Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione.
Identifieur interne : 001194 ( Main/Exploration ); précédent : 001193; suivant : 001195Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione.
Auteurs : M L Martínez-Chantar [Espagne] ; M A PajaresSource :
- FEBS letters [ 0014-5793 ] ; 1996.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Concentration en ions d'hydrogène (MeSH), Disulfures (métabolisme), Foie (enzymologie), Glutarédoxines (MeSH), Glutathion (pharmacologie), Isomerases (métabolisme), Isomerases (pharmacologie), Methionine adenosyltransferase (antagonistes et inhibiteurs), Methionine adenosyltransferase (composition chimique), Methionine adenosyltransferase (métabolisme), Mâle (MeSH), Oxidoreductases (métabolisme), Oxidoreductases (pharmacologie), Oxydoréduction (MeSH), Protein Disulfide-Isomerases (MeSH), Protein-disulfide reductase (glutathione) (MeSH), Rat Wistar (MeSH), Rats (MeSH), Thiorédoxines (métabolisme), Thiorédoxines (pharmacologie).
- MESH :
- antagonistes et inhibiteurs : Methionine adenosyltransferase.
- composition chimique : Methionine adenosyltransferase.
- enzymologie : Foie.
- métabolisme : Disulfures, Isomerases, Methionine adenosyltransferase, Oxidoreductases, Thiorédoxines.
- pharmacologie : Glutathion, Isomerases, Oxidoreductases, Thiorédoxines.
- Animaux, Concentration en ions d'hydrogène, Glutarédoxines, Mâle, Oxydoréduction, Protein Disulfide-Isomerases, Protein-disulfide reductase (glutathione), Rat Wistar, Rats.
English descriptors
- KwdEn :
- Animals (MeSH), Disulfides (metabolism), Glutaredoxins (MeSH), Glutathione (pharmacology), Hydrogen-Ion Concentration (MeSH), Isomerases (metabolism), Isomerases (pharmacology), Liver (enzymology), Male (MeSH), Methionine Adenosyltransferase (antagonists & inhibitors), Methionine Adenosyltransferase (chemistry), Methionine Adenosyltransferase (metabolism), Oxidation-Reduction (MeSH), Oxidoreductases (metabolism), Oxidoreductases (pharmacology), Protein Disulfide Reductase (Glutathione) (MeSH), Protein Disulfide-Isomerases (MeSH), Rats (MeSH), Rats, Wistar (MeSH), Thioredoxins (metabolism), Thioredoxins (pharmacology).
- MESH :
- chemical , antagonists & inhibitors : Methionine Adenosyltransferase.
- chemical , chemistry : Methionine Adenosyltransferase.
- chemical , metabolism : Disulfides, Isomerases, Methionine Adenosyltransferase, Oxidoreductases, Thioredoxins.
- chemical , pharmacology : Glutathione, Isomerases, Oxidoreductases, Thioredoxins.
- enzymology : Liver.
- Animals, Glutaredoxins, Hydrogen-Ion Concentration, Male, Oxidation-Reduction, Protein Disulfide Reductase (Glutathione), Protein Disulfide-Isomerases, Rats, Rats, Wistar.
Abstract
Rat liver S-adenosylmethionine synthetase, high- and low-Mr forms, are regulated in vitro by the GSH/GSSG ratio at pH 8. The inhibition and oxidation constants for both forms have been calculated in the presence of thioltransferases. The mechanism of the reaction appeared to involve the formation of intramolecular disulfides. Increases of 3- to 4-fold in the oxidation constants for both S-adenosylmethionine synthetase isoenzymes in the presence of protein disulfide isomerase suggested the possibility of a thiol-disulfide exchange regulatory mechanism for this enzyme in vivo. The significance of these results is discussed on the light of the data available relating glutathione changes and modulation of enzyme activities, either in vivo and in vitro.
