GlutaredoxinV1, Main, Exploration, bibRecord, 000B23

Glutaredoxin-1 mediates NADPH-dependent stimulation of calcium-dependent insulin secretion.

Identifieur interne : 000B23 ( Main/Exploration ); précédent : 000B22; suivant : 000B24

Glutaredoxin-1 mediates NADPH-dependent stimulation of calcium-dependent insulin secretion.

Auteurs : Thomas M. Reinbothe [Suède] ; Rosita Ivarsson ; Dai-Qing Li ; Omid Niazi ; Xingjun Jing ; Enming Zhang ; Lena Stenson ; Ulrika Bryborn ; Erik Renström

Source :

Molecular endocrinology (Baltimore, Md.) [ 1944-9917 ] ; 2009.

RBID : pubmed:19299446

Descripteurs français

English descriptors

KwdEn :
- Animals (MeSH), Calcium (metabolism), Cell Survival (drug effects), Exocytosis (drug effects), Gene Knockdown Techniques (MeSH), Gene Silencing (drug effects), Glucose (pharmacology), Glutaredoxins (metabolism), Immunohistochemistry (MeSH), Insulin (metabolism), Insulin Secretion (MeSH), Insulin-Secreting Cells (cytology), Insulin-Secreting Cells (drug effects), Insulin-Secreting Cells (enzymology), Insulin-Secreting Cells (metabolism), Intracellular Space (drug effects), Intracellular Space (enzymology), NADP (metabolism), Oxidation-Reduction (drug effects), Protein Transport (drug effects), Rats (MeSH), Subcellular Fractions (drug effects), Subcellular Fractions (enzymology), Thioredoxins (metabolism).
MESH :
- chemical , metabolism : Calcium, Glutaredoxins, Insulin, NADP, Thioredoxins.
- cytology : Insulin-Secreting Cells.
- drug effects : Cell Survival, Exocytosis, Gene Silencing, Insulin-Secreting Cells, Intracellular Space, Oxidation-Reduction, Protein Transport, Subcellular Fractions.
- enzymology : Insulin-Secreting Cells, Intracellular Space, Subcellular Fractions.
- metabolism : Insulin-Secreting Cells.
- chemical , pharmacology : Glucose.
- Animals, Gene Knockdown Techniques, Immunohistochemistry, Insulin Secretion, Rats.

Abstract

Nicotinamide adenine dinucleotide phosphate (NADPH) enhances Ca(2+)-induced exocytosis in pancreatic beta-cells, an effect suggested to involve the cytosolic redox protein glutaredoxin-1 (GRX-1). We here detail the role of GRX-1 in NADPH-stimulated beta-cell exocytosis and glucose-stimulated insulin secretion. Silencing of GRX-1 by RNA interference reduced glucose-stimulated insulin secretion in both clonal INS-1 832/13 cells and primary rat islets. GRX-1 silencing did not affect cell viability or the intracellular redox environment, suggesting that GRX-1 regulates the exocytotic machinery by a local action. By contrast, knockdown of the related protein thioredoxin-1 (TRX-1) was ineffective. Confocal immunocytochemistry revealed that GRX-1 locates to the cell periphery, whereas TRX-1 expression is uniform. These data suggest that the distinct subcellular localizations of TRX-1 and GRX-1 result in differences in substrate specificities and actions on insulin secretion. Single-cell exocytosis was likewise suppressed by GRX-1 knockdown in both rat beta-cells and clonal 832/13 cells, whereas after overexpression exocytosis increased by approximately 40%. Intracellular addition of NADPH (0.1 mm) stimulated Ca(2+)-evoked exocytosis in both cell types. Interestingly, the stimulatory action of NADPH on the exocytotic machinery coincided with an approximately 30% inhibition in whole-cell Ca(2+) currents. After GRX-1 silencing, NADPH failed to amplify insulin release but still inhibited Ca(2+) currents in 832/13 cells. In conclusion, NADPH stimulates the exocytotic machinery in pancreatic beta-cells. This effect is mediated by the NADPH acceptor protein GRX-1 by a local redox reaction that accelerates beta-cell exocytosis and, in turn, insulin secretion.

