Unraveling the role of thiosulfate sulfurtransferase in metabolic diseases.
Identifieur interne : 000004 ( Main/Exploration ); précédent : 000003; suivant : 000005Unraveling the role of thiosulfate sulfurtransferase in metabolic diseases.
Auteurs : Paul D. Kruithof [Pays-Bas] ; Sergey Lunev [Pays-Bas] ; Sheila P. Aguilar Lozano [Pays-Bas] ; Fernando De Assis Batista [Pays-Bas] ; Zayana M. Al-Dahmani [Pays-Bas] ; Jaap A. Joles [Pays-Bas] ; Amalia M. Dolga [Pays-Bas] ; Matthew R. Groves [Pays-Bas] ; Harry Van Goor [Pays-Bas]Source :
- Biochimica et biophysica acta. Molecular basis of disease [ 1879-260X ] ; 2020.
Descripteurs français
- KwdFr :
- Antioxydants (métabolisme), Ferrosulfoprotéines (génétique), Glutathion (métabolisme), Humains (MeSH), Maladies métaboliques (anatomopathologie), Maladies métaboliques (enzymologie), Maladies métaboliques (génétique), Soufre (métabolisme), Sélénium (métabolisme), Thiorédoxines (génétique), Thiorédoxines (métabolisme), Thiosulfate sulfurtransferase (génétique), Thiosulfate sulfurtransferase (métabolisme).
- MESH :
- anatomopathologie : Maladies métaboliques.
- enzymologie : Maladies métaboliques.
- génétique : Ferrosulfoprotéines, Maladies métaboliques, Thiorédoxines, Thiosulfate sulfurtransferase.
- métabolisme : Antioxydants, Glutathion, Soufre, Sélénium, Thiorédoxines, Thiosulfate sulfurtransferase.
- Humains.
English descriptors
- KwdEn :
- Antioxidants (metabolism), Glutathione (metabolism), Humans (MeSH), Iron-Sulfur Proteins (genetics), Metabolic Diseases (enzymology), Metabolic Diseases (genetics), Metabolic Diseases (pathology), Selenium (metabolism), Sulfur (metabolism), Thioredoxins (genetics), Thioredoxins (metabolism), Thiosulfate Sulfurtransferase (genetics), Thiosulfate Sulfurtransferase (metabolism).
- MESH :
- chemical , genetics : Iron-Sulfur Proteins, Thioredoxins, Thiosulfate Sulfurtransferase.
- chemical , metabolism : Antioxidants, Glutathione, Selenium, Sulfur, Thioredoxins, Thiosulfate Sulfurtransferase.
- enzymology : Metabolic Diseases.
- genetics : Metabolic Diseases.
- pathology : Metabolic Diseases.
- Humans.
Abstract
Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), also known as Rhodanese, is a mitochondrial enzyme which catalyzes the transfer of sulfur in several molecular pathways. After its initial identification as a cyanide detoxification enzyme, it was found that its functions also include sulfur metabolism, modification of iron‑sulfur clusters and the reduction of antioxidants glutathione and thioredoxin. TST deficiency was shown to be strongly related to the pathophysiology of metabolic diseases including diabetes and obesity. This review summarizes research related to the enzymatic properties and functions of TST, to then explore the association between the effects of TST on mitochondria and development of diseases such as diabetes and obesity.
