Serveur d'exploration sur la glutarédoxine

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Glutaredoxin 1 is a major player in copper metabolism in neuroblastoma cells.

Identifieur interne : 000657 ( Main/Exploration ); précédent : 000656; suivant : 000658

Glutaredoxin 1 is a major player in copper metabolism in neuroblastoma cells.

Auteurs : Maria Lisa De Benedetto [Italie] ; Concetta Rosa Capo ; Alberto Ferri ; Cristiana Valle ; Renato Polimanti ; Maria Teresa Carrì ; Luisa Rossi

Source :

RBID : pubmed:24041990

Descripteurs français

English descriptors

Abstract

BACKGROUND

Glutaredoxin 1 (Grx1), a small protein belonging to the thioredoxin family, is involved in redox-regulation since it catalyzes the reduction of protein disulfides and that of mixed disulfides. It was reported to modulate active copper extrusion from cells, by affecting the function of the pumps ATP7A and B. These are components of the network of protein chaperones involved in the control of the homeostasis of copper, an essential, though harmful, metal. However, the effect of Grx1 on copper levels, copper chaperones and copper-elicited cell toxicity was never investigated.

METHODS

In order to investigate the effect of Grx1 on copper metabolism, we constitutively overexpressed Grx1 in human neuroblastoma SH-SY5Y cells (SH-Grx1 cells) and assessed a number of copper-related parameters.

RESULTS

SH-Grx1 cells show a basal intracellular copper level higher than control cells, accumulate more copper upon CuSO4 treatment, but are more resistant to copper-induced toxicity. Grx1 shows copper-binding properties and copper overload produces a decrease of Grx1 enzyme activity in SH-Grx1 cells. Finally, Grx1 overexpression decreases copper accumulation in mitochondria upon copper overload and modulates the expression of copper transporter 1 (Ctr1).

CONCLUSION

Altogether, these data demonstrate that Grx1 is a major player in copper metabolism in neuronal cells.


DOI: 10.1016/j.bbagen.2013.09.008
PubMed: 24041990


Affiliations:


