GlutaredoxinV1, Main, Exploration, bibRecord, 000845

Methylselenol formed by spontaneous methylation of selenide is a superior selenium substrate to the thioredoxin and glutaredoxin systems.

Identifieur interne : 000845 ( Main/Exploration ); précédent : 000844; suivant : 000846

Methylselenol formed by spontaneous methylation of selenide is a superior selenium substrate to the thioredoxin and glutaredoxin systems.

Auteurs : Aristi P. Fernandes [Suède] ; Marita Wallenberg ; Valentina Gandin ; Sougat Misra ; Francesco Tisato ; Cristina Marzano ; Maria Pia Rigobello ; Sushil Kumar ; Mikael Björnstedt

Source :

PloS one [ 1932-6203 ] ; 2012.

RBID : pubmed:23226364

Descripteurs français

KwdFr :
- Adémétionine (métabolisme), Adémétionine (pharmacologie), Antinéoplasiques (métabolisme), Antinéoplasiques (pharmacologie), Composés du sélénium (métabolisme), Composés du sélénium (pharmacologie), Composés organiques du sélénium (métabolisme), Composés organiques du sélénium (pharmacologie), Cytochromes c (métabolisme), Disulfures (métabolisme), Espace intracellulaire (métabolisme), Glutarédoxines (métabolisme), Glutathion (analogues et dérivés), Glutathion (métabolisme), Humains (MeSH), Liaison aux protéines (MeSH), Lignée cellulaire tumorale (MeSH), Méthanol (analogues et dérivés), Méthanol (métabolisme), Méthanol (pharmacologie), Méthylation (MeSH), Oxydoréduction (MeSH), Superoxydes (métabolisme), Survie cellulaire (effets des médicaments et des substances chimiques), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme), Transport biologique (MeSH).
MESH :
- analogues et dérivés : Glutathion, Méthanol.
- effets des médicaments et des substances chimiques : Survie cellulaire.
- métabolisme : Adémétionine, Antinéoplasiques, Composés du sélénium, Composés organiques du sélénium, Cytochromes c, Disulfures, Espace intracellulaire, Glutarédoxines, Glutathion, Méthanol, Superoxydes, Thioredoxin-disulfide reductase, Thiorédoxines.
- pharmacologie : Adémétionine, Antinéoplasiques, Composés du sélénium, Composés organiques du sélénium, Méthanol.
- Humains, Liaison aux protéines, Lignée cellulaire tumorale, Méthylation, Oxydoréduction, Transport biologique.

English descriptors

KwdEn :
- Antineoplastic Agents (metabolism), Antineoplastic Agents (pharmacology), Biological Transport (MeSH), Cell Line, Tumor (MeSH), Cell Survival (drug effects), Cytochromes c (metabolism), Disulfides (metabolism), Glutaredoxins (metabolism), Glutathione (analogs & derivatives), Glutathione (metabolism), Humans (MeSH), Intracellular Space (metabolism), Methanol (analogs & derivatives), Methanol (metabolism), Methanol (pharmacology), Methylation (MeSH), Organoselenium Compounds (metabolism), Organoselenium Compounds (pharmacology), Oxidation-Reduction (MeSH), Protein Binding (MeSH), S-Adenosylmethionine (metabolism), S-Adenosylmethionine (pharmacology), Selenium Compounds (metabolism), Selenium Compounds (pharmacology), Superoxides (metabolism), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
MESH :
- chemical , analogs & derivatives : Glutathione, Methanol.
- chemical , metabolism : Antineoplastic Agents, Cytochromes c, Disulfides, Glutaredoxins, Glutathione, Methanol, Organoselenium Compounds, S-Adenosylmethionine, Selenium Compounds, Superoxides, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , pharmacology : Antineoplastic Agents, Methanol, Organoselenium Compounds, S-Adenosylmethionine, Selenium Compounds.
- drug effects : Cell Survival.
- metabolism : Intracellular Space.
- Biological Transport, Cell Line, Tumor, Humans, Methylation, Oxidation-Reduction, Protein Binding.

Abstract

Naturally occurring selenium compounds like selenite and selenodiglutathione are metabolized to selenide in plants and animals. This highly reactive form of selenium can undergo methylation and form monomethylated and multimethylated species. These redox active selenium metabolites are of particular biological and pharmacological interest since they are potent inducers of apoptosis in cancer cells. The mammalian thioredoxin and glutaredoxin systems efficiently reduce selenite and selenodiglutathione to selenide. The reactions are non-stoichiometric aerobically due to redox cycling of selenide with oxygen and thiols. Using LDI-MS, we identified that the addition of S-adenosylmethionine (SAM) to the reactions formed methylselenol. This metabolite was a superior substrate to both the thioredoxin and glutaredoxin systems increasing the velocities of the nonstoichiometric redox cycles three-fold. In vitro cell experiments demonstrated that the presence of SAM increased the cytotoxicity of selenite and selenodiglutathione, which could neither be explained by altered selenium uptake nor impaired extra-cellular redox environment, previously shown to be highly important to selenite uptake and cytotoxicity. Our data suggest that selenide and SAM react spontaneously forming methylselenol, a highly nucleophilic and cytotoxic agent, with important physiological and pharmacological implications for the highly interesting anticancer effects of selenium.