DOI: 10.1016/s0014-5793(96)01201-x
PubMed: 8955366
Affiliations:
Links toward previous steps (curation, corpus...)
Le document en format XML
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Adenosyltransferase (antagonists & inhibitors)</term><term>Methionine Adenosyltransferase (chemistry)</term><term>Methionine Adenosyltransferase (metabolism)</term><term>Oxidation-Reduction (MeSH)</term><term>Oxidoreductases (metabolism)</term><term>Oxidoreductases (pharmacology)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Protein Disulfide-Isomerases (MeSH)</term><term>Rats (MeSH)</term><term>Rats, Wistar (MeSH)</term><term>Thioredoxins (metabolism)</term><term>Thioredoxins (pharmacology)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Concentration en ions d'hydrogène (MeSH)</term><term>Disulfures (métabolisme)</term><term>Foie (enzymologie)</term><term>Glutarédoxines (MeSH)</term><term>Glutathion (pharmacologie)</term><term>Isomerases (métabolisme)</term><term>Isomerases (pharmacologie)</term><term>Methionine adenosyltransferase (antagonistes et inhibiteurs)</term><term>Methionine adenosyltransferase (composition chimique)</term><term>Methionine adenosyltransferase (métabolisme)</term><term>Mâle (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Oxidoreductases (pharmacologie)</term><term>Oxydoréduction (MeSH)</term><term>Protein Disulfide-Isomerases (MeSH)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Rat Wistar (MeSH)</term><term>Rats (MeSH)</term><term>Thiorédoxines (métabolisme)</term><term>Thiorédoxines (pharmacologie)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="antagonists & inhibitors" xml:lang="en"><term>Methionine Adenosyltransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="chemistry" xml:lang="en"><term>Methionine Adenosyltransferase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Disulfides</term><term>Isomerases</term><term>Methionine Adenosyltransferase</term><term>Oxidoreductases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Glutathione</term><term>Isomerases</term><term>Oxidoreductases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" qualifier="antagonistes et inhibiteurs" xml:lang="fr"><term>Methionine adenosyltransferase</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Methionine adenosyltransferase</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>Disulfures</term><term>Isomerases</term><term>Methionine adenosyltransferase</term><term>Oxidoreductases</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Glutathion</term><term>Isomerases</term><term>Oxidoreductases</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Glutaredoxins</term><term>Hydrogen-Ion Concentration</term><term>Male</term><term>Oxidation-Reduction</term><term>Protein Disulfide Reductase (Glutathione)</term><term>Protein Disulfide-Isomerases</term><term>Rats</term><term>Rats, Wistar</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Concentration en ions d'hydrogène</term><term>Glutarédoxines</term><term>Mâle</term><term>Oxydoréduction</term><term>Protein Disulfide-Isomerases</term><term>Protein-disulfide reductase (glutathione)</term><term>Rat Wistar</term><term>Rats</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Rat liver S-adenosylmethionine synthetase, high- and low-Mr forms, are regulated in vitro by the GSH/GSSG ratio at pH 8. The inhibition and oxidation constants for both forms have been calculated in the presence of thioltransferases. The mechanism of the reaction appeared to involve the formation of intramolecular disulfides. Increases of 3- to 4-fold in the oxidation constants for both S-adenosylmethionine synthetase isoenzymes in the presence of protein disulfide isomerase suggested the possibility of a thiol-disulfide exchange regulatory mechanism for this enzyme in vivo. The significance of these results is discussed on the light of the data available relating glutathione changes and modulation of enzyme activities, either in vivo and in vitro.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8955366</PMID><DateCompleted><Year>1997</Year><Month>01</Month><Day>13</Day></DateCompleted><DateRevised><Year>2019</Year><Month>06</Month><Day>21</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0014-5793</ISSN><JournalIssue CitedMedium="Print"><Volume>397</Volume><Issue>2-3</Issue><PubDate><Year>1996</Year><Month>Nov</Month><Day>18</Day></PubDate></JournalIssue><Title>FEBS letters</Title><ISOAbbreviation>FEBS Lett</ISOAbbreviation></Journal><ArticleTitle>Role of thioltransferases on the modulation of rat liver S-adenosylmethionine synthetase activity by glutathione.