Redox-sensitive YFP sensors for monitoring dynamic compartment-specific glutathione redox state

Banach-Latapy, Agata; He, Tiantian; Dardalhon, M.; Vernis, Laurence; Chanet, Roland; Huang, Meng‐Er

doi:10.1016/j.freeradbiomed.2013.07.033

Cited by 25 publications

(16 citation statements)

References 44 publications

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“…DUOX1 has been originally identified in the thyroid gland (12 (6) (Fig. 3B), which was recently shown to be associated with nuclear redox changes (22) (Fig. 3C).…”

Section: Discussionmentioning

confidence: 95%

NADPH oxidase DUOX1 promotes long-term persistence of oxidative stress after an exposure to irradiation

Ameziane-El-Hassani

Talbot

Santos

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

109

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Ionizing radiation (IR) causes not only acute tissue damage, but also late effects in several cell generations after the initial exposure. The thyroid gland is one of the most sensitive organs to the carcinogenic effects of IR, and we have recently highlighted that an oxidative stress is responsible for the chromosomal rearrangements found in radio-induced papillary thyroid carcinoma. Using both a human thyroid cell line and primary thyrocytes, we investigated the mechanism by which IR induces the generation of reactive oxygen species (ROS) several days after irradiation. We focused on NADPH oxidases, which are specialized ROS-generating enzymes known as NOX/DUOX. Our results show that IR induces delayed NADPH oxidase DUOX1-dependent H 2 O 2 production in a dose-dependent manner, which is sustained for several days. We report that p38 MAPK, activated after IR, increased DUOX1 via IL-13 expression, leading to persistent DNA damage and growth arrest. Pretreatment of cells with catalase, a scavenger of H 2 O 2 , or DUOX1 down-regulation by siRNA abrogated IR-induced DNA damage. Analysis of human thyroid tissues showed that DUOX1 is elevated not only in human radio-induced thyroid tumors, but also in sporadic thyroid tumors. Taken together, our data reveal a key role of DUOX1-dependent H 2 O 2 production in long-term persistent radio-induced DNA damage. Our data also show that DUOX1-dependent H 2 O 2 production, which induces DNA double-strand breaks, can cause genomic instability and promote the generation of neoplastic cells through its mutagenic effect.ionizing radiation | oxidative stress | NADPH oxidase | thyroid |

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“…DUOX1 has been originally identified in the thyroid gland (12 (6) (Fig. 3B), which was recently shown to be associated with nuclear redox changes (22) (Fig. 3C).…”

Section: Discussionmentioning

confidence: 95%

NADPH oxidase DUOX1 promotes long-term persistence of oxidative stress after an exposure to irradiation

Ameziane-El-Hassani

Talbot

Santos

et al. 2015

Proc. Natl. Acad. Sci. U.S.A.

109

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“…While it is now accepted that GSH is distributed in the cytosol, nucleus and mitochondria, it is still unclear if the regulation of the redox state by GSH in these locations bears differential features among them. The employment of compartment-targeted redox-sensitive fluorescent sensors is progressively allowing to gain insight into this fundamental question [7]. …”

Section: Glutathione Synthesismentioning

confidence: 99%

MicroRNA-mediated regulation of glutathione and methionine metabolism and its relevance for liver disease

Mato

Espinosa‐Díez

et al. 2016

Free Radical Biology and Medicine

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The discovery of the microRNA (miRNA) family of small RNAs as fundamental regulators of post-transcriptional gene expression has fostered research on their importance in every area of biology and clinical medicine. In the particular area of liver metabolism and disease, miRNAs are gaining increasing importance. By focusing on two fundamental hepatic biosynthetic pathways, glutathione and methionine, we review recent advances on the comprehension of the role of miRNAs in liver pathophysiology and more specifically of models of hepatic cholestasis/fibrosis and hepatocellular carcinoma.

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“…A disulfide bond has been engineered into green fluorescent proteins (GFPs) or yellow fluorescent proteins (YFPs) to develop redox potential probes, that, upon equilibrium with the ambient thiol/disulfide compounds, could be used to measure redox potentials in cells in real time . The L106C/V233 mutant described here is responsive to ambient thiol/disulfide redox potential change.…”

Section: Resultsmentioning

confidence: 99%

Lid mobility in lipase SMG1 validated using a thiol/disulfide redox potential probe

Guo

Popowicz

et al. 2016

FEBS Open Bio

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Most lipases possess a lid domain above the catalytic site that is responsible for their activation. Lipase SMG1 from Malassezia globose CBS 7966 ( Malassezia globosa LIP1), is a mono‐ and diacylglycerol lipase with an atypical loop‐like lid domain. Activation of SMG1 was proposed to be solely through a gating mechanism involving two residues (F278 and N102). However, through disulfide bond cross‐linking of the lid, this study shows that full activation also requires mobility of the lid domain, contrary to a previous proposal. The newly introduced disulfide bond makes lipase SMG1 eligible as a ratiometric thiol/disulfide redox potential probe, when it is coupled with chromogenic substrates. This redox‐switch lipase could also be of potential use in cascade biocatalysis.

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Redox-sensitive YFP sensors for monitoring dynamic compartment-specific glutathione redox state

Cited by 25 publications

References 44 publications

NADPH oxidase DUOX1 promotes long-term persistence of oxidative stress after an exposure to irradiation

NADPH oxidase DUOX1 promotes long-term persistence of oxidative stress after an exposure to irradiation

MicroRNA-mediated regulation of glutathione and methionine metabolism and its relevance for liver disease

Lid mobility in lipase SMG1 validated using a thiol/disulfide redox potential probe

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