Critical Contribution of Nuclear Factor Erythroid 2-related Factor 2 (NRF2) to Electrophile-induced Interleukin-11 Production

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