DOI: 10.1016/j.bbadis.2020.165716
PubMed: 32061776
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Groves</name><affiliation wicri:level="1"><nlm:affiliation>Univeristy of Groningen, Department of Pharmacy and Drug Design, the Netherlands.</nlm:affiliation><country xml:lang="fr" wicri:curation="lc">Pays-Bas</country><wicri:regionArea>Univeristy of Groningen, Department of Pharmacy and Drug Design</wicri:regionArea><wicri:noRegion>Department of Pharmacy and Drug Design</wicri:noRegion></affiliation></author><author><name sortKey="Van Goor, Harry" sort="Van Goor, Harry" uniqKey="Van Goor H" first="Harry" last="Van Goor">Harry Van Goor</name><affiliation wicri:level="1"><nlm:affiliation>University Medical Center Groningen, Department of Pathology and Medical Biology the Netherlands. Electronic address: h.van.goor@umcg.nl.</nlm:affiliation><country wicri:rule="url">Pays-Bas</country></affiliation></author></analytic><series><title level="j">Biochimica et biophysica acta. Molecular basis of disease</title><idno type="eISSN">1879-260X</idno><imprint><date when="2020" type="published">2020</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Antioxidants (metabolism)</term><term>Glutathione (metabolism)</term><term>Humans (MeSH)</term><term>Iron-Sulfur Proteins (genetics)</term><term>Metabolic Diseases (enzymology)</term><term>Metabolic Diseases (genetics)</term><term>Metabolic Diseases (pathology)</term><term>Selenium (metabolism)</term><term>Sulfur (metabolism)</term><term>Thioredoxins (genetics)</term><term>Thioredoxins (metabolism)</term><term>Thiosulfate Sulfurtransferase (genetics)</term><term>Thiosulfate Sulfurtransferase (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Antioxydants (métabolisme)</term><term>Ferrosulfoprotéines (génétique)</term><term>Glutathion (métabolisme)</term><term>Humains (MeSH)</term><term>Maladies métaboliques (anatomopathologie)</term><term>Maladies métaboliques (enzymologie)</term><term>Maladies métaboliques (génétique)</term><term>Soufre (métabolisme)</term><term>Sélénium (métabolisme)</term><term>Thiorédoxines (génétique)</term><term>Thiorédoxines (métabolisme)</term><term>Thiosulfate sulfurtransferase (génétique)</term><term>Thiosulfate sulfurtransferase (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="genetics" xml:lang="en"><term>Iron-Sulfur Proteins</term><term>Thioredoxins</term><term>Thiosulfate Sulfurtransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Antioxidants</term><term>Glutathione</term><term>Selenium</term><term>Sulfur</term><term>Thioredoxins</term><term>Thiosulfate Sulfurtransferase</term></keywords><keywords scheme="MESH" qualifier="anatomopathologie" xml:lang="fr"><term>Maladies métaboliques</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Maladies métaboliques</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Metabolic Diseases</term></keywords><keywords scheme="MESH" qualifier="genetics" xml:lang="en"><term>Metabolic Diseases</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Ferrosulfoprotéines</term><term>Maladies métaboliques</term><term>Thiorédoxines</term><term>Thiosulfate sulfurtransferase</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Antioxydants</term><term>Glutathion</term><term>Soufre</term><term>Sélénium</term><term>Thiorédoxines</term><term>Thiosulfate sulfurtransferase</term></keywords><keywords scheme="MESH" qualifier="pathology" xml:lang="en"><term>Metabolic Diseases</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Humans</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Humains</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), also known as Rhodanese, is a mitochondrial enzyme which catalyzes the transfer of sulfur in several molecular pathways. After its initial identification as a cyanide detoxification enzyme, it was found that its functions also include sulfur metabolism, modification of iron‑sulfur clusters and the reduction of antioxidants glutathione and thioredoxin. TST deficiency was shown to be strongly related to the pathophysiology of metabolic diseases including diabetes and obesity. This review summarizes research related to the enzymatic properties and functions of TST, to then explore the association between the effects of TST on mitochondria and development of diseases such as diabetes and obesity.