Immunohistochemical localization of glutaredoxin and thioredoxin in human endometrium: a possible association with pinopodes.
Identifieur interne : 000F80 ( Main/Exploration ); précédent : 000F79; suivant : 000F81Immunohistochemical localization of glutaredoxin and thioredoxin in human endometrium: a possible association with pinopodes.
Auteurs : A. Stavréus-Evers [Suède] ; B. Masironi ; B-M Landgren ; A. Holmgren ; H. Eriksson ; L. SahlinSource :
- Molecular human reproduction [ 1360-9947 ] ; 2002.
Descripteurs français
- KwdFr :
- Adulte (MeSH), Animaux (MeSH), Cycle menstruel (physiologie), Endomètre (composition chimique), Endomètre (métabolisme), Endomètre (ultrastructure), Femelle (MeSH), Glutarédoxines (MeSH), Humains (MeSH), Immunohistochimie (MeSH), Oxidoreductases (métabolisme), Protein-disulfide reductase (glutathione) (MeSH), Thiorédoxines (métabolisme).
- MESH :
- composition chimique : Endomètre.
- métabolisme : Endomètre, Oxidoreductases, Thiorédoxines.
- physiologie : Cycle menstruel.
- Adulte, Animaux, Endomètre, Femelle, Glutarédoxines, Humains, Immunohistochimie, Protein-disulfide reductase (glutathione).
English descriptors
- KwdEn :
- Adult (MeSH), Animals (MeSH), Endometrium (chemistry), Endometrium (metabolism), Endometrium (ultrastructure), Female (MeSH), Glutaredoxins (MeSH), Humans (MeSH), Immunohistochemistry (MeSH), Menstrual Cycle (physiology), Oxidoreductases (metabolism), Protein Disulfide Reductase (Glutathione) (MeSH), Thioredoxins (metabolism).
- MESH :
- chemical , metabolism : Oxidoreductases, Thioredoxins.
- chemical : Glutaredoxins, Protein Disulfide Reductase (Glutathione).
- chemistry : Endometrium.
- metabolism : Endometrium.
- physiology : Menstrual Cycle.
- ultrastructure : Endometrium.
- Adult, Animals, Female, Humans, Immunohistochemistry.
Abstract
The human endometrium is only receptive for blastocyst implantation during a short period of the menstrual cycle. Pinopodes have been suggested to be markers of uterine receptivity, but little is known about their function and the biochemical processes taking place in them. In this study, we have examined the presence of glutaredoxin (Grx) and thioredoxin (Trx) and their co-localization with pinopodes in the normal human endometrium. Endometrial biopsies were obtained from fertile women with normal menstrual cycles. The biopsies were examined by scanning electron microscopy for detection of pinopodes and by immunohistochemistry for the expression of Grx and Trx. The pinopodes showed strong immunostaining for Grx. Increasing levels of Grx immunoreactivity were seen in the luminal and glandular epithelial cells concomitant with pinopode formation. Trx immunostaining was most intense in the ciliated cells of the luminal and glandular epithelium, while the staining was moderate to strong in a majority of the other cells, both epithelial and stromal. Trx levels did not change during the secretory phase of the cycle. The intense immunostaining concomitant with the presence of pinopodes suggests that Grx plays an important role during implantation, possibly by protecting the epithelial cells from apoptotic actions of the trophoblast cells.