DOI: 10.1210/me.2008-0306
PubMed: 19299446
PubMed Central: PMC5419284

Affiliations:

Suède

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

to stream Main, to step Corpus: 000B14
to stream Main, to step Curation: 000B14

Le document en format XML

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<author><name sortKey="Ivarsson, Rosita" sort="Ivarsson, Rosita" uniqKey="Ivarsson R" first="Rosita" last="Ivarsson">Rosita Ivarsson</name>
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<author><name sortKey="Li, Dai Qing" sort="Li, Dai Qing" uniqKey="Li D" first="Dai-Qing" last="Li">Dai-Qing Li</name>
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<author><name sortKey="Niazi, Omid" sort="Niazi, Omid" uniqKey="Niazi O" first="Omid" last="Niazi">Omid Niazi</name>
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<author><name sortKey="Stenson, Lena" sort="Stenson, Lena" uniqKey="Stenson L" first="Lena" last="Stenson">Lena Stenson</name>
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<author><name sortKey="Bryborn, Ulrika" sort="Bryborn, Ulrika" uniqKey="Bryborn U" first="Ulrika" last="Bryborn">Ulrika Bryborn</name>
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<series><title level="j">Molecular endocrinology (Baltimore, Md.)</title>
<idno type="eISSN">1944-9917</idno>
<imprint><date when="2009" type="published">2009</date>
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<profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term>
<term>Calcium (metabolism)</term>
<term>Cell Survival (drug effects)</term>
<term>Exocytosis (drug effects)</term>
<term>Gene Knockdown Techniques (MeSH)</term>
<term>Gene Silencing (drug effects)</term>
<term>Glucose (pharmacology)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Immunohistochemistry (MeSH)</term>
<term>Insulin (metabolism)</term>
<term>Insulin Secretion (MeSH)</term>
<term>Insulin-Secreting Cells (cytology)</term>
<term>Insulin-Secreting Cells (drug effects)</term>
<term>Insulin-Secreting Cells (enzymology)</term>
<term>Insulin-Secreting Cells (metabolism)</term>
<term>Intracellular Space (drug effects)</term>
<term>Intracellular Space (enzymology)</term>
<term>NADP (metabolism)</term>
<term>Oxidation-Reduction (drug effects)</term>
<term>Protein Transport (drug effects)</term>
<term>Rats (MeSH)</term>
<term>Subcellular Fractions (drug effects)</term>
<term>Subcellular Fractions (enzymology)</term>
<term>Thioredoxins (metabolism)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term>
<term>Calcium (métabolisme)</term>
<term>Cellules à insuline (cytologie)</term>
<term>Cellules à insuline (effets des médicaments et des substances chimiques)</term>
<term>Cellules à insuline (enzymologie)</term>
<term>Cellules à insuline (métabolisme)</term>
<term>Espace intracellulaire (effets des médicaments et des substances chimiques)</term>
<term>Espace intracellulaire (enzymologie)</term>
<term>Exocytose (effets des médicaments et des substances chimiques)</term>
<term>Extinction de l'expression des gènes (effets des médicaments et des substances chimiques)</term>
<term>Fractions subcellulaires (effets des médicaments et des substances chimiques)</term>
<term>Fractions subcellulaires (enzymologie)</term>
<term>Glucose (pharmacologie)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Immunohistochimie (MeSH)</term>
<term>Insuline (métabolisme)</term>
<term>NADP (métabolisme)</term>
<term>Oxydoréduction (effets des médicaments et des substances chimiques)</term>
<term>Rats (MeSH)</term>
<term>Survie cellulaire (effets des médicaments et des substances chimiques)</term>
<term>Sécrétion d'insuline (MeSH)</term>
<term>Techniques de knock-down de gènes (MeSH)</term>
<term>Thiorédoxines (métabolisme)</term>
<term>Transport des protéines (effets des médicaments et des substances chimiques)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Calcium</term>
<term>Glutaredoxins</term>
<term>Insulin</term>
<term>NADP</term>
<term>Thioredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="cytologie" xml:lang="fr"><term>Cellules à insuline</term>
</keywords>
<keywords scheme="MESH" qualifier="cytology" xml:lang="en"><term>Insulin-Secreting Cells</term>
</keywords>
<keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Cell Survival</term>
<term>Exocytosis</term>
<term>Gene Silencing</term>
<term>Insulin-Secreting Cells</term>
<term>Intracellular Space</term>
<term>Oxidation-Reduction</term>
<term>Protein Transport</term>
<term>Subcellular Fractions</term>
</keywords>
<keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Cellules à insuline</term>
<term>Espace intracellulaire</term>
<term>Exocytose</term>
<term>Extinction de l'expression des gènes</term>
<term>Fractions subcellulaires</term>
<term>Oxydoréduction</term>
<term>Survie cellulaire</term>
<term>Transport des protéines</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cellules à insuline</term>
<term>Espace intracellulaire</term>
<term>Fractions subcellulaires</term>
