Immunohistochemical determination of thioredoxin and glutaredoxin distribution in the human cervix, and possible relation to cervical ripening.
Identifieur interne : 000F28 ( Main/Exploration ); précédent : 000F27; suivant : 000F29Immunohistochemical determination of thioredoxin and glutaredoxin distribution in the human cervix, and possible relation to cervical ripening.
Auteurs : J. Lysell [Suède] ; Y. Stjernholm Vladic ; N. Ciarlo ; A. Holmgren ; L. SahlinSource :
- Gynecological endocrinology : the official journal of the International Society of Gynecological Endocrinology [ 0951-3590 ] ; 2003.
Descripteurs français
- KwdFr :
- Adulte (MeSH), Biopsie (MeSH), Col de l'utérus (enzymologie), Col de l'utérus (physiologie), Femelle (MeSH), Glutarédoxines (MeSH), Grossesse (MeSH), Humains (MeSH), Immunohistochimie (MeSH), Maturation du col utérin (physiologie), Oxidoreductases (MeSH), Protéines (métabolisme), Statistique non paramétrique (MeSH), Thiorédoxines (métabolisme), Traitement d'image par ordinateur (MeSH).
- MESH :
- enzymologie : Col de l'utérus.
- métabolisme : Protéines, Thiorédoxines.
- physiologie : Col de l'utérus, Maturation du col utérin.
- Adulte, Biopsie, Femelle, Glutarédoxines, Grossesse, Humains, Immunohistochimie, Oxidoreductases, Statistique non paramétrique, Traitement d'image par ordinateur.
English descriptors
- KwdEn :
- Adult (MeSH), Biopsy (MeSH), Cervical Ripening (physiology), Cervix Uteri (enzymology), Cervix Uteri (physiology), Female (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Image Processing, Computer-Assisted (MeSH), Immunohistochemistry (MeSH), Oxidoreductases (MeSH), Pregnancy (MeSH), Proteins (metabolism), Statistics, Nonparametric (MeSH), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : Proteins, Thioredoxins.
- chemical : Glutaredoxins, Oxidoreductases.
- enzymology : Cervix Uteri.
- physiology : Cervical Ripening, Cervix Uteri.
- Adult, Biopsy, Female, Humans, Image Processing, Computer-Assisted, Immunohistochemistry, Pregnancy, Statistics, Nonparametric.
Abstract
Thioredoxin (Trx) and glutaredoxin (Grx) are dithiol redox enzymes, catalyzing general thiol-disulfide oxidoreductions apart from being hydrogen donors for ribonucleotide reductase, an enzyme essential for DNA synthesis. In mammals, isoenzymes of Trx and Grx are found in the cytoplasm (Trx1 and Grx1) or in mitochondria (Trx2 and Grx2). Trx and Grx play a role in cellular defence against oxidative stress and in redox regulation of cellular function. The localization and levels of human Trx1 and human Grx1 have been determined in the human cervix by immunohistochemistry and image analysis. Cervical biopsies were obtained from five non-pregnant, five term pregnant and five postpartum women. The levels of both Trx1 and Grx1 were increased in the nuclei (after translocation from the cytoplasm) of stromal cells in cervices from the term pregnant group as compared to the non-pregnant group, but the levels in the postpartum group did not differ significantly from those of the other two groups. These results are in agreement with our previous data on the mRNA expression of these two redox enzymes. The increased levels of the redox enzymes in term pregnancy suggest that they can be regulating factors involved in the process of cervical ripening, e.g. transcription factors and enzymes. Secreted Trx may participate in removing inhibitors of collagen-degrading metalloproteinases.
