Interactions of platinum complexes with thioltransferase(glutaredoxin), in vitro.
Identifieur interne : 001300 ( Main/Exploration ); précédent : 001299; suivant : 001301Interactions of platinum complexes with thioltransferase(glutaredoxin), in vitro.
Auteurs : W W Wells [États-Unis] ; P A Rocque ; D P Xu ; Y. Yang ; T L DeitsSource :
- Biochemical and biophysical research communications [ 0006-291X ] ; 1991.
Descripteurs français
- KwdFr :
- Anaérobiose (MeSH), Animaux (MeSH), Antinéoplasiques (pharmacologie), Aérobiose (MeSH), Carboplatine (pharmacologie), Cinétique (MeSH), Cisplatine (pharmacologie), Foie (enzymologie), Glutarédoxines (MeSH), Liaison aux protéines (MeSH), Masse moléculaire (MeSH), Oxidoreductases (antagonistes et inhibiteurs), Protein-disulfide reductase (glutathione) (MeSH), Protéines recombinantes (métabolisme), Structures macromoléculaires (MeSH), Suidae (MeSH).
- MESH :
- antagonistes et inhibiteurs : Oxidoreductases.
- enzymologie : Foie.
- métabolisme : Protéines recombinantes.
- pharmacologie : Antinéoplasiques, Carboplatine, Cisplatine.
- Anaérobiose, Animaux, Aérobiose, Cinétique, Glutarédoxines, Liaison aux protéines, Masse moléculaire, Protein-disulfide reductase (glutathione), Structures macromoléculaires, Suidae.
English descriptors
- KwdEn :
- Aerobiosis (MeSH), Anaerobiosis (MeSH), Animals (MeSH), Antineoplastic Agents (pharmacology), Carboplatin (pharmacology), Cisplatin (pharmacology), Glutaredoxins (MeSH), Kinetics (MeSH), Liver (enzymology), Macromolecular Substances (MeSH), Molecular Weight (MeSH), Oxidoreductases (antagonists & inhibitors), Protein Binding (MeSH), Protein Disulfide Reductase (Glutathione) (MeSH), Recombinant Proteins (metabolism), Swine (MeSH).
- MESH :
- chemical , antagonists & inhibitors : Oxidoreductases.
- chemical , metabolism : Recombinant Proteins.
- chemical , pharmacology : Antineoplastic Agents, Carboplatin, Cisplatin.
- enzymology : Liver.
- Aerobiosis, Anaerobiosis, Animals, Glutaredoxins, Kinetics, Macromolecular Substances, Molecular Weight, Protein Binding, Protein Disulfide Reductase (Glutathione), Swine.
Abstract
Under anaerobic conditions, recombinant pig liver thioltransferase (glutaredoxin)(TT, GRX) (EC 1.8.4.1) was strongly inhibited by cis and carbo-platin and somewhat less sensitive to trans-platin, in vitro. By extrapolation to total inhibition, the ratio of platinum drug/thioltransferase was approximately 1.0 for cis and carbo-platin, but greater than 1.0 for trans-platin. When thioltransferase was not reduced, inhibition by preincubation with the platinum complexes required molar excesses of 1,300 and 675 to one for cis-platin and trans-platin, respectively or 400-500 microM for 50% inhibition. The inhibition of thioltransferase at high drug concentrations in the presence of oxygen was associated with cross-linking of monomers into dimers within 5 min and, in the case of cis-platin treatment, to trimers in 20 min incubation.
