Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.
Identifieur interne : 001374 ( Main/Exploration ); précédent : 001373; suivant : 001375Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.
Auteurs : M L Tsang ; J A WeatherbeeSource :
- Proceedings of the National Academy of Sciences of the United States of America [ 0027-8424 ] ; 1981.
Descripteurs français
- KwdFr :
- Cellules HeLa (enzymologie), Femelle (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Masse moléculaire (MeSH), NADH, NADPH oxidoreductases (métabolisme), Oxidoreductases (MeSH), Protéines (métabolisme), Protéines bactériennes (métabolisme), Thioredoxin-disulfide reductase (isolement et purification), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (isolement et purification), Thiorédoxines (métabolisme).
- MESH :
- enzymologie : Cellules HeLa.
- isolement et purification : Thioredoxin-disulfide reductase, Thiorédoxines.
- métabolisme : NADH, NADPH oxidoreductases, Protéines, Protéines bactériennes, Thioredoxin-disulfide reductase, Thiorédoxines.
- Femelle, Glutarédoxines, Humains, Masse moléculaire, Oxidoreductases.
English descriptors
- KwdEn :
- Bacterial Proteins (metabolism), Female (MeSH), Glutaredoxins (MeSH), HeLa Cells (enzymology), Humans (MeSH), Molecular Weight (MeSH), NADH, NADPH Oxidoreductases (metabolism), Oxidoreductases (MeSH), Proteins (metabolism), Thioredoxin-Disulfide Reductase (isolation & purification), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (isolation & purification), Thioredoxins (metabolism).
- MESH :
- chemical , isolation & purification : Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , metabolism : Bacterial Proteins, NADH, NADPH Oxidoreductases, Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- enzymology : HeLa Cells.
- Female, Glutaredoxins, Humans, Molecular Weight, Oxidoreductases.
Abstract
Thioredoxin and glutaredoxin may be important in regulating cell metabolism by mediating interchanges between sulfhydryl and disulfide groups. Components of the thioredoxin/glutaredoxin system from cultured HeLa cells have been partially purified and characterized by using Escherichia coli adenosine 3'-phosphate 5'-phosphosulfate reductase, a thioredoxin/glutaredoxin-dependent enzyme on the pathway of sulfate reduction, as an assay system. In HeLa cells, a NADPH-thioredoxin reductase and three heat-labile proteins (designated PI, PII, and PIII) that have thioredoxin- or glutaredoxin-like properties are found. Both PI and PIII have molecular masses of approximately 12,000 daltons and are readily reduced by their homologous HeLa thioredoxin reductase. However, only PI can be reduced efficiently by the glutathione system and neither PI nor PIII has inherent glutathione-disulfide oxidoreductase activity. PII has a molecular mass of greater than 30,000 daltons and appears to be associated with a reductase activity. The HeLa NADPH-thioredoxin reductase has been purified to near homogeneity and found to be a 116,000-dalton flavoprotein composed of two 58,000-dalton subunits. The HeLa enzyme has low species and substrate specificity and can reduce HeLa PI and PIII, E. coli thioredoxin and glutaredoxin, and the disulfide bond in 5,5'-dithiobis(2-nitrobenzoic acid). The exact in vivo roles of the HeLa thioredoxin/glutaredoxin system remain to be determined.
DOI: 10.1073/pnas.78.12.7478
PubMed: 6950391
PubMed Central: PMC349291
Affiliations:
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<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.</title><author><name sortKey="Tsang, M L" sort="Tsang, M L" uniqKey="Tsang M" first="M L" last="Tsang">M L Tsang</name></author><author><name sortKey="Weatherbee, J A" sort="Weatherbee, J A" uniqKey="Weatherbee J" first="J A" last="Weatherbee">J A Weatherbee</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1981">1981</date><idno type="RBID">pubmed:6950391</idno><idno type="pmid">6950391</idno><idno type="pmc">PMC349291</idno><idno type="doi">10.1073/pnas.78.12.7478</idno><idno type="wicri:Area/Main/Corpus">001373</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001373</idno><idno type="wicri:Area/Main/Curation">001373</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001373</idno><idno type="wicri:Area/Main/Exploration">001373</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.</title><author><name sortKey="Tsang, M L" sort="Tsang, M L" uniqKey="Tsang M" first="M L" last="Tsang">M L Tsang</name></author><author><name sortKey="Weatherbee, J A" sort="Weatherbee, J A" uniqKey="Weatherbee J" first="J A" last="Weatherbee">J A Weatherbee</name></author></analytic><series><title level="j">Proceedings of the National Academy of Sciences of the United States of America</title><idno type="ISSN">0027-8424</idno><imprint><date when="1981" type="published">1981</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Bacterial Proteins (metabolism)</term><term>Female (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>HeLa Cells (enzymology)</term><term>Humans (MeSH)</term><term>Molecular Weight (MeSH)</term><term>NADH, NADPH Oxidoreductases (metabolism)</term><term>Oxidoreductases (MeSH)</term><term>Proteins (metabolism)</term><term>Thioredoxin-Disulfide Reductase (isolation & purification)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term><term>Thioredoxins (isolation & purification)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Cellules HeLa (enzymologie)</term><term>Femelle (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Masse moléculaire (MeSH)</term><term>NADH, NADPH oxidoreductases (métabolisme)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéines bactériennes (métabolisme)</term><term>Thioredoxin-disulfide reductase (isolement et purification)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxines (isolement et purification)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="isolation & purification" xml:lang="en"><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Bacterial Proteins</term><term>NADH, NADPH Oxidoreductases</term><term>Proteins</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Cellules HeLa</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>HeLa Cells</term></keywords><keywords scheme="MESH" qualifier="isolement et purification" xml:lang="fr"><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>NADH, NADPH oxidoreductases</term><term>Protéines</term><term>Protéines bactériennes</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Female</term><term>Glutaredoxins</term><term>Humans</term><term>Molecular Weight</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Femelle</term><term>Glutarédoxines</term><term>Humains</term><term>Masse moléculaire</term><term>Oxidoreductases</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin and glutaredoxin may be important in regulating cell metabolism by mediating interchanges between sulfhydryl and disulfide groups. Components of the thioredoxin/glutaredoxin system from cultured HeLa cells have been partially purified and characterized by using Escherichia coli adenosine 3'-phosphate 5'-phosphosulfate reductase, a thioredoxin/glutaredoxin-dependent enzyme on the pathway of sulfate reduction, as an assay system. In HeLa cells, a NADPH-thioredoxin reductase and three heat-labile proteins (designated PI, PII, and PIII) that have thioredoxin- or glutaredoxin-like properties are found. Both PI and PIII have molecular masses of approximately 12,000 daltons and are readily reduced by their homologous HeLa thioredoxin reductase. However, only PI can be reduced efficiently by the glutathione system and neither PI nor PIII has inherent glutathione-disulfide oxidoreductase activity. PII has a molecular mass of greater than 30,000 daltons and appears to be associated with a reductase activity. The HeLa NADPH-thioredoxin reductase has been purified to near homogeneity and found to be a 116,000-dalton flavoprotein composed of two 58,000-dalton subunits. The HeLa enzyme has low species and substrate specificity and can reduce HeLa PI and PIII, E. coli thioredoxin and glutaredoxin, and the disulfide bond in 5,5'-dithiobis(2-nitrobenzoic acid). The exact in vivo roles of the HeLa thioredoxin/glutaredoxin system remain to be determined.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">6950391</PMID><DateCompleted><Year>1982</Year><Month>05</Month><Day>21</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>01</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0027-8424</ISSN><JournalIssue CitedMedium="Print"><Volume>78</Volume><Issue>12</Issue><PubDate><Year>1981</Year><Month>Dec</Month></PubDate></JournalIssue><Title>Proceedings of the National Academy of Sciences of the United States of America</Title><ISOAbbreviation>Proc Natl Acad Sci U S A</ISOAbbreviation></Journal><ArticleTitle>Thioredoxin, glutaredoxin, and thioredoxin reductase from cultured HeLa cells.</ArticleTitle><Pagination><MedlinePgn>7478-82</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin and glutaredoxin may be important in regulating cell metabolism by mediating interchanges between sulfhydryl and disulfide groups. Components of the thioredoxin/glutaredoxin system from cultured HeLa cells have been partially purified and characterized by using Escherichia coli adenosine 3'-phosphate 5'-phosphosulfate reductase, a thioredoxin/glutaredoxin-dependent enzyme on the pathway of sulfate reduction, as an assay system. In HeLa cells, a NADPH-thioredoxin reductase and three heat-labile proteins (designated PI, PII, and PIII) that have thioredoxin- or glutaredoxin-like properties are found. Both PI and PIII have molecular masses of approximately 12,000 daltons and are readily reduced by their homologous HeLa thioredoxin reductase. However, only PI can be reduced efficiently by the glutathione system and neither PI nor PIII has inherent glutathione-disulfide oxidoreductase activity. PII has a molecular mass of greater than 30,000 daltons and appears to be associated with a reductase activity. The HeLa NADPH-thioredoxin reductase has been purified to near homogeneity and found to be a 116,000-dalton flavoprotein composed of two 58,000-dalton subunits. The HeLa enzyme has low species and substrate specificity and can reduce HeLa PI and PIII, E. coli thioredoxin and glutaredoxin, and the disulfide bond in 5,5'-dithiobis(2-nitrobenzoic acid). The exact in vivo roles of the HeLa thioredoxin/glutaredoxin system remain to be determined.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Tsang</LastName><ForeName>M L</ForeName><Initials>ML</Initials></Author><Author ValidYN="Y"><LastName>Weatherbee</LastName><ForeName>J A</ForeName><Initials>JA</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA-28078</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013486">Research Support, U.S. Gov't, Non-P.H.S.</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Proc Natl Acad Sci U S 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uniqKey="Tsang M" first="M L" last="Tsang">M L Tsang</name><name sortKey="Weatherbee, J A" sort="Weatherbee, J A" uniqKey="Weatherbee J" first="J A" last="Weatherbee">J A Weatherbee</name></noCountry></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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