DOI: 10.1080/gye.17.4.303.310
PubMed: 14503974
Affiliations:
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Lysell</name><affiliation wicri:level="1"><nlm:affiliation>Division for Reproductive Endocrinology, Department of Biochemistry and Biophysics, Karolinska Institutet, Karolinska Hospital, L5:01, S-171 76 Stockholm, Sweden.</nlm:affiliation><country xml:lang="fr">Suède</country><wicri:regionArea>Division for Reproductive Endocrinology, Department of Biochemistry and Biophysics, Karolinska Institutet, Karolinska Hospital, L5:01, S-171 76 Stockholm</wicri:regionArea><wicri:noRegion>S-171 76 Stockholm</wicri:noRegion></affiliation></author><author><name sortKey="Stjernholm Vladic, Y" sort="Stjernholm Vladic, Y" uniqKey="Stjernholm Vladic Y" first="Y" last="Stjernholm Vladic">Y. Stjernholm Vladic</name></author><author><name sortKey="Ciarlo, N" sort="Ciarlo, N" uniqKey="Ciarlo N" first="N" last="Ciarlo">N. Ciarlo</name></author><author><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name></author><author><name sortKey="Sahlin, L" sort="Sahlin, L" uniqKey="Sahlin L" first="L" last="Sahlin">L. Sahlin</name></author></analytic><series><title level="j">Gynecological endocrinology : the official journal of the International Society of Gynecological Endocrinology</title><idno type="ISSN">0951-3590</idno><imprint><date when="2003" type="published">2003</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adult (MeSH)</term><term>Biopsy (MeSH)</term><term>Cervical Ripening (physiology)</term><term>Cervix Uteri (enzymology)</term><term>Cervix Uteri (physiology)</term><term>Female (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Image Processing, Computer-Assisted (MeSH)</term><term>Immunohistochemistry (MeSH)</term><term>Oxidoreductases (MeSH)</term><term>Pregnancy (MeSH)</term><term>Proteins (metabolism)</term><term>Statistics, Nonparametric (MeSH)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adulte (MeSH)</term><term>Biopsie (MeSH)</term><term>Col de l'utérus (enzymologie)</term><term>Col de l'utérus (physiologie)</term><term>Femelle (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Grossesse (MeSH)</term><term>Humains (MeSH)</term><term>Immunohistochimie (MeSH)</term><term>Maturation du col utérin (physiologie)</term><term>Oxidoreductases (MeSH)</term><term>Protéines (métabolisme)</term><term>Statistique non paramétrique (MeSH)</term><term>Thiorédoxines (métabolisme)</term><term>Traitement d'image par ordinateur (MeSH)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Proteins</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Oxidoreductases</term></keywords><keywords scheme="MESH" qualifier="enzymologie" xml:lang="fr"><term>Col de l'utérus</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Cervix Uteri</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Protéines</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Col de l'utérus</term><term>Maturation du col utérin</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Cervical Ripening</term><term>Cervix Uteri</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Biopsy</term><term>Female</term><term>Humans</term><term>Image Processing, Computer-Assisted</term><term>Immunohistochemistry</term><term>Pregnancy</term><term>Statistics, Nonparametric</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adulte</term><term>Biopsie</term><term>Femelle</term><term>Glutarédoxines</term><term>Grossesse</term><term>Humains</term><term>Immunohistochimie</term><term>Oxidoreductases</term><term>Statistique non paramétrique</term><term>Traitement d'image par ordinateur</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Thioredoxin (Trx) and glutaredoxin (Grx) are dithiol redox enzymes, catalyzing general thiol-disulfide oxidoreductions apart from being hydrogen donors for ribonucleotide reductase, an enzyme essential for DNA synthesis. In mammals, isoenzymes of Trx and Grx are found in the cytoplasm (Trx1 and Grx1) or in mitochondria (Trx2 and Grx2). Trx and Grx play a role in cellular defence against oxidative stress and in redox regulation of cellular function. The localization and levels of human Trx1 and human Grx1 have been determined in the human cervix by immunohistochemistry and image analysis. Cervical biopsies were obtained from five non-pregnant, five term pregnant and five postpartum women. The levels of both Trx1 and Grx1 were increased in the nuclei (after translocation from the cytoplasm) of stromal cells in cervices from the term pregnant group as compared to the non-pregnant group, but the levels in the postpartum group did not differ significantly from those of the other two groups. These results are in agreement with our previous data on the mRNA expression of these two redox enzymes. The increased levels of the redox enzymes in term pregnancy suggest that they can be regulating factors involved in the process of cervical ripening, e.g. transcription factors and enzymes. Secreted Trx may participate in removing inhibitors of collagen-degrading metalloproteinases.