Thioredoxin and related molecules--from biology to health and disease.
Identifieur interne : 000C42 ( Main/Exploration ); précédent : 000C41; suivant : 000C43Thioredoxin and related molecules--from biology to health and disease.
Auteurs : Christopher Horst Lillig [Suède] ; Arne HolmgrenSource :
- Antioxidants & redox signaling [ 1523-0864 ] ; 2007.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Athérosclérose (métabolisme), Diabète (métabolisme), Distribution tissulaire (MeSH), Données de séquences moléculaires (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Modèles biologiques (MeSH), Oxidoreductases (composition chimique), Oxidoreductases (métabolisme), Pliage des protéines (MeSH), Structure secondaire des protéines (MeSH), Structure tertiaire des protéines (MeSH), Séquence d'acides aminés (MeSH), Thiorédoxines (composition chimique), Thiorédoxines (génétique), Thiorédoxines (immunologie), Thiorédoxines (métabolisme), Transduction du signal (MeSH).
- MESH :
- composition chimique : Oxidoreductases, Thiorédoxines.
- génétique : Thiorédoxines.
- immunologie : Thiorédoxines.
- métabolisme : Athérosclérose, Diabète, Oxidoreductases, Thiorédoxines.
- Animaux, Distribution tissulaire, Données de séquences moléculaires, Glutarédoxines, Humains, Modèles biologiques, Pliage des protéines, Structure secondaire des protéines, Structure tertiaire des protéines, Séquence d'acides aminés, Transduction du signal.
English descriptors
- KwdEn :
- Amino Acid Sequence (MeSH), Animals (MeSH), Atherosclerosis (metabolism), Diabetes Mellitus (metabolism), Glutaredoxins (MeSH), Humans (MeSH), Models, Biological (MeSH), Molecular Sequence Data (MeSH), Oxidoreductases (chemistry), Oxidoreductases (metabolism), Protein Folding (MeSH), Protein Structure, Secondary (MeSH), Protein Structure, Tertiary (MeSH), Signal Transduction (MeSH), Thioredoxins (chemistry), Thioredoxins (genetics), Thioredoxins (immunology), Thioredoxins (metabolism), Tissue Distribution (MeSH).
- MESH :
- chemical , chemistry : Oxidoreductases, Thioredoxins.
- chemical , genetics : Thioredoxins.
- chemical , immunology : Thioredoxins.
- chemical , metabolism : Oxidoreductases, Thioredoxins.
- chemical : Glutaredoxins.
- metabolism : Atherosclerosis, Diabetes Mellitus.
- Amino Acid Sequence, Animals, Humans, Models, Biological, Molecular Sequence Data, Protein Folding, Protein Structure, Secondary, Protein Structure, Tertiary, Signal Transduction, Tissue Distribution.
Abstract
Thioredoxin and glutaredoxin systems in mammalian cells utilize thiol and selenol groups to maintain a reducing intracellular redox state acting as antioxidants and reducing agents in redox signaling with oxidizing reactive oxygen species. During the last decade, the functional roles of thioredoxin in particular have continued to expand, also including novel functions such as a secreted growth factor or a chemokine for immune cells. The role of thioredoxin and glutaredoxin in antioxidant defense and the role of thioredoxin in controlling recruitment of inflammatory cells offer potential use in clinical therapy. The fundamental differences between bacterial and mammalian thioredoxin reductases offer new principles for treatment of infections. Clinical drugs already in use target the active site selenol in thioredoxin reductases, inducing cell death in tumor cells. Thioredoxin and binding proteins (ASK1 and TBP2) appear to control apoptosis or metabolic states such as carbohydrate and lipid metabolism related to diseases such as diabetes and atherosclerosis.