</keywords>
<keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Insulin-Secreting Cells</term>
<term>Intracellular Space</term>
<term>Subcellular Fractions</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Insulin-Secreting Cells</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Calcium</term>
<term>Cellules à insuline</term>
<term>Glutarédoxines</term>
<term>Insuline</term>
<term>NADP</term>
<term>Thiorédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glucose</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Glucose</term>
</keywords>
<keywords scheme="MESH" xml:lang="en"><term>Animals</term>
<term>Gene Knockdown Techniques</term>
<term>Immunohistochemistry</term>
<term>Insulin Secretion</term>
<term>Rats</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr"><term>Animaux</term>
<term>Immunohistochimie</term>
<term>Rats</term>
<term>Sécrétion d'insuline</term>
<term>Techniques de knock-down de gènes</term>
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<front><div type="abstract" xml:lang="en">Nicotinamide adenine dinucleotide phosphate (NADPH) enhances Ca(2+)-induced exocytosis in pancreatic beta-cells, an effect suggested to involve the cytosolic redox protein glutaredoxin-1 (GRX-1). We here detail the role of GRX-1 in NADPH-stimulated beta-cell exocytosis and glucose-stimulated insulin secretion. Silencing of GRX-1 by RNA interference reduced glucose-stimulated insulin secretion in both clonal INS-1 832/13 cells and primary rat islets. GRX-1 silencing did not affect cell viability or the intracellular redox environment, suggesting that GRX-1 regulates the exocytotic machinery by a local action. By contrast, knockdown of the related protein thioredoxin-1 (TRX-1) was ineffective. Confocal immunocytochemistry revealed that GRX-1 locates to the cell periphery, whereas TRX-1 expression is uniform. These data suggest that the distinct subcellular localizations of TRX-1 and GRX-1 result in differences in substrate specificities and actions on insulin secretion. Single-cell exocytosis was likewise suppressed by GRX-1 knockdown in both rat beta-cells and clonal 832/13 cells, whereas after overexpression exocytosis increased by approximately 40%. Intracellular addition of NADPH (0.1 mm) stimulated Ca(2+)-evoked exocytosis in both cell types. Interestingly, the stimulatory action of NADPH on the exocytotic machinery coincided with an approximately 30% inhibition in whole-cell Ca(2+) currents. After GRX-1 silencing, NADPH failed to amplify insulin release but still inhibited Ca(2+) currents in 832/13 cells. In conclusion, NADPH stimulates the exocytotic machinery in pancreatic beta-cells. This effect is mediated by the NADPH acceptor protein GRX-1 by a local redox reaction that accelerates beta-cell exocytosis and, in turn, insulin secretion.</div>
</front>
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<DateCompleted><Year>2009</Year>
<Month>08</Month>
<Day>11</Day>
</DateCompleted>
<DateRevised><Year>2020</Year>
<Month>02</Month>
<Day>04</Day>
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<Issue>6</Issue>
<PubDate><Year>2009</Year>
<Month>Jun</Month>
</PubDate>
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<Title>Molecular endocrinology (Baltimore, Md.)</Title>
<ISOAbbreviation>Mol Endocrinol</ISOAbbreviation>
</Journal>
<ArticleTitle>Glutaredoxin-1 mediates NADPH-dependent stimulation of calcium-dependent insulin secretion.</ArticleTitle>
<Pagination><MedlinePgn>893-900</MedlinePgn>
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<Abstract><AbstractText>Nicotinamide adenine dinucleotide phosphate (NADPH) enhances Ca(2+)-induced exocytosis in pancreatic beta-cells, an effect suggested to involve the cytosolic redox protein glutaredoxin-1 (GRX-1). We here detail the role of GRX-1 in NADPH-stimulated beta-cell exocytosis and glucose-stimulated insulin secretion. Silencing of GRX-1 by RNA interference reduced glucose-stimulated insulin secretion in both clonal INS-1 832/13 cells and primary rat islets. GRX-1 silencing did not affect cell viability or the intracellular redox environment, suggesting that GRX-1 regulates the exocytotic machinery by a local action. By contrast, knockdown of the related protein thioredoxin-1 (TRX-1) was ineffective. Confocal immunocytochemistry revealed that GRX-1 locates to the cell periphery, whereas TRX-1 expression is uniform. These data suggest that the distinct subcellular localizations of TRX-1 and GRX-1 result in differences in substrate specificities and actions on insulin secretion. Single-cell exocytosis was likewise suppressed by GRX-1 knockdown in both rat beta-cells and clonal 832/13 cells, whereas after overexpression exocytosis increased by approximately 40%. Intracellular addition of NADPH (0.1 mm) stimulated Ca(2+)-evoked exocytosis in both cell types. Interestingly, the stimulatory action of NADPH on the exocytotic machinery coincided with an approximately 30% inhibition in whole-cell Ca(2+) currents. After GRX-1 silencing, NADPH failed to amplify insulin release but still inhibited Ca(2+) currents in 832/13 cells. In conclusion, NADPH stimulates the exocytotic machinery in pancreatic beta-cells. This effect is mediated by the NADPH acceptor protein GRX-1 by a local redox reaction that accelerates beta-cell exocytosis and, in turn, insulin secretion.</AbstractText>
