17beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress.
Identifieur interne : 001118 ( Main/Exploration ); précédent : 001117; suivant : 00111917beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress.
Auteurs : K. Ejima [Japon] ; H. Nanri ; M. Araki ; K. Uchida ; M. Kashimura ; M. IkedaSource :
- European journal of endocrinology [ 0804-4643 ] ; 1999.
Descripteurs français
- KwdFr :
- Animaux (MeSH), Antioxydants (pharmacologie), Aorte (MeSH), Bovins (MeSH), Cellules cultivées (MeSH), Endothélium vasculaire (effets des médicaments et des substances chimiques), Endothélium vasculaire (métabolisme), Glutarédoxines (MeSH), Oestradiol (pharmacologie), Oxidoreductases (MeSH), Protein Disulfide-Isomerases (métabolisme), Protein-disulfide reductase (glutathione) (biosynthèse), Protéines (métabolisme), Stress oxydatif (MeSH), Thioredoxin-disulfide reductase (métabolisme), Thiorédoxines (métabolisme).
- MESH :
- biosynthèse : Protein-disulfide reductase (glutathione).
- effets des médicaments et des substances chimiques : Endothélium vasculaire.
- métabolisme : Endothélium vasculaire, Protein Disulfide-Isomerases, Protéines, Thioredoxin-disulfide reductase, Thiorédoxines.
- pharmacologie : Antioxydants, Oestradiol.
- Animaux, Aorte, Bovins, Cellules cultivées, Glutarédoxines, Oxidoreductases, Stress oxydatif.
English descriptors
- KwdEn :
- Animals (MeSH), Antioxidants (pharmacology), Aorta (MeSH), Cattle (MeSH), Cells, Cultured (MeSH), Endothelium, Vascular (drug effects), Endothelium, Vascular (metabolism), Estradiol (pharmacology), Glutaredoxins (MeSH), Oxidative Stress (MeSH), Oxidoreductases (MeSH), Protein Disulfide Reductase (Glutathione) (biosynthesis), Protein Disulfide-Isomerases (metabolism), Proteins (metabolism), Thioredoxin-Disulfide Reductase (metabolism), Thioredoxins (metabolism).
- MESH :
- chemical , biosynthesis : Protein Disulfide Reductase (Glutathione).
- chemical , metabolism : Protein Disulfide-Isomerases, Proteins, Thioredoxin-Disulfide Reductase, Thioredoxins.
- chemical , pharmacology : Antioxidants, Estradiol.
- drug effects : Endothelium, Vascular.
- metabolism : Endothelium, Vascular.
- Animals, Aorta, Cattle, Cells, Cultured, Glutaredoxins, Oxidative Stress, Oxidoreductases.
Abstract
OBJECTIVE
To examine whether or not estrogens induced the expression of protein thiol/disulfide oxidoreductases such as protein disulfide isomerase (PDI), thioredoxin (Trx), Trx reductase, and glutaredoxin (Grx) in vascular endothelial cells.
METHODS
The regenerative effects of the protein thiol/disulfide oxidoreductases, PDI, Trx and Grx, on oxidatively damaged proteins were assayed using H2O2-inactivated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a reporter enzyme. The induction of protein thiol/disulfide oxidoreductases and the accumulation of protein adducts generated by lipid peroxidation were examined by Western blotting in estrogen-treated bovine aortic endothelial cells (BAECs).
RESULTS
Reduced PDI, Trx and Grx regenerated the H2O2-inactivated GAPDH in vitro. The levels of these protein disulfide oxidoreductases in BAECs were increased by pretreatment with 0.01-10 micromol/l 17beta-estradiol, the largest increase (about fourfold of the control) being found for PDI. Other sex hormones such as progesterone and testosterone did not affect the contents of these oxidoreductases in BAECs. 4-Hydroxy-2-nonenal (HNE)-protein adducts, which are generated by lipid peroxidation, were accumulated in BAECs exposed to paraquat, whereas the pretreatment of BAECs with 17beta-estradiol suppressed their accumulation.
