Serveur d'exploration sur la glutarédoxine

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Role of rockfish (Sebastes schlegelii) glutaredoxin 1 in innate immunity, and alleviation of cellular oxidative stress: Insights into localization, molecular characteristics, transcription, and function.

Identifieur interne : 000019 ( Main/Exploration ); précédent : 000018; suivant : 000020

Role of rockfish (Sebastes schlegelii) glutaredoxin 1 in innate immunity, and alleviation of cellular oxidative stress: Insights into localization, molecular characteristics, transcription, and function.

Auteurs : Rajamanthrilage Kasun Madusanka [Corée du Sud] ; M D Neranjan Tharuka [Corée du Sud] ; D S Liyanage [Corée du Sud] ; D M K P. Sirisena [Corée du Sud] ; Jehee Lee [Corée du Sud]

Source :

RBID : pubmed:32119919

Descripteurs français

English descriptors

Abstract

Glutaredoxins are a group of heat stable oxidoreductases ubiquitously found in prokaryotes and eukaryotes. They are widely known for GSH (glutathione)-dependent protein disulfide reduction and cellular redox homeostasis. This study was performed to identify and characterize rockfish (Sebastes schlegelii) glutaredoxin 1 (SsGrx1) at molecular, transcriptional, and functional levels. The coding sequence of SsGrx1 was 318 bp in length and encoded a protein containing 106 amino acids. The molecular weight and theoretical isoelectric point of the putative SsGrx1 protein were 11.6 kDa and 6.71 kDa, respectively. The amino acid sequence of SsGrx1 comprised a CPYC redox active motif surrounded by several conserved GSH binding sites. The modeled protein structure was found to consist of five α-helices and four β-sheets, similar to human Grx1. SsGrx1 showed a tissue specific expression in all the tissues tested, with the highest expression in the kidney. Immune stimulation by lipopolysaccharides (LPS), polyinosinic:polycytidylic acid (polyI:C), and Streptococcus iniae (S. iniae) could significantly modulate the SsGrx1 expression pattern in the blood and gills. Analysis of its subcellular localization disclosed that SsGrx1 was prominently localized in the cytosol. Recombinant SsGrx1 (rSsGrx1) exhibited significant activity in insulin disulfide reduction assay and HED (β-Hydroxyethyl Disulfide) assay. Furthermore, transient overexpression of SsGrx1 in FHM (fathead minnow) cells significantly enhanced cell survival upon H2O2-induced apoptosis. Collectively, our findings strongly suggest that SsGrx1 plays a crucial role in providing rockfish immune protection against pathogens and oxidative stress.

