Cadmium increases the activity levels of glutamate dehydrogenase and cysteine synthase in Chlamydomonas reinhardtii

Domínguez, María José Tacoronte; Gutiérrez, Facundo; Léon, Rosa; Vílchez, Carlos; Vega, José M.; Vigara, Javier

doi:10.1016/s0981-9428(03)00114-1

Cited by 39 publications

(26 citation statements)

References 23 publications

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“…80 It caused induction of enzymes of S assimilation pathway in plants. 19,36,37 Cd-led upregulation of S metabolism pathway genes has been reported in Saccharomyces cerevisiae, 53 and induction of enzymes involved in the sulfate assimilation pathway in higher plants. 19,80,81 Sultr1;1 and Sultr2;1 (which encode two sulfate transporters) have also been found to be upregulated after 2 or 6 h of Cd-treatment and 12-24 h after sulfate-depletion.…”

Section: Cadmium Stress and Sulfur Metabolismmentioning

confidence: 96%

“…11,[29][30][31][32][33][34][35] Alternatively, Cd-caused induction of enzymes of S assimilation pathway has been reported in many plants. 19,36,37 Therefore, the regulation of S assimilation may be necessary to ensure an adequate supply of S compounds required for heavy metal tolerance. However, Cd is a non-redox active metal, but it induces the generation of reactive oxygen species (ROS) including superoxide radical (O 2…”

Section: Cadmium Stress Tolerance In Crop Plantsmentioning

confidence: 99%

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Cadmium stress tolerance in crop plants

Gill

Tuteja

2011

Plant Signaling & Behavior

324

137

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Section: Cadmium Stress and Sulfur Metabolismmentioning

confidence: 96%

Section: Cadmium Stress Tolerance In Crop Plantsmentioning

confidence: 99%

Cadmium stress tolerance in crop plants

Gill

Tuteja

2011

Plant Signaling & Behavior

324

137

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“…However a concomitant decrease in the activity of enzymes involved in primary nitrogen assimilation (GS/GOGAT) was observed in both leaves and roots (Chaffei et al, 2003 and this work). Inhibition of GS activity had been described in maize, pea and barley seedlings (Nussabum et al, 1988;Chugh et al, 1992;Boussama et al, 1999;Domingez et al, 2003). We showed that, in tomato, such inhibition was closely linked to a decrease in the cognate proteins.…”

Section: Discussionmentioning

confidence: 62%

Physiological and biochemical effects of cadmium toxicity in enzymes involved in nitrogen and amino—acid metabolism in tomato plants

Chaffei-Haouari

Carrayol

Ghorbel

et al. 2009

Acta Botanica Gallica

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Abstract.-The activities of several enzymes related to amino-acid metabolism were investigated in tomato plants (Lycopersicon esculentum Mill. 63/5F1) in control and treated leaves and roots. Glutamine synthetase and glutamate synthase ferredoxine dependent activities rapidly declined in stress condition. In presence of cadmium, the decline of glutamine synthetase activity was retarded, while the activity of glutamate synthase significantly and more rapid declined. The activity of NADH-dependent glutamate dehydrogenase was markedly increased in presence of cadmium. Western blots analysis from cadmium treated plants, showed a decrease in chloroplastic GS (GS2) protein and an increase in cytosolic GS (GS1) and glutamate dehydrogenase (GDH) proteins. The activities of phosphoenol pyruvate carboxylase and NADP-dependent isocitrate dehydrogenase also increased in both organs of plantes treated. The activity of NAD and NADP-dependent malate dehydrogenase were decreased especially in leaves.Key words : cadmium -glutamine synthetase -glutamate synthase -glutamate dehydrogenase -tomato.Résumé.-Les activités de la majorité des enzymes impliquées dans le méta-bolisme d'amino-acides et de l'azote ont été examinées chez les plantules de tomate (Lycopersicon esculentum Mill. 63/5 F1) contrôles et traités dans les feuilles et les racines. Les activités de la glutamine synthétase et la glutamate synthase ferredoxine dépendante ont diminué rapidement en condition de stress. En présence du cadmium, la diminution de l'activité de la glutamine synthétase a été retardée, alors que l'activité de la glutamate synthase est significative. L'activité de la glutamate déshydrogénase NADH-dépendante a remarquablement augmenté. Les analyses de Western blot à partir des plantules traitées ont montré une baisse dans la protéine chloroplastique GS (GS2) et une augmentation des protéines GS cytosolique (GS1) et de la glutamate déshydrogénase (GDH). Les activités de la phosphoénol pyruvate carboxylase NADP-dépendante et isocitrate déshydrogénase ont augmenté dans les deux organes des plantes traitées. L'activité malate déshydrogénase NAD et NADPdépendant ont diminué spécialement dans les feuilles.Mots clés : cadmium -glutamine synthétase -glutamate synthase -glutamate déshydrogénase -tomate.received June 17, 2008, accepted December 12, 2008 Abbreviations -Cd = cadmium, GS = glutamine synthètase, Fd-GOGAT = ferredoxin dependent glutamate synthase, GDH = glutamate dehydrogenase, ICDH = isocitrate dehydrogenase, MDH = malate dehydrogenase, NAD-MDH = NAD-dependent MDH, NADP-MDH = NADP-dependent MDH, PEPC = phosphoenol pyruvate carboxylase.