DOI: 10.1016/s0006-291x(05)81127-1
PubMed: 1953747
Affiliations:
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Le document en format XML
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Yang</name></author><author><name sortKey="Deits, T L" sort="Deits, T L" uniqKey="Deits T" first="T L" last="Deits">T L Deits</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1991">1991</date><idno type="RBID">pubmed:1953747</idno><idno type="pmid">1953747</idno><idno type="doi">10.1016/s0006-291x(05)81127-1</idno><idno type="wicri:Area/Main/Corpus">001291</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001291</idno><idno type="wicri:Area/Main/Curation">001291</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001291</idno><idno type="wicri:Area/Main/Exploration">001291</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Interactions of platinum complexes with thioltransferase(glutaredoxin), in vitro.</title><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</nlm:affiliation><orgName type="university">Université d'État du Michigan</orgName><country>États-Unis</country><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Rocque, P A" sort="Rocque, P A" uniqKey="Rocque P" first="P A" last="Rocque">P A Rocque</name></author><author><name sortKey="Xu, D P" sort="Xu, D P" uniqKey="Xu D" first="D P" last="Xu">D P Xu</name></author><author><name sortKey="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. Yang</name></author><author><name sortKey="Deits, T L" sort="Deits, T L" uniqKey="Deits T" first="T L" last="Deits">T L Deits</name></author></analytic><series><title level="j">Biochemical and biophysical research communications</title><idno type="ISSN">0006-291X</idno><imprint><date when="1991" type="published">1991</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Aerobiosis (MeSH)</term><term>Anaerobiosis (MeSH)</term><term>Animals (MeSH)</term><term>Antineoplastic Agents (pharmacology)</term><term>Carboplatin (pharmacology)</term><term>Cisplatin (pharmacology)</term><term>Glutaredoxins (MeSH)</term><term>Kinetics (MeSH)</term><term>Liver (enzymology)</term><term>Macromolecular Substances (MeSH)</term><term>Molecular Weight (MeSH)</term><term>Oxidoreductases (antagonists & inhibitors)</term><term>Protein Binding (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Recombinant Proteins (metabolism)</term><term>Swine (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Anaérobiose (MeSH)</term><term>Animaux (MeSH)</term><term>Antinéoplasiques (pharmacologie)</term><term>Aérobiose (MeSH)</term><term>Carboplatine (pharmacologie)</term><term>Cinétique (MeSH)</term><term>Cisplatine (pharmacologie)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Liaison aux protéines (MeSH)</term><term>Masse moléculaire (MeSH)</term><term>Oxidoreductases (antagonistes et inhibiteurs)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Protéines recombinantes (métabolisme)</term><term>Structures macromoléculaires (MeSH)</term><term>Suidae (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antineoplastic Agents</term><term>Carboplatin</term><term>Cisplatin</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Foie</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Liver</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antinéoplasiques</term><term>Carboplatine</term><term>Cisplatine</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Aerobiosis</term><term>Anaerobiosis</term><term>Animals</term><term>Glutaredoxins</term><term>Kinetics</term><term>Macromolecular Substances</term><term>Molecular Weight</term><term>Protein Binding</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Anaérobiose</term><term>Animaux</term><term>Aérobiose</term><term>Cinétique</term><term>Glutarédoxines</term><term>Liaison aux protéines</term><term>Masse moléculaire</term><term>Protein-disulfide reductase (glutathione)</term><term>Structures macromoléculaires</term><term>Suidae</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Under anaerobic conditions, recombinant pig liver thioltransferase (glutaredoxin)(TT, GRX) (EC 1.8.4.1) was strongly inhibited by cis and carbo-platin and somewhat less sensitive to trans-platin, in vitro. By extrapolation to total inhibition, the ratio of platinum drug/thioltransferase was approximately 1.0 for cis and carbo-platin, but greater than 1.0 for trans-platin. When thioltransferase was not reduced, inhibition by preincubation with the platinum complexes required molar excesses of 1,300 and 675 to one for cis-platin and trans-platin, respectively or 400-500 microM for 50% inhibition. The inhibition of thioltransferase at high drug concentrations in the presence of oxygen was associated with cross-linking of monomers into dimers within 5 min and, in the case of cis-platin treatment, to trimers in 20 min incubation.