DOI: 10.1371/journal.pone.0050727
PubMed: 23226364
PubMed Central: PMC3511371

Affiliations:

Links toward previous steps (curation, corpus...)

to stream Main, to step Corpus: 000786
to stream Main, to step Curation: 000786

Le document en format XML

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<term>Antineoplastic Agents (pharmacology)</term>
<term>Biological Transport (MeSH)</term>
<term>Cell Line, Tumor (MeSH)</term>
<term>Cell Survival (drug effects)</term>
<term>Cytochromes c (metabolism)</term>
<term>Disulfides (metabolism)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (analogs & derivatives)</term>
<term>Glutathione (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Intracellular Space (metabolism)</term>
<term>Methanol (analogs & derivatives)</term>
<term>Methanol (metabolism)</term>
<term>Methanol (pharmacology)</term>
<term>Methylation (MeSH)</term>
<term>Organoselenium Compounds (metabolism)</term>
<term>Organoselenium Compounds (pharmacology)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>Protein Binding (MeSH)</term>
<term>S-Adenosylmethionine (metabolism)</term>
<term>S-Adenosylmethionine (pharmacology)</term>
<term>Selenium Compounds (metabolism)</term>
<term>Selenium Compounds (pharmacology)</term>
<term>Superoxides (metabolism)</term>
<term>Thioredoxin-Disulfide Reductase (metabolism)</term>
<term>Thioredoxins (metabolism)</term>
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<term>Adémétionine (pharmacologie)</term>
<term>Antinéoplasiques (métabolisme)</term>
<term>Antinéoplasiques (pharmacologie)</term>
<term>Composés du sélénium (métabolisme)</term>
<term>Composés du sélénium (pharmacologie)</term>
<term>Composés organiques du sélénium (métabolisme)</term>
<term>Composés organiques du sélénium (pharmacologie)</term>
<term>Cytochromes c (métabolisme)</term>
<term>Disulfures (métabolisme)</term>
<term>Espace intracellulaire (métabolisme)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (analogues et dérivés)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Liaison aux protéines (MeSH)</term>
<term>Lignée cellulaire tumorale (MeSH)</term>
<term>Méthanol (analogues et dérivés)</term>
<term>Méthanol (métabolisme)</term>
<term>Méthanol (pharmacologie)</term>
<term>Méthylation (MeSH)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Superoxydes (métabolisme)</term>
<term>Survie cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Thioredoxin-disulfide reductase (métabolisme)</term>
<term>Thiorédoxines (métabolisme)</term>
<term>Transport biologique (MeSH)</term>
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<keywords scheme="MESH" type="chemical" qualifier="analogs & derivatives" xml:lang="en"><term>Glutathione</term>
<term>Methanol</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antineoplastic Agents</term>
<term>Cytochromes c</term>
<term>Disulfides</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Methanol</term>
<term>Organoselenium Compounds</term>
<term>S-Adenosylmethionine</term>
<term>Selenium Compounds</term>
<term>Superoxides</term>
<term>Thioredoxin-Disulfide Reductase</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antineoplastic Agents</term>
<term>Methanol</term>
<term>Organoselenium Compounds</term>
<term>S-Adenosylmethionine</term>
<term>Selenium Compounds</term>
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<term>Méthanol</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Survival</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Survie cellulaire</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Intracellular Space</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Adémétionine</term>
<term>Antinéoplasiques</term>
<term>Composés du sélénium</term>
<term>Composés organiques du sélénium</term>
<term>Cytochromes c</term>
<term>Disulfures</term>
<term>Espace intracellulaire</term>
<term>Glutarédoxines</term>
<term>Glutathion</term>
<term>Méthanol</term>
<term>Superoxydes</term>
<term>Thioredoxin-disulfide reductase</term>
<term>Thiorédoxines</term>
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<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Adémétionine</term>
<term>Antinéoplasiques</term>
<term>Composés du sélénium</term>
<term>Composés organiques du sélénium</term>
<term>Méthanol</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Biological Transport</term>
<term>Cell Line, Tumor</term>
<term>Humans</term>
<term>Methylation</term>
<term>Oxidation-Reduction</term>
<term>Protein Binding</term>
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<keywords scheme="MESH" xml:lang="fr"><term>Humains</term>
<term>Liaison aux protéines</term>
<term>Lignée cellulaire tumorale</term>
<term>Méthylation</term>
<term>Oxydoréduction</term>
<term>Transport biologique</term>
