Glutathione oxidation in response to intracellular H2O2: Key but overlapping roles for dehydroascorbate reductases
Autor: | Andrée Tuzet, Gilles Chatel-Innocenti, Marie Sylviane Rahantaniaina, Graham Noctor, Hélène Vanacker, Shengchun Li, Amna Mhamdi |
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Přispěvatelé: | Institut des Sciences des Plantes de Paris-Saclay (IPS2 (UMR_9213 / UMR_1403)), Institut National de la Recherche Agronomique (INRA)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS)-Université Paris Diderot - Paris 7 (UPD7)-Université Paris-Saclay-Université Paris-Sud - Paris 11 (UP11), Ecologie fonctionnelle et écotoxicologie des agroécosystèmes (ECOSYS), Institut National de la Recherche Agronomique (INRA)-AgroParisTech, Université Paris-Saclay, Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Centre National de la Recherche Scientifique (CNRS)-Université d'Évry-Val-d'Essonne (UEVE)-Institut National de la Recherche Agronomique (INRA), Institut National de la Recherche Agronomique (INRA)-Université Paris-Sud - Paris 11 (UP11)-Université Paris Diderot - Paris 7 (UPD7)-Université d'Évry-Val-d'Essonne (UEVE)-Centre National de la Recherche Scientifique (CNRS), Unité Mixte de Recherche 9213/Unité Mixte de Recherche 1403, Institute of Plant Sciences Paris-Saclay, Institut des Sciences des Plantes de Paris-Saclay ( IPS2 ), Institut National de la Recherche Agronomique ( INRA ) -Université Paris-Sud - Paris 11 ( UP11 ) -Université Paris-Saclay-Centre National de la Recherche Scientifique ( CNRS ), Ecologie fonctionnelle et écotoxicologie des agroécosystèmes ( ECOSYS ), AgroParisTech-Institut National de la Recherche Agronomique ( INRA ), Université Paris Saclay |
Jazyk: | angličtina |
Rok vydání: | 2017 |
Předmět: |
0106 biological sciences
0301 basic medicine GPX1 GPX3 [SDV]Life Sciences [q-bio] Glutathione reductase hydrogen peroxide Plant Science Biology GPX4 01 natural sciences GPX6 03 medical and health sciences chemistry.chemical_compound Glutaredoxin oxidative stress glutathione glutathione S-transferase [ SDV ] Life Sciences [q-bio] peroxiredoxin Glutathione ascorbate 030104 developmental biology Glutathione S-transferase Biochemistry chemistry biology.protein Antioxidant 010606 plant biology & botany |
Zdroj: | Plant Signaling and Behavior Plant Signaling and Behavior, Taylor & Francis, 2017, 12 (8), pp.e1356531. ⟨10.1080/15592324.2017.1356531⟩ Plant Signaling and Behavior, 2017, 12 (8), pp.e1356531. ⟨10.1080/15592324.2017.1356531⟩ Plant signaling & behavior Plant signaling & behavior, 2017, 12 (8), pp.e1356531. 〈10.1080/15592324.2017.1356531〉 |
ISSN: | 1559-2316 1559-2324 |
DOI: | 10.1080/15592324.2017.1356531⟩ |
Popis: | Glutathione is a pivotal molecule in oxidative stress, during which it is potentially oxidized by several pathways linked to H2O2 detoxification. We have investigated the response and functional importance of 3 potential routes for glutathione oxidation pathways mediated by glutathione S-transferases (GST), glutaredoxin-dependent peroxiredoxins (PRXII), and dehydroascorbate reductases (DHAR) in Arabidopsis during oxidative stress. Loss-of-function gstU8, gstU24, gstF8, prxIIE and prxIIF mutants as well as double gstU8 gstU24, gstU8 gstF8, gstU24 gstF8, prxIIE prxIIF mutants were obtained. No mutant lines showed marked changes in their phenotype and glutathione profiles in comparison to the wild-type plants in either optimal conditions or oxidative stress triggered by catalase inhibition. By contrast, multiple loss of DHAR functions markedly decreased glutathione oxidation triggered by catalase deficiency. To assess whether this effect was mediated directly by loss of DHAR enzyme activity, or more indirectly by upregulation of other enzymes involved in glutathione and ascorbate recycling, we measured expression of glutathione reductase (GR) and expression and activity of monodehydroascorbate reductases (MDHAR). No evidence was obtained that either GRs or MDHARs were upregulated in plants lacking DHAR function. Hence, interplay between different DHARs appears to be necessary to couple ascorbate and glutathione pools and to allow glutathione-related signaling during enhanced H2O2 metabolism. |
Databáze: | OpenAIRE |
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