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silene davidii/glutathione

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ArticlesClinical trialsPatents
11 results

Phytochelatin synthase catalyzes key step in turnover of glutathione conjugates.

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Conjugation of xenobiotic compounds and endogenous metabolites to glutathione is an ubiquitous process in eukaryotes. In animals, the first and rate-limiting step of glutathione-S-conjugate metabolism is characterized by the removal of the aminoterminal glutamic acid residue of glutathione. In

Glutathione Depletion Due to Copper-Induced Phytochelatin Synthesis Causes Oxidative Stress in Silene cucubalus.

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The relation between loss of glutathione due to metal-induced phytochelatin synthesis and oxidative stress was studied in the roots of copper-sensitive and tolerant Silene cucubalus (L.) Wib., resistant to 1 and 40 micromolar Cu, respectively. The amount of nonprotein sulfhydryl compounds other than

Phytochelatins, the heavy-metal-binding peptides of plants, are synthesized from glutathione by a specific gamma-glutamylcysteine dipeptidyl transpeptidase (phytochelatin synthase).

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An enzyme has been discovered and characterized from Silene cucubalus cell suspension cultures that catalyzes the transfer of the gamma-glutamylcysteine dipeptide moiety of glutathione to an acceptor glutathione molecule or a growing chain of [Glu(-Cys)](n)-Gly oligomers, thus synthesizing

Nucleotide Sequence of the Gene for a Glutathione S-Transferase from Cell Suspension Cultures of Silene cucubalus.

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Nucleotide Sequence of a cDNA Encoding a Constitutively Expressed Glutathione S-Transferase from Cell Suspension Cultures of Silene cucubalus.

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Arsenate tolerance in Silene paradoxa does not rely on phytochelatin-dependent sequestration.

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Arsenate tolerance, As accumulation and As-induced phytochelatin accumulation were compared in populations of Silene paradoxa, one from a mine site enriched in As, Cu and Zn, the other from an uncontaminated site. The mine population was significantly more arsenate-tolerant. Arsenate uptake and

Ecotype-Specific Pathways of Reactive Oxygen Species Deactivation in Facultative Metallophyte Silene Vulgaris (Moench) Garcke Treated with Heavy Metals.

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This research aimed to indicate mechanisms involved in protection against the imbalanced generation of reactive oxygen species (ROS) during heavy metals (HMs) exposition of Silene vulgaris ecotypes with different levels of metal tolerance. Specimens of non-metallicolous (NM), calamine (CAL),

Increased Zinc Tolerance in Silene vulgaris (Moench) Garcke Is Not Due to Increased Production of Phytochelatins.

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The concentration of acid-soluble thiols other than reduced glutathione (SH - GSH) increases in the roots of zinc-sensitive and zinc-tolerant Silene vulgaris (Moench) Garcke after exposure to zinc for 1 to 3 d. The concentration of SH - GSH in the roots is higher in the sensitive plants than in the

Distinct co-tolerance responses to combined salinity and cadmium exposure in metallicolous and non-metallicolous ecotypes of Silene vulgaris

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This study compared co-tolerance to salinity and cadmium and investigated its mechanisms in a facultative metallophyte Silene vulgaris originating from distinct habitats. Shoots of calamine (Cal) and non-metallicolous (N-Cal) ecotypes grown in vitro were exposed to 10 and 100 mM NaCl, 5 μM

Effects of lead, cadmium and zinc on protein changes in Silene vulgaris shoots cultured in vitro

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In the present research, Silene vulgaris as a representative species growing on both unpolluted and heavy metal (HM) polluted terrains were used to identify ecotype-specific responses to metallic stress. Growth, cell ultrastructure and element accumulations were compared between non-metallicolous

Characterization of phytochelatin synthase produced by the primitive red alga Cyanidioschyzon merolae.

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Phytochelatins (PCs), non-protein peptides with the general structure [(γ-Glu-Cys)n-Gly (n≥ 2)], are involved in the detoxification of toxic heavy metals mainly in higher plants. The synthesis of the peptides is mediated by phytochelatin synthase (PCS), which is activated by a range of heavy metals.
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