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


Le document en format XML

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<term>Apoptosis (MeSH)</term>
<term>Blotting, Western (MeSH)</term>
<term>Cation Transport Proteins (genetics)</term>
<term>Cation Transport Proteins (metabolism)</term>
<term>Cell Proliferation (MeSH)</term>
<term>Chromatography, Affinity (MeSH)</term>
<term>Copper (metabolism)</term>
<term>Copper Transporter 1 (MeSH)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Glutathione (metabolism)</term>
<term>Humans (MeSH)</term>
<term>Mitochondria (metabolism)</term>
<term>Mitochondria (pathology)</term>
<term>Neuroblastoma (genetics)</term>
<term>Neuroblastoma (metabolism)</term>
<term>Neuroblastoma (pathology)</term>
<term>Oxidation-Reduction (MeSH)</term>
<term>RNA, Messenger (genetics)</term>
<term>Real-Time Polymerase Chain Reaction (MeSH)</term>
<term>Reverse Transcriptase Polymerase Chain Reaction (MeSH)</term>
<term>Superoxide Dismutase (genetics)</term>
<term>Superoxide Dismutase (metabolism)</term>
<term>Superoxide Dismutase-1 (MeSH)</term>
<term>Tumor Cells, Cultured (MeSH)</term>
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<term>ARN messager (génétique)</term>
<term>Apoptose (MeSH)</term>
<term>Cellules cancéreuses en culture (MeSH)</term>
<term>Chromatographie d'affinité (MeSH)</term>
<term>Cuivre (métabolisme)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Glutathion (métabolisme)</term>
<term>Humains (MeSH)</term>
<term>Mitochondries (anatomopathologie)</term>
<term>Mitochondries (métabolisme)</term>
<term>Neuroblastome (anatomopathologie)</term>
<term>Neuroblastome (génétique)</term>
<term>Neuroblastome (métabolisme)</term>
<term>Oxydoréduction (MeSH)</term>
<term>Prolifération cellulaire (MeSH)</term>
<term>RT-PCR (MeSH)</term>
<term>Réaction de polymérisation en chaine en temps réel (MeSH)</term>
<term>Superoxide dismutase (génétique)</term>
<term>Superoxide dismutase (métabolisme)</term>
<term>Superoxide dismutase-1 (MeSH)</term>
<term>Technique de Western (MeSH)</term>
<term>Transporteurs de cations (génétique)</term>
<term>Transporteurs de cations (métabolisme)</term>
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<term>Cation Transport Proteins</term>
<term>Glutaredoxins</term>
<term>RNA, Messenger</term>
<term>Superoxide Dismutase</term>
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<term>Cation Transport Proteins</term>
<term>Copper</term>
<term>Glutaredoxins</term>
<term>Glutathione</term>
<term>Superoxide Dismutase</term>
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<term>Mitochondries</term>
<term>Neuroblastome</term>
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<term>Glutarédoxines</term>
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<term>Glutarédoxines</term>
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<term>Transporteurs de cations</term>
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<term>Mitochondria</term>
<term>Neuroblastoma</term>
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<term>Apoptosis</term>
<term>Blotting, Western</term>
<term>Cell Proliferation</term>
<term>Chromatography, Affinity</term>
<term>Copper Transporter 1</term>
<term>Humans</term>
<term>Oxidation-Reduction</term>
<term>Real-Time Polymerase Chain Reaction</term>
<term>Reverse Transcriptase Polymerase Chain Reaction</term>
<term>Superoxide Dismutase-1</term>
<term>Tumor Cells, Cultured</term>
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<term>Apoptose</term>
<term>Cellules cancéreuses en culture</term>
<term>Chromatographie d'affinité</term>
<term>Humains</term>
<term>Oxydoréduction</term>
<term>Prolifération cellulaire</term>
<term>RT-PCR</term>
<term>Réaction de polymérisation en chaine en temps réel</term>
<term>Superoxide dismutase-1</term>
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<div type="abstract" xml:lang="en">
<p>
<b>BACKGROUND</b>
</p>
<p>Glutaredoxin 1 (Grx1), a small protein belonging to the thioredoxin family, is involved in redox-regulation since it catalyzes the reduction of protein disulfides and that of mixed disulfides. It was reported to modulate active copper extrusion from cells, by affecting the function of the pumps ATP7A and B. These are components of the network of protein chaperones involved in the control of the homeostasis of copper, an essential, though harmful, metal. However, the effect of Grx1 on copper levels, copper chaperones and copper-elicited cell toxicity was never investigated.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>METHODS</b>
</p>
<p>In order to investigate the effect of Grx1 on copper metabolism, we constitutively overexpressed Grx1 in human neuroblastoma SH-SY5Y cells (SH-Grx1 cells) and assessed a number of copper-related parameters.</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>RESULTS</b>
</p>
<p>SH-Grx1 cells show a basal intracellular copper level higher than control cells, accumulate more copper upon CuSO4 treatment, but are more resistant to copper-induced toxicity. Grx1 shows copper-binding properties and copper overload produces a decrease of Grx1 enzyme activity in SH-Grx1 cells. Finally, Grx1 overexpression decreases copper accumulation in mitochondria upon copper overload and modulates the expression of copper transporter 1 (Ctr1).</p>
</div>
<div type="abstract" xml:lang="en">
<p>
<b>CONCLUSION</b>
</p>
<p>Altogether, these data demonstrate that Grx1 is a major player in copper metabolism in neuronal cells.</p>
</div>
</front>
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<AbstractText Label="BACKGROUND" NlmCategory="BACKGROUND">Glutaredoxin 1 (Grx1), a small protein belonging to the thioredoxin family, is involved in redox-regulation since it catalyzes the reduction of protein disulfides and that of mixed disulfides. It was reported to modulate active copper extrusion from cells, by affecting the function of the pumps ATP7A and B. These are components of the network of protein chaperones involved in the control of the homeostasis of copper, an essential, though harmful, metal. However, the effect of Grx1 on copper levels, copper chaperones and copper-elicited cell toxicity was never investigated.</AbstractText>
<AbstractText Label="METHODS" NlmCategory="METHODS">In order to investigate the effect of Grx1 on copper metabolism, we constitutively overexpressed Grx1 in human neuroblastoma SH-SY5Y cells (SH-Grx1 cells) and assessed a number of copper-related parameters.</AbstractText>
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<name sortKey="Carri, Maria Teresa" sort="Carri, Maria Teresa" uniqKey="Carri M" first="Maria Teresa" last="Carrì">Maria Teresa Carrì</name>
<name sortKey="Ferri, Alberto" sort="Ferri, Alberto" uniqKey="Ferri A" first="Alberto" last="Ferri">Alberto Ferri</name>
<name sortKey="Polimanti, Renato" sort="Polimanti, Renato" uniqKey="Polimanti R" first="Renato" last="Polimanti">Renato Polimanti</name>
<name sortKey="Rossi, Luisa" sort="Rossi, Luisa" uniqKey="Rossi L" first="Luisa" last="Rossi">Luisa Rossi</name>
<name sortKey="Valle, Cristiana" sort="Valle, Cristiana" uniqKey="Valle C" first="Cristiana" last="Valle">Cristiana Valle</name>
</noCountry>
<country name="Italie">
<noRegion>
<name sortKey="De Benedetto, Maria Lisa" sort="De Benedetto, Maria Lisa" uniqKey="De Benedetto M" first="Maria Lisa" last="De Benedetto">Maria Lisa De Benedetto</name>
</noRegion>
</country>
</tree>
</affiliations>
</record>

Pour manipuler ce document sous Unix (Dilib)

EXPLOR_STEP=$WICRI_ROOT/Bois/explor/GlutaredoxinV1/Data/Main/Exploration
HfdSelect -h $EXPLOR_STEP/biblio.hfd -nk 000657 | SxmlIndent | more

Ou

HfdSelect -h $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd -nk 000657 | SxmlIndent | more

Pour mettre un lien sur cette page dans le réseau Wicri

{{Explor lien
   |wiki=    Bois
   |area=    GlutaredoxinV1
   |flux=    Main
   |étape=   Exploration
   |type=    RBID
   |clé=     pubmed:24041990
   |texte=   Glutaredoxin 1 is a major player in copper metabolism in neuroblastoma cells.
}}

Pour générer des pages wiki

HfdIndexSelect -h $EXPLOR_AREA/Data/Main/Exploration/RBID.i   -Sk "pubmed:24041990" \
       | HfdSelect -Kh $EXPLOR_AREA/Data/Main/Exploration/biblio.hfd   \
       | NlmPubMed2Wicri -a GlutaredoxinV1 

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This area was generated with Dilib version V0.6.37.
Data generation: Wed Nov 18 15:13:42 2020. Site generation: Wed Nov 18 15:16:12 2020