CONCLUSIONS
The estrogen-mediated induction of the protein thiol/disulfide oxidoreductases such as PDI, Trx, Trx reductase and Grx suggested a possible involvement of these oxidoreductases in the antioxidant protection of estrogen observed in the vascular system.
DOI: 10.1530/eje.0.1400608
PubMed: 10366417
Affiliations:
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Araki</name></author><author><name sortKey="Uchida, K" sort="Uchida, K" uniqKey="Uchida K" first="K" last="Uchida">K. Uchida</name></author><author><name sortKey="Kashimura, M" sort="Kashimura, M" uniqKey="Kashimura M" first="M" last="Kashimura">M. Kashimura</name></author><author><name sortKey="Ikeda, M" sort="Ikeda, M" uniqKey="Ikeda M" first="M" last="Ikeda">M. Ikeda</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1999">1999</date><idno type="RBID">pubmed:10366417</idno><idno type="pmid">10366417</idno><idno type="doi">10.1530/eje.0.1400608</idno><idno type="wicri:Area/Main/Corpus">001106</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">001106</idno><idno type="wicri:Area/Main/Curation">001106</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Curation">001106</idno><idno type="wicri:Area/Main/Exploration">001106</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">17beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress.</title><author><name sortKey="Ejima, K" sort="Ejima, K" uniqKey="Ejima K" first="K" last="Ejima">K. Ejima</name><affiliation wicri:level="1"><nlm:affiliation>Department of Health Development, University of Occupational and Environmental Health, Kitakyushu 807-8555, Japan.</nlm:affiliation><country xml:lang="fr">Japon</country><wicri:regionArea>Department of Health Development, University of Occupational and Environmental Health, Kitakyushu 807-8555</wicri:regionArea><wicri:noRegion>Kitakyushu 807-8555</wicri:noRegion></affiliation></author><author><name sortKey="Nanri, H" sort="Nanri, H" uniqKey="Nanri H" first="H" last="Nanri">H. Nanri</name></author><author><name sortKey="Araki, M" sort="Araki, M" uniqKey="Araki M" first="M" last="Araki">M. Araki</name></author><author><name sortKey="Uchida, K" sort="Uchida, K" uniqKey="Uchida K" first="K" last="Uchida">K. Uchida</name></author><author><name sortKey="Kashimura, M" sort="Kashimura, M" uniqKey="Kashimura M" first="M" last="Kashimura">M. Kashimura</name></author><author><name sortKey="Ikeda, M" sort="Ikeda, M" uniqKey="Ikeda M" first="M" last="Ikeda">M. Ikeda</name></author></analytic><series><title level="j">European journal of endocrinology</title><idno type="ISSN">0804-4643</idno><imprint><date when="1999" type="published">1999</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Antioxidants (pharmacology)</term><term>Aorta (MeSH)</term><term>Cattle (MeSH)</term><term>Cells, Cultured (MeSH)</term><term>Endothelium, Vascular (drug effects)</term><term>Endothelium, Vascular (metabolism)</term><term>Estradiol (pharmacology)</term><term>Glutaredoxins (MeSH)</term><term>Oxidative Stress (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Protein Disulfide Reductase (Glutathione) (biosynthesis)</term><term>Protein Disulfide-Isomerases (metabolism)</term><term>Proteins (metabolism)</term><term>Thioredoxin-Disulfide Reductase (metabolism)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Animaux (MeSH)</term><term>Antioxydants (pharmacologie)</term><term>Aorte (MeSH)</term><term>Bovins (MeSH)</term><term>Cellules cultivées (MeSH)</term><term>Endothélium vasculaire (effets des médicaments et des substances chimiques)</term><term>Endothélium vasculaire (métabolisme)</term><term>Glutarédoxines (MeSH)</term><term>Oestradiol (pharmacologie)</term><term>Oxidoreductases (MeSH)</term><term>Protein Disulfide-Isomerases (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (biosynthèse)</term><term>Protéines (métabolisme)</term><term>Stress oxydatif (MeSH)</term><term>Thioredoxin-disulfide reductase (métabolisme)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Protein Disulfide-Isomerases</term><term>Proteins</term><term>Thioredoxin-Disulfide Reductase</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Antioxidants</term><term>Estradiol</term></keywords><keywords scheme="MESH" qualifier="biosynthèse" xml:lang="fr"><term>Protein-disulfide reductase (glutathione)</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Endothelium, Vascular</term></keywords><keywords scheme="MESH" qualifier="effets des médicaments et des substances chimiques" xml:lang="fr"><term>Endothélium vasculaire</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endothelium, Vascular</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endothélium vasculaire</term><term>Protein Disulfide-Isomerases</term><term>Protéines</term><term>Thioredoxin-disulfide reductase</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="pharmacologie" xml:lang="fr"><term>Antioxydants</term><term>Oestradiol</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Aorta</term><term>Cattle</term><term>Cells, Cultured</term><term>Glutaredoxins</term><term>Oxidative Stress</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Animaux</term><term>Aorte</term><term>Bovins</term><term>Cellules cultivées</term><term>Glutarédoxines</term><term>Oxidoreductases</term><term>Stress oxydatif</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en"><p><b>OBJECTIVE</b></p><p>To examine whether or not estrogens induced the expression of protein thiol/disulfide oxidoreductases such as protein disulfide isomerase (PDI), thioredoxin (Trx), Trx reductase, and glutaredoxin (Grx) in vascular endothelial cells.</p></div><div type="abstract" xml:lang="en"><p><b>METHODS</b></p><p>The regenerative effects of the protein thiol/disulfide oxidoreductases, PDI, Trx and Grx, on oxidatively damaged proteins were assayed using H2O2-inactivated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a reporter enzyme. The induction of protein thiol/disulfide oxidoreductases and the accumulation of protein adducts generated by lipid peroxidation were examined by Western blotting in estrogen-treated bovine aortic endothelial cells (BAECs).</p></div><div type="abstract" xml:lang="en"><p><b>RESULTS</b></p><p>Reduced PDI, Trx and Grx regenerated the H2O2-inactivated GAPDH in vitro. The levels of these protein disulfide oxidoreductases in BAECs were increased by pretreatment with 0.01-10 micromol/l 17beta-estradiol, the largest increase (about fourfold of the control) being found for PDI. Other sex hormones such as progesterone and testosterone did not affect the contents of these oxidoreductases in BAECs. 4-Hydroxy-2-nonenal (HNE)-protein adducts, which are generated by lipid peroxidation, were accumulated in BAECs exposed to paraquat, whereas the pretreatment of BAECs with 17beta-estradiol suppressed their accumulation.</p></div><div type="abstract" xml:lang="en"><p><b>CONCLUSIONS</b></p><p>The estrogen-mediated induction of the protein thiol/disulfide oxidoreductases such as PDI, Trx, Trx reductase and Grx suggested a possible involvement of these oxidoreductases in the antioxidant protection of estrogen observed in the vascular system.</p></div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">10366417</PMID><DateCompleted><Year>1999</Year><Month>07</Month><Day>28</Day></DateCompleted><DateRevised><Year>2019</Year><Month>09</Month><Day>05</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0804-4643</ISSN><JournalIssue CitedMedium="Print"><Volume>140</Volume><Issue>6</Issue><PubDate><Year>1999</Year><Month>Jun</Month></PubDate></JournalIssue><Title>European journal of endocrinology</Title><ISOAbbreviation>Eur J Endocrinol</ISOAbbreviation></Journal><ArticleTitle>17beta-estradiol induces protein thiol/disulfide oxidoreductases and protects cultured bovine aortic endothelial cells from oxidative stress.</ArticleTitle><Pagination><MedlinePgn>608-13</MedlinePgn></Pagination><Abstract><AbstractText Label="OBJECTIVE" NlmCategory="OBJECTIVE">To examine whether or not estrogens induced the expression of protein thiol/disulfide oxidoreductases such as protein disulfide isomerase (PDI), thioredoxin (Trx), Trx reductase, and glutaredoxin (Grx) in vascular endothelial cells.</AbstractText><AbstractText Label="METHODS" NlmCategory="METHODS">The regenerative effects of the protein thiol/disulfide oxidoreductases, PDI, Trx and Grx, on oxidatively damaged proteins were assayed using H2O2-inactivated glyceraldehyde-3-phosphate dehydrogenase (GAPDH) as a reporter enzyme. The induction of protein thiol/disulfide oxidoreductases and the accumulation of protein adducts generated by lipid peroxidation were examined by Western blotting in estrogen-treated bovine aortic endothelial cells (BAECs).