DOI: 10.1016/j.cbpb.2020.110432
PubMed: 32119919


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Le document en format XML

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<term>Amino Acid Motifs (MeSH)</term>
<term>Amino Acid Sequence (MeSH)</term>
<term>Animals (MeSH)</term>
<term>Apoptosis (genetics)</term>
<term>Apoptosis (immunology)</term>
<term>Bass (blood)</term>
<term>Bass (genetics)</term>
<term>Bass (immunology)</term>
<term>Bass (metabolism)</term>
<term>Binding Sites (genetics)</term>
<term>Cells, Cultured (MeSH)</term>
<term>Cytosol (metabolism)</term>
<term>Gene Expression Regulation (genetics)</term>
<term>Gene Expression Regulation (immunology)</term>
<term>Glutaredoxins (chemistry)</term>
<term>Glutaredoxins (genetics)</term>
<term>Glutaredoxins (metabolism)</term>
<term>Immunity, Innate (MeSH)</term>
<term>Lipopolysaccharides (pharmacology)</term>
<term>Organ Specificity (MeSH)</term>
<term>Oxidative Stress (MeSH)</term>
<term>Phylogeny (MeSH)</term>
<term>Poly I-C (pharmacology)</term>
<term>Protein Conformation, alpha-Helical (MeSH)</term>
<term>Protein Conformation, beta-Strand (MeSH)</term>
<term>Streptococcus iniae (immunology)</term>
<term>Streptococcus iniae (pathogenicity)</term>
<term>Transcription, Genetic (MeSH)</term>
</keywords>
<keywords scheme="KwdFr" xml:lang="fr">
<term>Animaux (MeSH)</term>
<term>Apoptose (génétique)</term>
<term>Apoptose (immunologie)</term>
<term>Cellules cultivées (MeSH)</term>
<term>Cytosol (métabolisme)</term>
<term>Glutarédoxines (composition chimique)</term>
<term>Glutarédoxines (génétique)</term>
<term>Glutarédoxines (métabolisme)</term>
<term>Immunité innée (MeSH)</term>
<term>Lipopolysaccharides (pharmacologie)</term>
<term>Motifs d'acides aminés (MeSH)</term>
<term>Phylogenèse (MeSH)</term>
<term>Poly I-C (pharmacologie)</term>
<term>Régulation de l'expression des gènes (génétique)</term>
<term>Régulation de l'expression des gènes (immunologie)</term>
<term>Serran (génétique)</term>
<term>Serran (immunologie)</term>
<term>Serran (métabolisme)</term>
<term>Serran (sang)</term>
<term>Sites de fixation (génétique)</term>
<term>Spécificité d'organe (MeSH)</term>
<term>Streptococcus iniae (immunologie)</term>
<term>Streptococcus iniae (pathogénicité)</term>
<term>Stress oxydatif (MeSH)</term>
<term>Structure en brin bêta (MeSH)</term>
<term>Structure en hélice alpha (MeSH)</term>
<term>Séquence d'acides aminés (MeSH)</term>
<term>Transcription génétique (MeSH)</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en">
<term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="blood" xml:lang="en">
<term>Bass</term>
</keywords>
<keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr">
<term>Glutarédoxines</term>
</keywords>
<keywords scheme="MESH" qualifier="genetics" xml:lang="en">
<term>Apoptosis</term>
<term>Bass</term>
<term>Binding Sites</term>
<term>Gene Expression Regulation</term>
<term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="génétique" xml:lang="fr">
<term>Apoptose</term>
<term>Glutarédoxines</term>
<term>Régulation de l'expression des gènes</term>
<term>Serran</term>
<term>Sites de fixation</term>
</keywords>
<keywords scheme="MESH" qualifier="immunologie" xml:lang="fr">
<term>Apoptose</term>
<term>Régulation de l'expression des gènes</term>
<term>Serran</term>
<term>Streptococcus iniae</term>
</keywords>
<keywords scheme="MESH" qualifier="immunology" xml:lang="en">
<term>Apoptosis</term>
<term>Bass</term>
<term>Gene Expression Regulation</term>
<term>Streptococcus iniae</term>
</keywords>
<keywords scheme="MESH" qualifier="metabolism" xml:lang="en">
<term>Bass</term>
<term>Cytosol</term>
<term>Glutaredoxins</term>
</keywords>
<keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr">
<term>Cytosol</term>
<term>Glutarédoxines</term>
<term>Serran</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogenicity" xml:lang="en">
<term>Streptococcus iniae</term>
</keywords>
<keywords scheme="MESH" qualifier="pathogénicité" xml:lang="fr">
<term>Streptococcus iniae</term>
</keywords>
<keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr">
<term>Lipopolysaccharides</term>
<term>Poly I-C</term>
</keywords>
<keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en">
<term>Lipopolysaccharides</term>
<term>Poly I-C</term>
</keywords>
<keywords scheme="MESH" qualifier="sang" xml:lang="fr">
<term>Serran</term>
</keywords>
<keywords scheme="MESH" xml:lang="en">
<term>Amino Acid Motifs</term>
<term>Amino Acid Sequence</term>
<term>Animals</term>
<term>Cells, Cultured</term>
<term>Immunity, Innate</term>
<term>Organ Specificity</term>
<term>Oxidative Stress</term>
<term>Phylogeny</term>
<term>Protein Conformation, alpha-Helical</term>
<term>Protein Conformation, beta-Strand</term>
<term>Transcription, Genetic</term>
</keywords>
<keywords scheme="MESH" xml:lang="fr">
<term>Animaux</term>
<term>Cellules cultivées</term>
<term>Immunité innée</term>
<term>Motifs d'acides aminés</term>
<term>Phylogenèse</term>
<term>Spécificité d'organe</term>
<term>Stress oxydatif</term>
<term>Structure en brin bêta</term>
<term>Structure en hélice alpha</term>
<term>Séquence d'acides aminés</term>
<term>Transcription génétique</term>
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<front>