DOI: 10.1089/ars.2007.9.25
PubMed: 17115886
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>The Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm</wicri:regionArea><placeName><settlement type="city">Stockholm</settlement><region nuts="2">Svealand</region></placeName></affiliation></author><author><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></author></analytic><series><title level="j">Antioxidants & redox signaling</title><idno type="ISSN">1523-0864</idno><imprint><date when="2007" type="published">2007</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Amino Acid Sequence (MeSH)</term><term>Animals (MeSH)</term><term>Atherosclerosis (metabolism)</term><term>Diabetes Mellitus 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type="chemical" xml:lang="en"><term>Glutaredoxins</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Oxidoreductases</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="génétique" xml:lang="fr"><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="immunologie" xml:lang="fr"><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Atherosclerosis</term><term>Diabetes Mellitus</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Athérosclérose</term><term>Diabète</term><term>Oxidoreductases</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Amino Acid Sequence</term><term>Animals</term><term>Humans</term><term>Models, Biological</term><term>Molecular Sequence Data</term><term>Protein Folding</term><term>Protein Structure, Secondary</term><term>Protein Structure, Tertiary</term><term>Signal Transduction</term><term>Tissue Distribution</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Distribution tissulaire</term><term>Données de séquences moléculaires</term><term>Glutarédoxines</term><term>Humains</term><term>Modèles biologiques</term><term>Pliage des protéines</term><term>Structure secondaire des protéines</term><term>Structure tertiaire des protéines</term><term>Séquence d'acides aminés</term><term>Transduction du signal</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin and glutaredoxin systems in mammalian cells utilize thiol and selenol groups to maintain a reducing intracellular redox state acting as antioxidants and reducing agents in redox signaling with oxidizing reactive oxygen species. During the last decade, the functional roles of thioredoxin in particular have continued to expand, also including novel functions such as a secreted growth factor or a chemokine for immune cells. The role of thioredoxin and glutaredoxin in antioxidant defense and the role of thioredoxin in controlling recruitment of inflammatory cells offer potential use in clinical therapy. The fundamental differences between bacterial and mammalian thioredoxin reductases offer new principles for treatment of infections. Clinical drugs already in use target the active site selenol in thioredoxin reductases, inducing cell death in tumor cells. Thioredoxin and binding proteins (ASK1 and TBP2) appear to control apoptosis or metabolic states such as carbohydrate and lipid metabolism related to diseases such as diabetes and atherosclerosis.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">17115886</PMID><DateCompleted><Year>2007</Year><Month>04</Month><Day>25</Day></DateCompleted><DateRevised><Year>2007</Year><Month>11</Month><Day>15</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1523-0864</ISSN><JournalIssue CitedMedium="Print"><Volume>9</Volume><Issue>1</Issue><PubDate><Year>2007</Year><Month>Jan</Month></PubDate></JournalIssue><Title>Antioxidants & redox signaling</Title><ISOAbbreviation>Antioxid Redox Signal</ISOAbbreviation></Journal><ArticleTitle>Thioredoxin and related molecules--from biology to health and disease.</ArticleTitle><Pagination><MedlinePgn>25-47</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin and glutaredoxin systems in mammalian cells utilize thiol and selenol groups to maintain a reducing intracellular redox state acting as antioxidants and reducing agents in redox signaling with oxidizing reactive oxygen species. During the last decade, the functional roles of thioredoxin in particular have continued to expand, also including novel functions such as a secreted growth factor or a chemokine for immune cells. The role of thioredoxin and glutaredoxin in antioxidant defense and the role of thioredoxin in controlling recruitment of inflammatory cells offer potential use in clinical therapy. The fundamental differences between bacterial and mammalian thioredoxin reductases offer new principles for treatment of infections. Clinical drugs already in use target the active site selenol in thioredoxin reductases, inducing cell death in tumor cells. Thioredoxin and binding proteins (ASK1 and TBP2) appear to control apoptosis or metabolic states such as carbohydrate and lipid metabolism related to diseases such as diabetes and atherosclerosis.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lillig</LastName><ForeName>Christopher Horst</ForeName><Initials>CH</Initials><AffiliationInfo><Affiliation>The Medical Nobel Institute for Biochemistry, Department of Medical Biochemistry and Biophysics, Karolinska Institute, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>Arne</ForeName><Initials>A</Initials></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></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Antioxid Redox Signal</MedlineTA><NlmUniqueID>100888899</NlmUniqueID><ISSNLinking>1523-0864</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>52500-60-4</RegistryNumber><NameOfSubstance UI="D013879">Thioredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000595" MajorTopicYN="N">Amino Acid Sequence</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D050197" MajorTopicYN="N">Atherosclerosis</DescriptorName><QualifierName UI="Q000378" 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Folding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017433" MajorTopicYN="N">Protein Structure, Secondary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017434" MajorTopicYN="N">Protein Structure, Tertiary</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D015398" MajorTopicYN="N">Signal Transduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="Y">Thioredoxins</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000235" MajorTopicYN="N">genetics</QualifierName><QualifierName UI="Q000276" MajorTopicYN="N">immunology</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D014018" MajorTopicYN="N">Tissue Distribution</DescriptorName></MeshHeading></MeshHeadingList><NumberOfReferences>281</NumberOfReferences></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2006</Year><Month>11</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2007</Year><Month>4</Month><Day>26</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2006</Year><Month>11</Month><Day>23</Day><Hour>9</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">17115886</ArticleId><ArticleId IdType="doi">10.1089/ars.2007.9.25</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Holmgren, Arne" sort="Holmgren, Arne" uniqKey="Holmgren A" first="Arne" last="Holmgren">Arne Holmgren</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Lillig, Christopher Horst" sort="Lillig, Christopher Horst" 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