</AbstractText><AbstractText Label="RESULTS" NlmCategory="RESULTS">Reduced PDI, Trx and Grx regenerated the H2O2-inactivated GAPDH in vitro. The levels of these protein disulfide oxidoreductases in BAECs were increased by pretreatment with 0.01-10 micromol/l 17beta-estradiol, the largest increase (about fourfold of the control) being found for PDI. Other sex hormones such as progesterone and testosterone did not affect the contents of these oxidoreductases in BAECs. 4-Hydroxy-2-nonenal (HNE)-protein adducts, which are generated by lipid peroxidation, were accumulated in BAECs exposed to paraquat, whereas the pretreatment of BAECs with 17beta-estradiol suppressed their accumulation.</AbstractText><AbstractText Label="CONCLUSIONS" NlmCategory="CONCLUSIONS">The estrogen-mediated induction of the protein thiol/disulfide oxidoreductases such as PDI, Trx, Trx reductase and Grx suggested a possible involvement of these oxidoreductases in the antioxidant protection of estrogen observed in the vascular system.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Ejima</LastName><ForeName>K</ForeName><Initials>K</Initials><AffiliationInfo><Affiliation>Department of Health Development, University of Occupational and Environmental Health, Kitakyushu 807-8555, Japan.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Nanri</LastName><ForeName>H</ForeName><Initials>H</Initials></Author><Author ValidYN="Y"><LastName>Araki</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Uchida</LastName><ForeName>K</ForeName><Initials>K</Initials></Author><Author ValidYN="Y"><LastName>Kashimura</LastName><ForeName>M</ForeName><Initials>M</Initials></Author><Author ValidYN="Y"><LastName>Ikeda</LastName><ForeName>M</ForeName><Initials>M</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>Eur J Endocrinol</MedlineTA><NlmUniqueID>9423848</NlmUniqueID><ISSNLinking>0804-4643</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance 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5.3.4.1</RegistryNumber><NameOfSubstance UI="D019704">Protein Disulfide-Isomerases</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000975" MajorTopicYN="N">Antioxidants</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="Y">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D001011" MajorTopicYN="N">Aorta</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002417" MajorTopicYN="N">Cattle</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D002478" MajorTopicYN="N">Cells, Cultured</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004730" MajorTopicYN="N">Endothelium, Vascular</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="Y">drug effects</QualifierName><QualifierName UI="Q000378" 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MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013880" MajorTopicYN="N">Thioredoxin-Disulfide Reductase</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1999</Year><Month>6</Month><Day>12</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1999</Year><Month>6</Month><Day>12</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1999</Year><Month>6</Month><Day>12</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">10366417</ArticleId><ArticleId IdType="pii">1400608</ArticleId><ArticleId IdType="doi">10.1530/eje.0.1400608</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Japon</li></country></list><tree><noCountry><name sortKey="Araki, M" sort="Araki, M" uniqKey="Araki M" first="M" last="Araki">M. Araki</name><name sortKey="Ikeda, M" sort="Ikeda, M" uniqKey="Ikeda M" first="M" last="Ikeda">M. Ikeda</name><name sortKey="Kashimura, M" sort="Kashimura, M" uniqKey="Kashimura M" first="M" last="Kashimura">M. Kashimura</name><name sortKey="Nanri, H" sort="Nanri, H" uniqKey="Nanri H" first="H" last="Nanri">H. Nanri</name><name sortKey="Uchida, K" sort="Uchida, K" uniqKey="Uchida K" first="K" last="Uchida">K. Uchida</name></noCountry><country name="Japon"><noRegion><name sortKey="Ejima, K" sort="Ejima, K" uniqKey="Ejima K" first="K" last="Ejima">K. Ejima</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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