<div type="abstract" xml:lang="en">Glutaredoxins are a group of heat stable oxidoreductases ubiquitously found in prokaryotes and eukaryotes. They are widely known for GSH (glutathione)-dependent protein disulfide reduction and cellular redox homeostasis. This study was performed to identify and characterize rockfish (Sebastes schlegelii) glutaredoxin 1 (SsGrx1) at molecular, transcriptional, and functional levels. The coding sequence of SsGrx1 was 318 bp in length and encoded a protein containing 106 amino acids. The molecular weight and theoretical isoelectric point of the putative SsGrx1 protein were 11.6 kDa and 6.71 kDa, respectively. The amino acid sequence of SsGrx1 comprised a CPYC redox active motif surrounded by several conserved GSH binding sites. The modeled protein structure was found to consist of five α-helices and four β-sheets, similar to human Grx1. SsGrx1 showed a tissue specific expression in all the tissues tested, with the highest expression in the kidney. Immune stimulation by lipopolysaccharides (LPS), polyinosinic:polycytidylic acid (polyI:C), and Streptococcus iniae (S. iniae) could significantly modulate the SsGrx1 expression pattern in the blood and gills. Analysis of its subcellular localization disclosed that SsGrx1 was prominently localized in the cytosol. Recombinant SsGrx1 (rSsGrx1) exhibited significant activity in insulin disulfide reduction assay and HED (β-Hydroxyethyl Disulfide) assay. Furthermore, transient overexpression of SsGrx1 in FHM (fathead minnow) cells significantly enhanced cell survival upon H
<sub>2</sub>
O
<sub>2</sub>
-induced apoptosis. Collectively, our findings strongly suggest that SsGrx1 plays a crucial role in providing rockfish immune protection against pathogens and oxidative stress.</div>
</front>
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<AbstractText>Glutaredoxins are a group of heat stable oxidoreductases ubiquitously found in prokaryotes and eukaryotes. They are widely known for GSH (glutathione)-dependent protein disulfide reduction and cellular redox homeostasis. This study was performed to identify and characterize rockfish (Sebastes schlegelii) glutaredoxin 1 (SsGrx1) at molecular, transcriptional, and functional levels. The coding sequence of SsGrx1 was 318 bp in length and encoded a protein containing 106 amino acids. The molecular weight and theoretical isoelectric point of the putative SsGrx1 protein were 11.6 kDa and 6.71 kDa, respectively. The amino acid sequence of SsGrx1 comprised a CPYC redox active motif surrounded by several conserved GSH binding sites. The modeled protein structure was found to consist of five α-helices and four β-sheets, similar to human Grx1. SsGrx1 showed a tissue specific expression in all the tissues tested, with the highest expression in the kidney. Immune stimulation by lipopolysaccharides (LPS), polyinosinic:polycytidylic acid (polyI:C), and Streptococcus iniae (S. iniae) could significantly modulate the SsGrx1 expression pattern in the blood and gills. Analysis of its subcellular localization disclosed that SsGrx1 was prominently localized in the cytosol. Recombinant SsGrx1 (rSsGrx1) exhibited significant activity in insulin disulfide reduction assay and HED (β-Hydroxyethyl Disulfide) assay. Furthermore, transient overexpression of SsGrx1 in FHM (fathead minnow) cells significantly enhanced cell survival upon H
<sub>2</sub>
O
<sub>2</sub>
-induced apoptosis. Collectively, our findings strongly suggest that SsGrx1 plays a crucial role in providing rockfish immune protection against pathogens and oxidative stress.</AbstractText>
<CopyrightInformation>Copyright © 2020 Elsevier Inc. All rights reserved.</CopyrightInformation>
</Abstract>
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<LastName>Madusanka</LastName>
<ForeName>Rajamanthrilage Kasun</ForeName>
<Initials>RK</Initials>
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<Affiliation>Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province 63243, Republic of Korea; Marine Science Institute, Jeju National University, Jeju Self-Governing Province 63333, Republic of Korea.</Affiliation>
</AffiliationInfo>
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<LastName>Tharuka</LastName>
<ForeName>M D Neranjan</ForeName>
<Initials>MDN</Initials>
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<Affiliation>Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province 63243, Republic of Korea; Marine Science Institute, Jeju National University, Jeju Self-Governing Province 63333, Republic of Korea.</Affiliation>
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<Initials>DS</Initials>
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<Affiliation>Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province 63243, Republic of Korea; Marine Science Institute, Jeju National University, Jeju Self-Governing Province 63333, Republic of Korea.</Affiliation>
</AffiliationInfo>
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<LastName>Sirisena</LastName>
<ForeName>D M K P</ForeName>
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<Affiliation>Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province 63243, Republic of Korea; Marine Science Institute, Jeju National University, Jeju Self-Governing Province 63333, Republic of Korea.</Affiliation>
</AffiliationInfo>
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<LastName>Lee</LastName>
<ForeName>Jehee</ForeName>
<Initials>J</Initials>
