Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.
Identifieur interne : 001174 ( Main/Exploration ); précédent : 001173; suivant : 001175Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.
Auteurs : M P Washburn [États-Unis] ; W W WellsSource :
- Free radical biology & medicine [ 0891-5849 ] ; 1997.
Descripteurs français
- KwdFr :
- Alloxane (métabolisme), Alloxane (toxicité), Animaux (MeSH), Barbituriques (métabolisme), Catalase (pharmacologie), Catalyse (MeSH), Cinétique (MeSH), Consommation d'oxygène (MeSH), Foie (enzymologie), Glutarédoxines (MeSH), Glutathion (métabolisme), NADP (métabolisme), Oxidoreductases (MeSH), Oxydoréduction (MeSH), Protéines (métabolisme), Protéines recombinantes (métabolisme), Spectrophotométrie (MeSH), Suidae (MeSH), Superoxide dismutase (pharmacologie).
- MESH :
- enzymologie : Foie.
- métabolisme : Alloxane, Barbituriques, Glutathion, NADP, Protéines, Protéines recombinantes.
- pharmacologie : Catalase, Superoxide dismutase.
- toxicité : Alloxane.
- Animaux, Catalyse, Cinétique, Consommation d'oxygène, Glutarédoxines, Oxidoreductases, Oxydoréduction, Spectrophotométrie, Suidae.
English descriptors
- KwdEn :
- Alloxan (metabolism), Alloxan (toxicity), Animals (MeSH), Barbiturates (metabolism), Catalase (pharmacology), Catalysis (MeSH), Glutaredoxins (MeSH), Glutathione (metabolism), Kinetics (MeSH), Liver (enzymology), NADP (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (MeSH), Oxygen Consumption (MeSH), Proteins (metabolism), Recombinant Proteins (metabolism), Spectrophotometry (MeSH), Superoxide Dismutase (pharmacology), Swine (MeSH).
- MESH :
- chemical , metabolism : Alloxan, Barbiturates, Glutathione, NADP, Proteins, Recombinant Proteins.
- chemical , pharmacology : Catalase, Superoxide Dismutase.
- chemical , toxicity : Alloxan.
- enzymology : Liver.
- Animals, Catalysis, Glutaredoxins, Kinetics, Oxidation-Reduction, Oxidoreductases, Oxygen Consumption, Spectrophotometry, Swine.
Abstract
Recombinant pig liver thioltransferase (rPLTT) catalyzes the reduction of alloxan to dialuric acid by glutathione (GSH). This is the second non-disulfide substrate, after dehydroascorbic acid, described for thioltransferase. The reaction kinetics, measured by a coupled assay including glutathione disulfide reductase and NADPH yielded a Km = 82 microM for alloxan, a k(cat) = 37 s(-1), and a k(cat)/Km = 4.5 x 10(5) M(-1) s(-1). The presence of rPLTT suppressed the competitive formation of compound 305, an alloxan-GSH conjugate of unknown structure, and at GSH concentrations between 0.05 mM and 1.5 mM, oxygen consumption was greater than that recorded in the uncatalyzed reaction. Both superoxide dismutase and catalase inhibited oxygen consumption in 1.0 mM GSH and 0.2 mM alloxan in the presence of rPLTT. This study suggests that thioltransferase (glutaredoxin) plays a significant role in the cytotoxicity of alloxan in vulnerable tissues.
DOI: 10.1016/s0891-5849(97)00001-4
PubMed: 9215802
Affiliations:
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Le document en format XML
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Wells</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1997">1997</date><idno type="RBID">pubmed:9215802</idno><idno type="pmid">9215802</idno><idno type="doi">10.1016/s0891-5849(97)00001-4</idno><idno type="wicri:Area/Main/Corpus">001182</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001182</idno><idno type="wicri:Area/Main/Curation">001182</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001182</idno><idno type="wicri:Area/Main/Exploration">001182</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.</title><author><name sortKey="Washburn, M P" sort="Washburn, M P" uniqKey="Washburn M" first="M P" last="Washburn">M P Washburn</name><affiliation wicri:level="4"><nlm:affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</nlm:affiliation><country xml:lang="fr">États-Unis</country><wicri:regionArea>Department of Biochemistry, Michigan State University, East Lansing 48824</wicri:regionArea><orgName type="university">Université d'État du Michigan</orgName><placeName><settlement type="city">East Lansing</settlement><region type="state">Michigan</region></placeName></affiliation></author><author><name sortKey="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></author></analytic><series><title level="j">Free radical biology & medicine</title><idno type="ISSN">0891-5849</idno><imprint><date when="1997" type="published">1997</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Alloxan (metabolism)</term><term>Alloxan (toxicity)</term><term>Animals (MeSH)</term><term>Barbiturates (metabolism)</term><term>Catalase (pharmacology)</term><term>Catalysis (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Glutathione (metabolism)</term><term>Kinetics (MeSH)</term><term>Liver (enzymology)</term><term>NADP (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Oxygen Consumption (MeSH)</term><term>Proteins (metabolism)</term><term>Recombinant Proteins (metabolism)</term><term>Spectrophotometry (MeSH)</term><term>Superoxide Dismutase (pharmacology)</term><term>Swine (MeSH)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Alloxane (métabolisme)</term><term>Alloxane (toxicité)</term><term>Animaux (MeSH)</term><term>Barbituriques (métabolisme)</term><term>Catalase (pharmacologie)</term><term>Catalyse (MeSH)</term><term>Cinétique (MeSH)</term><term>Consommation d'oxygène (MeSH)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (métabolisme)</term><term>NADP (métabolisme)</term><term>Oxidoreductases (MeSH)</term><term>Oxydoréduction (MeSH)</term><term>Protéines (métabolisme)</term><term>Protéines recombinantes (métabolisme)</term><term>Spectrophotométrie (MeSH)</term><term>Suidae (MeSH)</term><term>Superoxide