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<front><div type="abstract" xml:lang="en">Naturally occurring selenium compounds like selenite and selenodiglutathione are metabolized to selenide in plants and animals. This highly reactive form of selenium can undergo methylation and form monomethylated and multimethylated species. These redox active selenium metabolites are of particular biological and pharmacological interest since they are potent inducers of apoptosis in cancer cells. The mammalian thioredoxin and glutaredoxin systems efficiently reduce selenite and selenodiglutathione to selenide. The reactions are non-stoichiometric aerobically due to redox cycling of selenide with oxygen and thiols. Using LDI-MS, we identified that the addition of S-adenosylmethionine (SAM) to the reactions formed methylselenol. This metabolite was a superior substrate to both the thioredoxin and glutaredoxin systems increasing the velocities of the nonstoichiometric redox cycles three-fold. In vitro cell experiments demonstrated that the presence of SAM increased the cytotoxicity of selenite and selenodiglutathione, which could neither be explained by altered selenium uptake nor impaired extra-cellular redox environment, previously shown to be highly important to selenite uptake and cytotoxicity. Our data suggest that selenide and SAM react spontaneously forming methylselenol, a highly nucleophilic and cytotoxic agent, with important physiological and pharmacological implications for the highly interesting anticancer effects of selenium.</div>
</front>
</TEI>
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<DateCompleted><Year>2013</Year>
<Month>05</Month>
<Day>23</Day>
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<DateRevised><Year>2018</Year>
<Month>11</Month>
<Day>13</Day>
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<PubDate><Year>2012</Year>
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<Title>PloS one</Title>
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<ArticleTitle>Methylselenol formed by spontaneous methylation of selenide is a superior selenium substrate to the thioredoxin and glutaredoxin systems.</ArticleTitle>
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<Abstract><AbstractText>Naturally occurring selenium compounds like selenite and selenodiglutathione are metabolized to selenide in plants and animals. This highly reactive form of selenium can undergo methylation and form monomethylated and multimethylated species. These redox active selenium metabolites are of particular biological and pharmacological interest since they are potent inducers of apoptosis in cancer cells. The mammalian thioredoxin and glutaredoxin systems efficiently reduce selenite and selenodiglutathione to selenide. The reactions are non-stoichiometric aerobically due to redox cycling of selenide with oxygen and thiols. Using LDI-MS, we identified that the addition of S-adenosylmethionine (SAM) to the reactions formed methylselenol. This metabolite was a superior substrate to both the thioredoxin and glutaredoxin systems increasing the velocities of the nonstoichiometric redox cycles three-fold. In vitro cell experiments demonstrated that the presence of SAM increased the cytotoxicity of selenite and selenodiglutathione, which could neither be explained by altered selenium uptake nor impaired extra-cellular redox environment, previously shown to be highly important to selenite uptake and cytotoxicity. Our data suggest that selenide and SAM react spontaneously forming methylselenol, a highly nucleophilic and cytotoxic agent, with important physiological and pharmacological implications for the highly interesting anticancer effects of selenium.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Fernandes</LastName>
<ForeName>Aristi P</ForeName>
<Initials>AP</Initials>
<AffiliationInfo><Affiliation>Division of Pathology F46, Department of Laboratory Medicine, Karolinska Institutet, Karolinska University Hospital Huddinge, Stockholm, Sweden. aristi.fernandes@ki.se</Affiliation>
</AffiliationInfo>
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<Author ValidYN="Y"><LastName>Wallenberg</LastName>
<ForeName>Marita</ForeName>
<Initials>M</Initials>
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<Author ValidYN="Y"><LastName>Gandin</LastName>
<ForeName>Valentina</ForeName>
<Initials>V</Initials>
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<Author ValidYN="Y"><LastName>Misra</LastName>
<ForeName>Sougat</ForeName>
<Initials>S</Initials>
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<Author ValidYN="Y"><LastName>Tisato</LastName>
<ForeName>Francesco</ForeName>
<Initials>F</Initials>
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<Author ValidYN="Y"><LastName>Marzano</LastName>
<ForeName>Cristina</ForeName>
<Initials>C</Initials>
</Author>
<Author ValidYN="Y"><LastName>Rigobello</LastName>
<ForeName>Maria Pia</ForeName>
<Initials>MP</Initials>
</Author>
<Author ValidYN="Y"><LastName>Kumar</LastName>
<ForeName>Sushil</ForeName>
<Initials>S</Initials>
</Author>
<Author ValidYN="Y"><LastName>Björnstedt</LastName>
<ForeName>Mikael</ForeName>
<Initials>M</Initials>
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<NameOfSubstance UI="C019003">methaneselenol</NameOfSubstance>
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<NameOfSubstance UI="D012436">S-Adenosylmethionine</NameOfSubstance>
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<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
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   |texte=   Methylselenol formed by spontaneous methylation of selenide is a superior selenium substrate to the thioredoxin and glutaredoxin systems.
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	Serveur d'exploration sur la glutarédoxine
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Serveur d'exploration sur la glutarédoxine

Methylselenol formed by spontaneous methylation of selenide is a superior selenium substrate to the thioredoxin and glutaredoxin systems.

Methylselenol formed by spontaneous methylation of selenide is a superior selenium substrate to the thioredoxin and glutaredoxin systems.

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