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">1953747</PMID><DateCompleted><Year>1991</Year><Month>12</Month><Day>02</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>12</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0006-291X</ISSN><JournalIssue CitedMedium="Print"><Volume>180</Volume><Issue>2</Issue><PubDate><Year>1991</Year><Month>Oct</Month><Day>31</Day></PubDate></JournalIssue><Title>Biochemical and biophysical research communications</Title><ISOAbbreviation>Biochem Biophys Res Commun</ISOAbbreviation></Journal><ArticleTitle>Interactions of platinum complexes with thioltransferase(glutaredoxin), in vitro.</ArticleTitle><Pagination><MedlinePgn>735-41</MedlinePgn></Pagination><Abstract><AbstractText>Under anaerobic conditions, recombinant pig liver thioltransferase (glutaredoxin)(TT, GRX) (EC 1.8.4.1) was strongly inhibited by cis and carbo-platin and somewhat less sensitive to trans-platin, in vitro. By extrapolation to total inhibition, the ratio of platinum drug/thioltransferase was approximately 1.0 for cis and carbo-platin, but greater than 1.0 for trans-platin. When thioltransferase was not reduced, inhibition by preincubation with the platinum complexes required molar excesses of 1,300 and 675 to one for cis-platin and trans-platin, respectively or 400-500 microM for 50% inhibition. The inhibition of thioltransferase at high drug concentrations in the presence of oxygen was associated with cross-linking of monomers into dimers within 5 min and, in the case of cis-platin treatment, to trimers in 20 min incubation.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>W W</ForeName><Initials>WW</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Rocque</LastName><ForeName>P A</ForeName><Initials>PA</Initials></Author><Author ValidYN="Y"><LastName>Xu</LastName><ForeName>D P</ForeName><Initials>DP</Initials></Author><Author ValidYN="Y"><LastName>Yang</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Deits</LastName><ForeName>T L</ForeName><Initials>TL</Initials></Author></AuthorList><Language>eng</Language><GrantList 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Substances</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>14913-33-8</RegistryNumber><NameOfSubstance UI="C034697">transplatin</NameOfSubstance></Chemical><Chemical><RegistryNumber>BG3F62OND5</RegistryNumber><NameOfSubstance UI="D016190">Carboplatin</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.-</RegistryNumber><NameOfSubstance UI="D010088">Oxidoreductases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>Q20Q21Q62J</RegistryNumber><NameOfSubstance UI="D002945">Cisplatin</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000332" MajorTopicYN="N">Aerobiosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000693" MajorTopicYN="N">Anaerobiosis</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000970" MajorTopicYN="N">Antineoplastic Agents</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D016190" MajorTopicYN="N">Carboplatin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002945" MajorTopicYN="N">Cisplatin</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007700" MajorTopicYN="N">Kinetics</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D046911" MajorTopicYN="N">Macromolecular Substances</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008970" MajorTopicYN="N">Molecular Weight</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011485" MajorTopicYN="N">Protein Binding</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011994" MajorTopicYN="N">Recombinant Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013552" MajorTopicYN="N">Swine</DescriptorName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1991</Year><Month>10</Month><Day>31</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1991</Year><Month>10</Month><Day>31</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1991</Year><Month>10</Month><Day>31</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">1953747</ArticleId><ArticleId IdType="pii">S0006-291X(05)81127-1</ArticleId><ArticleId IdType="doi">10.1016/s0006-291x(05)81127-1</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>États-Unis</li></country><region><li>Michigan</li></region><settlement><li>East Lansing</li></settlement><orgName><li>Université d'État du Michigan</li></orgName></list><tree><noCountry><name sortKey="Deits, T L" sort="Deits, T L" uniqKey="Deits T" first="T L" last="Deits">T L Deits</name><name sortKey="Rocque, P A" sort="Rocque, P A" uniqKey="Rocque P" first="P A" last="Rocque">P A Rocque</name><name sortKey="Xu, D P" sort="Xu, D P" uniqKey="Xu D" first="D P" last="Xu">D P Xu</name><name sortKey="Yang, Y" sort="Yang, Y" uniqKey="Yang Y" first="Y" last="Yang">Y. Yang</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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