DOI: 10.1093/molehr/8.6.546
PubMed: 12029072
Affiliations:
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Holmgren</name></author><author><name sortKey="Eriksson, H" sort="Eriksson, H" uniqKey="Eriksson H" first="H" last="Eriksson">H. Eriksson</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">Molecular human reproduction</title><idno type="ISSN">1360-9947</idno><imprint><date when="2002" type="published">2002</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Adult (MeSH)</term><term>Animals (MeSH)</term><term>Endometrium (chemistry)</term><term>Endometrium (metabolism)</term><term>Endometrium (ultrastructure)</term><term>Female (MeSH)</term><term>Glutaredoxins (MeSH)</term><term>Humans (MeSH)</term><term>Immunohistochemistry (MeSH)</term><term>Menstrual Cycle (physiology)</term><term>Oxidoreductases (metabolism)</term><term>Protein Disulfide Reductase (Glutathione) (MeSH)</term><term>Thioredoxins (metabolism)</term></keywords><keywords scheme="KwdFr" xml:lang="fr"><term>Adulte (MeSH)</term><term>Animaux (MeSH)</term><term>Cycle menstruel (physiologie)</term><term>Endomètre (composition chimique)</term><term>Endomètre (métabolisme)</term><term>Endomètre (ultrastructure)</term><term>Femelle (MeSH)</term><term>Glutarédoxines (MeSH)</term><term>Humains (MeSH)</term><term>Immunohistochimie (MeSH)</term><term>Oxidoreductases (métabolisme)</term><term>Protein-disulfide reductase (glutathione) (MeSH)</term><term>Thiorédoxines (métabolisme)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Oxidoreductases</term><term>Thioredoxins</term></keywords><keywords scheme="MESH" type="chemical" xml:lang="en"><term>Glutaredoxins</term><term>Protein Disulfide Reductase (Glutathione)</term></keywords><keywords scheme="MESH" qualifier="chemistry" xml:lang="en"><term>Endometrium</term></keywords><keywords scheme="MESH" qualifier="composition chimique" xml:lang="fr"><term>Endomètre</term></keywords><keywords scheme="MESH" qualifier="metabolism" xml:lang="en"><term>Endometrium</term></keywords><keywords scheme="MESH" qualifier="métabolisme" xml:lang="fr"><term>Endomètre</term><term>Oxidoreductases</term><term>Thiorédoxines</term></keywords><keywords scheme="MESH" qualifier="physiologie" xml:lang="fr"><term>Cycle menstruel</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Menstrual Cycle</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Endometrium</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Adult</term><term>Animals</term><term>Female</term><term>Humans</term><term>Immunohistochemistry</term></keywords><keywords scheme="MESH" xml:lang="fr"><term>Adulte</term><term>Animaux</term><term>Endomètre</term><term>Femelle</term><term>Glutarédoxines</term><term>Humains</term><term>Immunohistochimie</term><term>Protein-disulfide reductase (glutathione)</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">The human endometrium is only receptive for blastocyst implantation during a short period of the menstrual cycle. Pinopodes have been suggested to be markers of uterine receptivity, but little is known about their function and the biochemical processes taking place in them. In this study, we have examined the presence of glutaredoxin (Grx) and thioredoxin (Trx) and their co-localization with pinopodes in the normal human endometrium. Endometrial biopsies were obtained from fertile women with normal menstrual cycles. The biopsies were examined by scanning electron microscopy for detection of pinopodes and by immunohistochemistry for the expression of Grx and Trx. The pinopodes showed strong immunostaining for Grx. Increasing levels of Grx immunoreactivity were seen in the luminal and glandular epithelial cells concomitant with pinopode formation. Trx immunostaining was most intense in the ciliated cells of the luminal and glandular epithelium, while the staining was moderate to strong in a majority of the other cells, both epithelial and stromal. Trx levels did not change during the secretory phase of the cycle. The intense immunostaining concomitant with the presence of pinopodes suggests that Grx plays an important role during implantation, possibly by protecting the epithelial cells from apoptotic actions of the trophoblast cells.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">12029072</PMID><DateCompleted><Year>2003</Year><Month>01</Month><Day>13</Day></DateCompleted><DateRevised><Year>2019</Year><Month>05</Month><Day>13</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1360-9947</ISSN><JournalIssue CitedMedium="Print"><Volume>8</Volume><Issue>6</Issue><PubDate><Year>2002</Year><Month>Jun</Month></PubDate></JournalIssue><Title>Molecular human reproduction</Title><ISOAbbreviation>Mol Hum Reprod</ISOAbbreviation></Journal><ArticleTitle>Immunohistochemical localization of glutaredoxin and thioredoxin in human endometrium: a possible association with pinopodes.