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“…The source of glutathione biosynthesis is cystein, which is consequently utilized for next sulphur compounds biosynthesis (Hall 2002). In addition, glutathione participates in oxidativereduction reactions where oxidised glutathion (glutathione disulfide) originates (Dominguez et al 2003). Results obtained demonstrate well-evident differences in various cadmium(II) ions concentrations with sulphur or without sulphur supplementation and show the importance of sulphur source in cultivation media to glutathione-derived compounds biosynthesis.…”

Section: Reduced and Oxidized Glutathionementioning

confidence: 88%

“…Some studies predicate the cysteine importance in detoxification of certain heavy metal ions, such as cobalt (Oven et al 2002). Cysteine molecule further serves as the substrate for GSH and PC2 biosynthesis (Dominguez et al 2003). Moreover, the effect of sulphates presence in cultivation media as suitable source of sulphur for cysteine biosynthesis is obvious (Fig.…”

Section: Cysteinementioning

confidence: 99%

The role of sulphur in cadmium(II) ions detoxification demonstrated in in vitro model: Dionaea muscipula Ell.

et al. 2008

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Fertilization by phosphorus and also nitrogen fertilizers are the main source of cadmium soil contamination. Cadmium is relatively easily taken up by plants and then consequently enters their food chain. We investigated whether the cultivation medium with or without sulphates supplement affects the synthesis of protective low molecular mass thiols such as cysteine, reduced glutathione, oxidized glutathione and phytochelatins (PC2) in Dionaea muscipula treated with cadmium(II) ions at 0, 1, 5, 10, 25, 50, 100, 250, 500 and 1,000 lM for 6 weeks. The plants cultivated in the presence of sulphates showed higher cadmium tolerance due to faster growth and lesser number of necrosis hallmarks.Further, we utilized liquid chromatography with electrochemical detection for determination of the thiols in plant tissues. In the case of the plants cultivated on media supplemented with sulphates for 6 weeks the average PC2 level was 2,830 ng/g of fresh weight (FW). However, the plants cultivated on media without the presence of sulphates on average contained 1,160 ng PC2/g FW. Results obtained showed the positive effect of sulphur supplementation in cadmium detoxification processes in plants. In addition to thiol content, we also determined level of majority secondary metabolite of Venus flytrap, naphthoquinone plumbagin. Generally, the presence of sulphates in the media enhanced the protective mechanism and did not affect directly the synthesis of secondary metabolite plumbagin.

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Cadmium increases the activity levels of glutamate dehydrogenase and cysteine synthase in Chlamydomonas reinhardtii

Cited by 39 publications

References 23 publications

Cadmium stress tolerance in crop plants

Cadmium stress tolerance in crop plants

Physiological and biochemical effects of cadmium toxicity in enzymes involved in nitrogen and amino—acid metabolism in tomato plants

The role of sulphur in cadmium(II) ions detoxification demonstrated in in vitro model: Dionaea muscipula Ell.

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