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<Affiliation>Department of Marine Life Sciences & Fish Vaccine Research Center, Jeju National University, Jeju Self-Governing Province 63243, Republic of Korea; Marine Science Institute, Jeju National University, Jeju Self-Governing Province 63333, Republic of Korea. Electronic address: jehee@jejunu.ac.kr.</Affiliation>
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<Day>29</Day>
</ArticleDate>
</Article>
<MedlineJournalInfo>
<Country>England</Country>
<MedlineTA>Comp Biochem Physiol B Biochem Mol Biol</MedlineTA>
<NlmUniqueID>9516061</NlmUniqueID>
<ISSNLinking>1096-4959</ISSNLinking>
</MedlineJournalInfo>
<ChemicalList>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>0</RegistryNumber>
<NameOfSubstance UI="D008070">Lipopolysaccharides</NameOfSubstance>
</Chemical>
<Chemical>
<RegistryNumber>O84C90HH2L</RegistryNumber>
<NameOfSubstance UI="D011070">Poly I-C</NameOfSubstance>
</Chemical>
</ChemicalList>
<CitationSubset>IM</CitationSubset>
<MeshHeadingList>
<MeshHeading>
<DescriptorName UI="D020816" MajorTopicYN="N">Amino Acid Motifs</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D017209" MajorTopicYN="N">Apoptosis</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001492" MajorTopicYN="N">Bass</DescriptorName>
<QualifierName UI="Q000097" MajorTopicYN="N">blood</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="Y">immunology</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D001665" MajorTopicYN="N">Binding Sites</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D003600" MajorTopicYN="N">Cytosol</DescriptorName>
<QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D005786" MajorTopicYN="N">Gene Expression Regulation</DescriptorName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName>
<QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName>
<QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName>
<QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D007113" MajorTopicYN="Y">Immunity, Innate</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D008070" MajorTopicYN="N">Lipopolysaccharides</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D009928" MajorTopicYN="N">Organ Specificity</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D018384" MajorTopicYN="N">Oxidative Stress</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D010802" MajorTopicYN="N">Phylogeny</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D011070" MajorTopicYN="N">Poly I-C</DescriptorName>
<QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D000072756" MajorTopicYN="N">Protein Conformation, alpha-Helical</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D000072757" MajorTopicYN="N">Protein Conformation, beta-Strand</DescriptorName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D000070058" MajorTopicYN="N">Streptococcus iniae</DescriptorName>
<QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName>
<QualifierName UI="Q000472" MajorTopicYN="N">pathogenicity</QualifierName>
</MeshHeading>
<MeshHeading>
<DescriptorName UI="D014158" MajorTopicYN="N">Transcription, Genetic</DescriptorName>
</MeshHeading>
</MeshHeadingList>
<KeywordList Owner="NOTNLM">
<Keyword MajorTopicYN="N">Deglutathionylation</Keyword>
<Keyword MajorTopicYN="N">Disulfide</Keyword>
<Keyword MajorTopicYN="N">Oxidoreductase</Keyword>
<Keyword MajorTopicYN="N">Redox</Keyword>
<Keyword MajorTopicYN="N">S-glutathionylation</Keyword>
</KeywordList>
<CoiStatement>Declaration of Competing Interest Authors declare no conflict of interests</CoiStatement>
</MedlineCitation>
<PubmedData>
<History>
<PubMedPubDate PubStatus="received">
<Year>2019</Year>
<Month>12</Month>
<Day>05</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="revised">
<Year>2020</Year>
<Month>02</Month>
<Day>21</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="accepted">
<Year>2020</Year>
<Month>02</Month>
<Day>25</Day>
</PubMedPubDate>
<PubMedPubDate PubStatus="pubmed">
<Year>2020</Year>
<Month>3</Month>
<Day>3</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="medline">
<Year>2020</Year>
<Month>11</Month>
<Day>12</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
<PubMedPubDate PubStatus="entrez">
<Year>2020</Year>
<Month>3</Month>
<Day>3</Day>
<Hour>6</Hour>
<Minute>0</Minute>
</PubMedPubDate>
</History>
<PublicationStatus>ppublish</PublicationStatus>
<ArticleIdList>
<ArticleId IdType="pubmed">32119919</ArticleId>
<ArticleId IdType="pii">S1096-4959(20)30026-9</ArticleId>
<ArticleId IdType="doi">10.1016/j.cbpb.2020.110432</ArticleId>
</ArticleIdList>
</PubmedData>
</pubmed>
<affiliations>
<list>
<country>
<li>Corée du Sud</li>
</country>
</list>
<tree>
<country name="Corée du Sud">
<noRegion>
<name sortKey="Madusanka, Rajamanthrilage Kasun" sort="Madusanka, Rajamanthrilage Kasun" uniqKey="Madusanka R" first="Rajamanthrilage Kasun" last="Madusanka">Rajamanthrilage Kasun Madusanka</name>
</noRegion>
<name sortKey="Lee, Jehee" sort="Lee, Jehee" uniqKey="Lee J" first="Jehee" last="Lee">Jehee Lee</name>
<name sortKey="Liyanage, D S" sort="Liyanage, D S" uniqKey="Liyanage D" first="D S" last="Liyanage">D S Liyanage</name>
<name sortKey="Sirisena, D M K P" sort="Sirisena, D M K P" uniqKey="Sirisena D" first="D M K P" last="Sirisena">D M K P. Sirisena</name>
<name sortKey="Tharuka, M D Neranjan" sort="Tharuka, M D Neranjan" uniqKey="Tharuka M" first="M D Neranjan" last="Tharuka">M D Neranjan Tharuka</name>
</country>
</tree>
</affiliations>
</record>

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