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">32061776</PMID><DateCompleted><Year>2020</Year><Month>10</Month><Day>19</Day></DateCompleted><DateRevised><Year>2020</Year><Month>10</Month><Day>19</Day></DateRevised><Article PubModel="Print-Electronic"><Journal><ISSN IssnType="Electronic">1879-260X</ISSN><JournalIssue CitedMedium="Internet"><Volume>1866</Volume><Issue>6</Issue><PubDate><Year>2020</Year><Month>06</Month><Day>01</Day></PubDate></JournalIssue><Title>Biochimica et biophysica acta. Molecular basis of disease</Title><ISOAbbreviation>Biochim Biophys Acta Mol Basis Dis</ISOAbbreviation></Journal><ArticleTitle>Unraveling the role of thiosulfate sulfurtransferase in metabolic diseases.</ArticleTitle><Pagination><MedlinePgn>165716</MedlinePgn></Pagination><ELocationID EIdType="pii" ValidYN="Y">S0925-4439(20)30061-2</ELocationID><ELocationID EIdType="doi" ValidYN="Y">10.1016/j.bbadis.2020.165716</ELocationID><Abstract><AbstractText>Thiosulfate sulfurtransferase (TST, EC 2.8.1.1), also known as Rhodanese, is a mitochondrial enzyme which catalyzes the transfer of sulfur in several molecular pathways. After its initial identification as a cyanide detoxification enzyme, it was found that its functions also include sulfur metabolism, modification of iron‑sulfur clusters and the reduction of antioxidants glutathione and thioredoxin. TST deficiency was shown to be strongly related to the pathophysiology of metabolic diseases including diabetes and obesity. This review summarizes research related to the enzymatic properties and functions of TST, to then explore the association between the effects of TST on mitochondria and development of diseases such as diabetes and obesity.</AbstractText><CopyrightInformation>Copyright © 2020 Elsevier B.V. All rights reserved.</CopyrightInformation></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Kruithof</LastName><ForeName>Paul D</ForeName><Initials>PD</Initials><AffiliationInfo><Affiliation>Univeristy of Groningen, Department of Pharmacy and Drug Design, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Lunev</LastName><ForeName>Sergey</ForeName><Initials>S</Initials><AffiliationInfo><Affiliation>Univeristy of Groningen, Department of Pharmacy and Drug Design, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Aguilar Lozano</LastName><ForeName>Sheila P</ForeName><Initials>SP</Initials><AffiliationInfo><Affiliation>Univeristy of Groningen, Department of Pharmacy and Drug Design, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>de Assis Batista</LastName><ForeName>Fernando</ForeName><Initials>F</Initials><AffiliationInfo><Affiliation>Univeristy of Groningen, Department of Pharmacy and Drug Design, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Al-Dahmani</LastName><ForeName>Zayana M</ForeName><Initials>ZM</Initials><AffiliationInfo><Affiliation>Univeristy of Groningen, Department of Pharmacy and Drug Design, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Joles</LastName><ForeName>Jaap A</ForeName><Initials>JA</Initials><AffiliationInfo><Affiliation>University Medical Center Utrecht, Department of Nephrology and Hypertension, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Dolga</LastName><ForeName>Amalia M</ForeName><Initials>AM</Initials><AffiliationInfo><Affiliation>University of Groningen, Department of Pharmacy, Molecular Pharmacology, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Groves</LastName><ForeName>Matthew R</ForeName><Initials>MR</Initials><AffiliationInfo><Affiliation>Univeristy of Groningen, Department of Pharmacy and Drug Design, the Netherlands.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>van Goor</LastName><ForeName>Harry</ForeName><Initials>H</Initials><AffiliationInfo><Affiliation>University Medical Center Groningen, Department of Pathology and Medical Biology the Netherlands. Electronic address: h.van.goor@umcg.nl.