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">14503974</PMID><DateCompleted><Year>2004</Year><Month>05</Month><Day>06</Day></DateCompleted><DateRevised><Year>2019</Year><Month>11</Month><Day>08</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">0951-3590</ISSN><JournalIssue CitedMedium="Print"><Volume>17</Volume><Issue>4</Issue><PubDate><Year>2003</Year><Month>Aug</Month></PubDate></JournalIssue><Title>Gynecological endocrinology : the official journal of the International Society of Gynecological Endocrinology</Title><ISOAbbreviation>Gynecol Endocrinol</ISOAbbreviation></Journal><ArticleTitle>Immunohistochemical determination of thioredoxin and glutaredoxin distribution in the human cervix, and possible relation to cervical ripening.</ArticleTitle><Pagination><MedlinePgn>303-10</MedlinePgn></Pagination><Abstract><AbstractText>Thioredoxin (Trx) and glutaredoxin (Grx) are dithiol redox enzymes, catalyzing general thiol-disulfide oxidoreductions apart from being hydrogen donors for ribonucleotide reductase, an enzyme essential for DNA synthesis. In mammals, isoenzymes of Trx and Grx are found in the cytoplasm (Trx1 and Grx1) or in mitochondria (Trx2 and Grx2). Trx and Grx play a role in cellular defence against oxidative stress and in redox regulation of cellular function. The localization and levels of human Trx1 and human Grx1 have been determined in the human cervix by immunohistochemistry and image analysis. Cervical biopsies were obtained from five non-pregnant, five term pregnant and five postpartum women. The levels of both Trx1 and Grx1 were increased in the nuclei (after translocation from the cytoplasm) of stromal cells in cervices from the term pregnant group as compared to the non-pregnant group, but the levels in the postpartum group did not differ significantly from those of the other two groups. These results are in agreement with our previous data on the mRNA expression of these two redox enzymes. The increased levels of the redox enzymes in term pregnancy suggest that they can be regulating factors involved in the process of cervical ripening, e.g. transcription factors and enzymes. Secreted Trx may participate in removing inhibitors of collagen-degrading metalloproteinases.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Lysell</LastName><ForeName>J</ForeName><Initials>J</Initials><AffiliationInfo><Affiliation>Division for Reproductive Endocrinology, Department of Biochemistry and Biophysics, Karolinska Institutet, Karolinska Hospital, L5:01, S-171 76 Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Stjernholm Vladic</LastName><ForeName>Y</ForeName><Initials>Y</Initials></Author><Author ValidYN="Y"><LastName>Ciarlo</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Sahlin</LastName><ForeName>L</ForeName><Initials>L</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>Gynecol Endocrinol</MedlineTA><NlmUniqueID>8807913</NlmUniqueID><ISSNLinking>0951-3590</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516005">GLRX protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="C516008">GLRX2 protein, human</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D054477">Glutaredoxins</NameOfSubstance></Chemical><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D011506">Proteins</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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000328" MajorTopicYN="N">Adult</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D001706" MajorTopicYN="N">Biopsy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D020070" MajorTopicYN="N">Cervical Ripening</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D002584" MajorTopicYN="N">Cervix Uteri</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000502" MajorTopicYN="Y">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D054477" MajorTopicYN="N">Glutaredoxins</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D006801" MajorTopicYN="N">Humans</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007091" MajorTopicYN="N">Image Processing, Computer-Assisted</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007150" MajorTopicYN="N">Immunohistochemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="Y">Oxidoreductases</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011247" MajorTopicYN="N">Pregnancy</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D011506" MajorTopicYN="N">Proteins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D018709" MajorTopicYN="N">Statistics, Nonparametric</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013879" MajorTopicYN="N">Thioredoxins</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>2003</Year><Month>9</Month><Day>25</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2004</Year><Month>5</Month><Day>7</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2003</Year><Month>9</Month><Day>25</Day><Hour>5</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">14503974</ArticleId><ArticleId IdType="doi">10.1080/gye.17.4.303.310</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country></list><tree><noCountry><name sortKey="Ciarlo, N" sort="Ciarlo, N" uniqKey="Ciarlo N" first="N" last="Ciarlo">N. Ciarlo</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Sahlin, L" sort="Sahlin, L" uniqKey="Sahlin L" first="L" last="Sahlin">L. Sahlin</name><name sortKey="Stjernholm Vladic, Y" sort="Stjernholm Vladic, Y" uniqKey="Stjernholm Vladic Y" first="Y" last="Stjernholm Vladic">Y. Stjernholm Vladic</name></noCountry><country name="Suède"><noRegion><name sortKey="Lysell, J" sort="Lysell, J" uniqKey="Lysell J" first="J" last="Lysell">J. Lysell</name></noRegion></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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