</ArticleTitle><Pagination><MedlinePgn>293-7</MedlinePgn></Pagination><Abstract><AbstractText>Rat liver S-adenosylmethionine synthetase, high- and low-Mr forms, are regulated in vitro by the GSH/GSSG ratio at pH 8. The inhibition and oxidation constants for both forms have been calculated in the presence of thioltransferases. The mechanism of the reaction appeared to involve the formation of intramolecular disulfides. Increases of 3- to 4-fold in the oxidation constants for both S-adenosylmethionine synthetase isoenzymes in the presence of protein disulfide isomerase suggested the possibility of a thiol-disulfide exchange regulatory mechanism for this enzyme in vivo. The significance of these results is discussed on the light of the data available relating glutathione changes and modulation of enzyme activities, either in vivo and in vitro.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Martínez-Chantar</LastName><ForeName>M L</ForeName><Initials>ML</Initials><AffiliationInfo><Affiliation>Instituto de Investigaciones Biomédicas (CSIC), Madrid, Spain.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Pajares</LastName><ForeName>M A</ForeName><Initials>MA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013485">Research Support, Non-U.S. Gov't</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>England</Country><MedlineTA>FEBS Lett</MedlineTA><NlmUniqueID>0155157</NlmUniqueID><ISSNLinking>0014-5793</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004220">Disulfides</NameOfSubstance></Chemical><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><Chemical><RegistryNumber>EC 1.8.4.2</RegistryNumber><NameOfSubstance UI="D011490">Protein Disulfide Reductase (Glutathione)</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 2.5.1.6</RegistryNumber><NameOfSubstance UI="D008716">Methionine Adenosyltransferase</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.-</RegistryNumber><NameOfSubstance UI="D007535">Isomerases</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 5.3.4.1</RegistryNumber><NameOfSubstance UI="D019704">Protein Disulfide-Isomerases</NameOfSubstance></Chemical><Chemical><RegistryNumber>GAN16C9B8O</RegistryNumber><NameOfSubstance UI="D005978">Glutathione</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004220" MajorTopicYN="N">Disulfides</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D005978" MajorTopicYN="N">Glutathione</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D006863" MajorTopicYN="N">Hydrogen-Ion Concentration</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007535" MajorTopicYN="N">Isomerases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008099" MajorTopicYN="N">Liver</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008716" MajorTopicYN="N">Methionine Adenosyltransferase</DescriptorName><QualifierName UI="Q000037" MajorTopicYN="Y">antagonists & inhibitors</QualifierName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010084" MajorTopicYN="N">Oxidation-Reduction</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D019704" MajorTopicYN="N">Protein Disulfide-Isomerases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017208" MajorTopicYN="N">Rats, Wistar</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1996</Year><Month>11</Month><Day>18</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1996</Year><Month>11</Month><Day>18</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1996</Year><Month>11</Month><Day>18</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8955366</ArticleId><ArticleId IdType="pii">S0014-5793(96)01201-X</ArticleId><ArticleId IdType="doi">10.1016/s0014-5793(96)01201-x</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Espagne</li></country><region><li>Communauté de Madrid</li></region><settlement><li>Madrid</li></settlement></list><tree><noCountry><name sortKey="Pajares, M A" sort="Pajares, M A" uniqKey="Pajares M" first="M A" last="Pajares">M A Pajares</name></noCountry><country name="Espagne"><region name="Communauté de Madrid"><name sortKey="Martinez Chantar, M L" sort="Martinez Chantar, M L" uniqKey="Martinez Chantar M" first="M L" last="Martínez-Chantar">M L Martínez-Chantar</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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