</Affiliation></AffiliationInfo></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType><PublicationType UI="D016454">Review</PublicationType></PublicationTypeList><ArticleDate DateType="Electronic"><Year>2020</Year><Month>02</Month><Day>19</Day></ArticleDate></Article><MedlineJournalInfo><Country>Netherlands</Country><MedlineTA>Biochim Biophys Acta Mol Basis Dis</MedlineTA><NlmUniqueID>101731730</NlmUniqueID><ISSNLinking>0925-4439</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D000975">Antioxidants</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D007506">Iron-Sulfur Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C491203">TXN protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>70FD1KFU70</RegistryNumber><NameOfSubstance UI="D013455">Sulfur</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.8.1.1</RegistryNumber><NameOfSubstance UI="D013884">Thiosulfate Sulfurtransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical><Chemical><RegistryNumber>H6241UJ22B</RegistryNumber><NameOfSubstance UI="D012643">Selenium</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007506" MajorTopicYN="N">Iron-Sulfur Proteins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008659" MajorTopicYN="N">Metabolic Diseases</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000473" MajorTopicYN="N">pathology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D012643" MajorTopicYN="N">Selenium</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013455" MajorTopicYN="N">Sulfur</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013884" MajorTopicYN="N">Thiosulfate Sulfurtransferase</DescriptorName><QualifierName UI="Q000235" MajorTopicYN="Y">genetics</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList><KeywordList Owner="NOTNLM"><Keyword MajorTopicYN="Y">Antioxidant systems</Keyword><Keyword MajorTopicYN="Y">Diabetes</Keyword><Keyword MajorTopicYN="Y">Obesity</Keyword><Keyword MajorTopicYN="Y">Rhodanese</Keyword><Keyword MajorTopicYN="Y">Sulfurtransferase</Keyword><Keyword MajorTopicYN="Y">TST</Keyword></KeywordList><CoiStatement>Declaration of competing interest The authors declare that they have no known competing financial interests or personal relationships that could have appeared to influence the work reported in this paper.</CoiStatement></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="received"><Year>2019</Year><Month>08</Month><Day>28</Day></PubMedPubDate><PubMedPubDate PubStatus="revised"><Year>2020</Year><Month>01</Month><Day>10</Day></PubMedPubDate><PubMedPubDate PubStatus="accepted"><Year>2020</Year><Month>01</Month><Day>30</Day></PubMedPubDate><PubMedPubDate PubStatus="pubmed"><Year>2020</Year><Month>2</Month><Day>18</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2020</Year><Month>10</Month><Day>21</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2020</Year><Month>2</Month><Day>17</Day><Hour>6</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">32061776</ArticleId><ArticleId IdType="pii">S0925-4439(20)30061-2</ArticleId><ArticleId IdType="doi">10.1016/j.bbadis.2020.165716</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Pays-Bas</li></country><region><li>Groningue (province)</li></region><settlement><li>Groningue (ville)</li></settlement><orgName><li>Université de Groningue</li></orgName></list><tree><country name="Pays-Bas"><noRegion><name sortKey="Kruithof, Paul D" sort="Kruithof, Paul D" uniqKey="Kruithof P" first="Paul D" last="Kruithof">Paul D. Kruithof</name></noRegion><name sortKey="Aguilar Lozano, Sheila P" sort="Aguilar Lozano, Sheila P" uniqKey="Aguilar Lozano S" first="Sheila P" last="Aguilar Lozano">Sheila P. Aguilar Lozano</name><name sortKey="Al Dahmani, Zayana M" sort="Al Dahmani, Zayana M" uniqKey="Al Dahmani Z" first="Zayana M" last="Al-Dahmani">Zayana M. Al-Dahmani</name><name sortKey="De Assis Batista, Fernando" sort="De Assis Batista, Fernando" uniqKey="De Assis Batista F" first="Fernando" last="De Assis Batista">Fernando De Assis Batista</name><name sortKey="Dolga, Amalia M" sort="Dolga, Amalia M" uniqKey="Dolga A" first="Amalia M" last="Dolga">Amalia M. Dolga</name><name sortKey="Groves, Matthew R" sort="Groves, Matthew R" uniqKey="Groves M" first="Matthew R" last="Groves">Matthew R. Groves</name><name sortKey="Joles, Jaap A" sort="Joles, Jaap A" uniqKey="Joles J" first="Jaap A" last="Joles">Jaap A. Joles</name><name sortKey="Lunev, Sergey" sort="Lunev, Sergey" uniqKey="Lunev S" first="Sergey" last="Lunev">Sergey Lunev</name><name sortKey="Van Goor, Harry" sort="Van Goor, Harry" uniqKey="Van Goor H" first="Harry" last="Van Goor">Harry Van Goor</name></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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