</ArticleTitle><Pagination><MedlinePgn>546-51</MedlinePgn></Pagination><Abstract><AbstractText>The human endometrium is only receptive for blastocyst implantation during a short period of the menstrual cycle. Pinopodes have been suggested to be markers of uterine receptivity, but little is known about their function and the biochemical processes taking place in them. In this study, we have examined the presence of glutaredoxin (Grx) and thioredoxin (Trx) and their co-localization with pinopodes in the normal human endometrium. Endometrial biopsies were obtained from fertile women with normal menstrual cycles. The biopsies were examined by scanning electron microscopy for detection of pinopodes and by immunohistochemistry for the expression of Grx and Trx. The pinopodes showed strong immunostaining for Grx. Increasing levels of Grx immunoreactivity were seen in the luminal and glandular epithelial cells concomitant with pinopode formation. Trx immunostaining was most intense in the ciliated cells of the luminal and glandular epithelium, while the staining was moderate to strong in a majority of the other cells, both epithelial and stromal. Trx levels did not change during the secretory phase of the cycle. The intense immunostaining concomitant with the presence of pinopodes suggests that Grx plays an important role during implantation, possibly by protecting the epithelial cells from apoptotic actions of the trophoblast cells.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Stavréus-Evers</LastName><ForeName>A</ForeName><Initials>A</Initials><AffiliationInfo><Affiliation>Division for Reproductive Endocrinology, Department of Woman and Child Health, Karolinska Hospital, Stockholm, Sweden.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Masironi</LastName><ForeName>B</ForeName><Initials>B</Initials></Author><Author ValidYN="Y"><LastName>Landgren</LastName><ForeName>B-M</ForeName><Initials>BM</Initials></Author><Author ValidYN="Y"><LastName>Holmgren</LastName><ForeName>A</ForeName><Initials>A</Initials></Author><Author ValidYN="Y"><LastName>Eriksson</LastName><ForeName>H</ForeName><Initials>H</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>Mol Hum Reprod</MedlineTA><NlmUniqueID>9513710</NlmUniqueID><ISSNLinking>1360-9947</ISSNLinking></MedlineJournalInfo><ChemicalList><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></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000328" MajorTopicYN="N">Adult</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004717" MajorTopicYN="N">Endometrium</DescriptorName><QualifierName UI="Q000737" MajorTopicYN="N">chemistry</QualifierName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName><QualifierName UI="Q000648" MajorTopicYN="Y">ultrastructure</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="D007150" MajorTopicYN="N">Immunohistochemistry</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008597" MajorTopicYN="N">Menstrual Cycle</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D010088" MajorTopicYN="N">Oxidoreductases</DescriptorName><QualifierName UI="Q000378" MajorTopicYN="Y">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D011490" MajorTopicYN="Y">Protein Disulfide Reductase (Glutathione)</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>2002</Year><Month>5</Month><Day>25</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>2003</Year><Month>1</Month><Day>14</Day><Hour>4</Hour><Minute>0</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>2002</Year><Month>5</Month><Day>25</Day><Hour>10</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">12029072</ArticleId><ArticleId IdType="doi">10.1093/molehr/8.6.546</ArticleId></ArticleIdList></PubmedData></pubmed><affiliations><list><country><li>Suède</li></country><region><li>Svealand</li></region><settlement><li>Stockholm</li></settlement></list><tree><noCountry><name sortKey="Eriksson, H" sort="Eriksson, H" uniqKey="Eriksson H" first="H" last="Eriksson">H. Eriksson</name><name sortKey="Holmgren, A" sort="Holmgren, A" uniqKey="Holmgren A" first="A" last="Holmgren">A. Holmgren</name><name sortKey="Landgren, B M" sort="Landgren, B M" uniqKey="Landgren B" first="B-M" last="Landgren">B-M Landgren</name><name sortKey="Masironi, B" sort="Masironi, B" uniqKey="Masironi B" first="B" last="Masironi">B. Masironi</name><name sortKey="Sahlin, L" sort="Sahlin, L" uniqKey="Sahlin L" first="L" last="Sahlin">L. Sahlin</name></noCountry><country name="Suède"><region name="Svealand"><name sortKey="Stavreus Evers, A" sort="Stavreus Evers, A" uniqKey="Stavreus Evers A" first="A" last="Stavréus-Evers">A. Stavréus-Evers</name></region></country></tree></affiliations></record>Pour manipuler ce document sous Unix (Dilib)
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