dismutase (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Alloxan</term><term>Barbiturates</term><term>Glutathione</term><term>NADP</term><term>Proteins</term><term>Recombinant Proteins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Catalase</term><term>Superoxide Dismutase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="toxicity" xml:lang="en"><term>Alloxan</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>Alloxane</term><term>Barbituriques</term><term>Glutathion</term><term>NADP</term><term>Protéines</term><term>Protéines recombinantes</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Catalase</term><term>Superoxide dismutase</term></keywords><keywords scheme="MESH" qualifier="toxicité" xml:lang="fr"><term>Alloxane</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Catalysis</term><term>Glutaredoxins</term><term>Kinetics</term><term>Oxidation-Reduction</term><term>Oxidoreductases</term><term>Oxygen Consumption</term><term>Spectrophotometry</term><term>Swine</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Catalyse</term><term>Cinétique</term><term>Consommation d'oxygène</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Oxydoréduction</term><term>Spectrophotométrie</term><term>Suidae</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Recombinant pig liver thioltransferase (rPLTT) catalyzes the reduction of alloxan to dialuric acid by glutathione (GSH). This is the second non-disulfide substrate, after dehydroascorbic acid, described for thioltransferase. The reaction kinetics, measured by a coupled assay including glutathione disulfide reductase and NADPH yielded a Km = 82 microM for alloxan, a k(cat) = 37 s(-1), and a k(cat)/Km = 4.5 x 10(5) M(-1) s(-1). The presence of rPLTT suppressed the competitive formation of compound 305, an alloxan-GSH conjugate of unknown structure, and at GSH concentrations between 0.05 mM and 1.5 mM, oxygen consumption was greater than that recorded in the uncatalyzed reaction. Both superoxide dismutase and catalase inhibited oxygen consumption in 1.0 mM GSH and 0.2 mM alloxan in the presence of rPLTT. This study suggests that thioltransferase (glutaredoxin) plays a significant role in the cytotoxicity of alloxan in vulnerable tissues.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">9215802</PMID><DateCompleted><Year>1997</Year><Month>09</Month><Day>05</Day></DateCompleted><DateRevised><Year>2019</Year><Month>08</Month><Day>26</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0891-5849</ISSN><JournalIssue CitedMedium="Print"><Volume>23</Volume><Issue>4</Issue><PubDate><Year>1997</Year></PubDate></JournalIssue><Title>Free radical biology & medicine</Title><ISOAbbreviation>Free Radic Biol Med</ISOAbbreviation></Journal><ArticleTitle>Glutathione dependent reduction of alloxan to dialuric acid catalyzed by thioltransferase (glutaredoxin): a possible role for thioltransferase in alloxan toxicity.</ArticleTitle><Pagination><MedlinePgn>563-70</MedlinePgn></Pagination><Abstract><AbstractText>Recombinant pig liver thioltransferase (rPLTT) catalyzes the reduction of alloxan to dialuric acid by glutathione (GSH). This is the second non-disulfide substrate, after dehydroascorbic acid, described for thioltransferase. The reaction kinetics, measured by a coupled assay including glutathione disulfide reductase and NADPH yielded a Km = 82 microM for alloxan, a k(cat) = 37 s(-1), and a k(cat)/Km = 4.5 x 10(5) M(-1) s(-1). The presence of rPLTT suppressed the competitive formation of compound 305, an alloxan-GSH conjugate of unknown structure, and at GSH concentrations between 0.05 mM and 1.5 mM, oxygen consumption was greater than that recorded in the uncatalyzed reaction. Both superoxide dismutase and catalase inhibited oxygen consumption in 1.0 mM GSH and 0.2 mM alloxan in the presence of rPLTT. This study suggests that thioltransferase (glutaredoxin) plays a significant role in the cytotoxicity of alloxan in vulnerable tissues.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Washburn</LastName><ForeName>M P</ForeName><Initials>MP</Initials><AffiliationInfo><Affiliation>Department of Biochemistry, Michigan State University, East Lansing 48824, USA.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Wells</LastName><ForeName>W W</ForeName><Initials>WW</Initials></Author></AuthorList><Language>eng</Language><GrantList CompleteYN="Y"><Grant><GrantID>CA-51972</GrantID><Acronym>CA</Acronym><Agency>NCI NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>DK-44456</GrantID><Acronym>DK</Acronym><Agency>NIDDK NIH HHS</Agency><Country>United States</Country></Grant><Grant><GrantID>ES-07255</GrantID><Acronym>ES</Acronym><Agency>NIEHS NIH HHS</Agency><Country>United States</Country></Grant></GrantList><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>United States</Country><MedlineTA>Free Radic Biol Med</MedlineTA><NlmUniqueID>8709159</NlmUniqueID><ISSNLinking>0891-5849</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D001463">Barbiturates</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011994">Recombinant Proteins</NameOfSubstance></Chemical><Chemical><RegistryNumber>444-15-5</RegistryNumber><NameOfSubstance UI="C004718">dialuric 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IdType="pii">S0891-5849(97)00001-4</ArticleId><ArticleId IdType="doi">10.1016/s0891-5849(97)00001-4</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="Wells, W W" sort="Wells, W W" uniqKey="Wells W" first="W W" last="Wells">W W Wells</name></noCountry><country name="États-Unis"><region name="Michigan"><name sortKey="Washburn, M P" sort="Washburn, M P" uniqKey="Washburn M" first="M P" last="Washburn">M P Washburn</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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