</Abstract>
<AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Reinbothe</LastName>
<ForeName>Thomas M</ForeName>
<Initials>TM</Initials>
<AffiliationInfo><Affiliation>Department of Clinical Sciences, Islet Pathophysiology, Lund University, Clinical Research Centre, Malmö, Sweden. thomas.reinbothe@med.lu.se</Affiliation>
</AffiliationInfo>
</Author>
<Author ValidYN="Y"><LastName>Ivarsson</LastName>
<ForeName>Rosita</ForeName>
<Initials>R</Initials>
</Author>
<Author ValidYN="Y"><LastName>Li</LastName>
<ForeName>Dai-Qing</ForeName>
<Initials>DQ</Initials>
</Author>
<Author ValidYN="Y"><LastName>Niazi</LastName>
<ForeName>Omid</ForeName>
<Initials>O</Initials>
</Author>
<Author ValidYN="Y"><LastName>Jing</LastName>
<ForeName>Xingjun</ForeName>
<Initials>X</Initials>
</Author>
<Author ValidYN="Y"><LastName>Zhang</LastName>
<ForeName>Enming</ForeName>
<Initials>E</Initials>
</Author>
<Author ValidYN="Y"><LastName>Stenson</LastName>
<ForeName>Lena</ForeName>
<Initials>L</Initials>
</Author>
<Author ValidYN="Y"><LastName>Bryborn</LastName>
<ForeName>Ulrika</ForeName>
<Initials>U</Initials>
</Author>
<Author ValidYN="Y"><LastName>Renström</LastName>
<ForeName>Erik</ForeName>
<Initials>E</Initials>
</Author>
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<Language>eng</Language>
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<Month>03</Month>
<Day>19</Day>
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<MedlineTA>Mol Endocrinol</MedlineTA>
<NlmUniqueID>8801431</NlmUniqueID>
<ISSNLinking>0888-8809</ISSNLinking>
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<ChemicalList><Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="C516007">Glrx protein, rat</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D007328">Insulin</NameOfSubstance>
</Chemical>
<Chemical><RegistryNumber>52500-60-4</RegistryNumber>
<NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance>
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<Chemical><RegistryNumber>53-59-8</RegistryNumber>
<NameOfSubstance UI="D009249">NADP</NameOfSubstance>
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<Chemical><RegistryNumber>IY9XDZ35W2</RegistryNumber>
<NameOfSubstance UI="D005947">Glucose</NameOfSubstance>
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<Chemical><RegistryNumber>SY7Q814VUP</RegistryNumber>
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<MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002118" MajorTopicYN="N">Calcium</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D002470" MajorTopicYN="N">Cell Survival</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D005089" MajorTopicYN="N">Exocytosis</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D055785" MajorTopicYN="N">Gene Knockdown Techniques</DescriptorName>
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<MeshHeading><DescriptorName UI="D020868" MajorTopicYN="N">Gene Silencing</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
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<MeshHeading><DescriptorName UI="D005947" MajorTopicYN="N">Glucose</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
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<MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007150" MajorTopicYN="N">Immunohistochemistry</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D007328" MajorTopicYN="N">Insulin</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D000078790" MajorTopicYN="N">Insulin Secretion</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D050417" MajorTopicYN="N">Insulin-Secreting Cells</DescriptorName>
<QualifierName UI="Q000166" MajorTopicYN="N">cytology</QualifierName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D042541" MajorTopicYN="N">Intracellular Space</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D009249" MajorTopicYN="N">NADP</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D021381" MajorTopicYN="N">Protein Transport</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013347" MajorTopicYN="N">Subcellular Fractions</DescriptorName>
<QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName>
<QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName>
</MeshHeading>
<MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
</MeshHeadingList>
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Glutaredoxin-1 mediates NADPH-dependent stimulation of calcium-dependent insulin secretion.

Glutaredoxin-1 mediates NADPH-dependent stimulation of calcium-dependent insulin secretion.

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