Estrogen induced peroxidase secretion from the endometrial epithelium: a possible function for the luminal enzyme.
Identifieur interne : 000C92 ( Main/Corpus ); précédent : 000C91; suivant : 000C93Estrogen induced peroxidase secretion from the endometrial epithelium: a possible function for the luminal enzyme.
Auteurs : G. Wang ; N. Bhattacharyya ; C. Wilkerson ; R A Ramsammy ; E. Eatman ; W A AndersonSource :
- Journal of submicroscopic cytology and pathology [ 1122-9497 ] ; 1994.
English descriptors
- KwdEn :
- Animals (MeSH), Endometrium (drug effects), Endometrium (enzymology), Endometrium (ultrastructure), Enzyme Induction (drug effects), Epithelium (enzymology), Estrogens (pharmacology), Female (MeSH), Isoelectric Focusing (MeSH), Male (MeSH), Microscopy, Electron (MeSH), Peroxidase (biosynthesis), Peroxidase (metabolism), Rats (MeSH), Rats, Sprague-Dawley (MeSH), Sperm-Ovum Interactions (physiology).
- MESH :
- chemical , biosynthesis : Peroxidase.
- chemical , metabolism : Peroxidase.
- chemical , pharmacology : Estrogens.
- drug effects : Endometrium, Enzyme Induction.
- enzymology : Endometrium, Epithelium.
- physiology : Sperm-Ovum Interactions.
- ultrastructure : Endometrium.
- Animals, Female, Isoelectric Focusing, Male, Microscopy, Electron, Rats, Rats, Sprague-Dawley.
Abstract
Estrogen induced peroxidase (EIP) activity revealed as a diaminobenzidine-H2O2 product in electron micrographs is apparent within cisternae of the RER and in large dilated apical vesicles, of which only a few have been seen to open into the uterine lumen. EIP activity is infrequently present in the trans cisternae of the rather diminutive Golgi complex in uterine epithelial cells from 12-72 h after treatment with estrogen. EIP activity is, however, prominent on the surface of microvilli of epithelial cells and as deposits in the lumen. Desalted uterine fluid (72 h) isolated by rotofor (Biorad) and analysed on isoelectric focusing gels that were stained with the diaminobenzidine-H2O2 reaction, reveal the existence of at least 6 peroxidase isoelectric variants with isoelectric points between pI 3.5 and pI 5.0. In similar preparations doubly-stained by diaminobenzidine-H2O2 and silver, peroxidase positive bands are enhanced, along with other isoelectric variants in the acidic pI range. In SDS-PAGE preparations, five prominent proteins ranging from 29-115 kD are present in 72 h uterine fluid. Luminal EIP coats the surface microvilli of the reproductive tract cells, and of viable spermatozoa incubated in uterine fluid. Peroxidase coated bacteria appear to be in the process of decay, and enzyme activity is present on the surface of most spermatozoa. It is not yet determined if EIP has bactericidal, spermicidal or capacitation functions.
PubMed: 8087802
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pubmed:8087802Le document en format XML
<record><TEI><teiHeader><fileDesc><titleStmt><title xml:lang="en">Estrogen induced peroxidase secretion from the endometrial epithelium: a possible function for the luminal enzyme.</title><author><name sortKey="Wang, G" sort="Wang, G" uniqKey="Wang G" first="G" last="Wang">G. Wang</name><affiliation><nlm:affiliation>Department of Biology, Howard University, Washington, D.C. 20059.</nlm:affiliation></affiliation></author><author><name sortKey="Bhattacharyya, N" sort="Bhattacharyya, N" uniqKey="Bhattacharyya N" first="N" last="Bhattacharyya">N. Bhattacharyya</name></author><author><name sortKey="Wilkerson, C" sort="Wilkerson, C" uniqKey="Wilkerson C" first="C" last="Wilkerson">C. Wilkerson</name></author><author><name sortKey="Ramsammy, R A" sort="Ramsammy, R A" uniqKey="Ramsammy R" first="R A" last="Ramsammy">R A Ramsammy</name></author><author><name sortKey="Eatman, E" sort="Eatman, E" uniqKey="Eatman E" first="E" last="Eatman">E. Eatman</name></author><author><name sortKey="Anderson, W A" sort="Anderson, W A" uniqKey="Anderson W" first="W A" last="Anderson">W A Anderson</name></author></titleStmt><publicationStmt><idno type="wicri:source">PubMed</idno><date when="1994">1994</date><idno type="RBID">pubmed:8087802</idno><idno type="pmid">8087802</idno><idno type="wicri:Area/Main/Corpus">000C92</idno><idno type="wicri:explorRef" wicri:stream="Main" wicri:step="Corpus" wicri:corpus="PubMed">000C92</idno></publicationStmt><sourceDesc><biblStruct><analytic><title xml:lang="en">Estrogen induced peroxidase secretion from the endometrial epithelium: a possible function for the luminal enzyme.</title><author><name sortKey="Wang, G" sort="Wang, G" uniqKey="Wang G" first="G" last="Wang">G. Wang</name><affiliation><nlm:affiliation>Department of Biology, Howard University, Washington, D.C. 20059.</nlm:affiliation></affiliation></author><author><name sortKey="Bhattacharyya, N" sort="Bhattacharyya, N" uniqKey="Bhattacharyya N" first="N" last="Bhattacharyya">N. Bhattacharyya</name></author><author><name sortKey="Wilkerson, C" sort="Wilkerson, C" uniqKey="Wilkerson C" first="C" last="Wilkerson">C. Wilkerson</name></author><author><name sortKey="Ramsammy, R A" sort="Ramsammy, R A" uniqKey="Ramsammy R" first="R A" last="Ramsammy">R A Ramsammy</name></author><author><name sortKey="Eatman, E" sort="Eatman, E" uniqKey="Eatman E" first="E" last="Eatman">E. Eatman</name></author><author><name sortKey="Anderson, W A" sort="Anderson, W A" uniqKey="Anderson W" first="W A" last="Anderson">W A Anderson</name></author></analytic><series><title level="j">Journal of submicroscopic cytology and pathology</title><idno type="ISSN">1122-9497</idno><imprint><date when="1994" type="published">1994</date></imprint></series></biblStruct></sourceDesc></fileDesc><profileDesc><textClass><keywords scheme="KwdEn" xml:lang="en"><term>Animals (MeSH)</term><term>Endometrium (drug effects)</term><term>Endometrium (enzymology)</term><term>Endometrium (ultrastructure)</term><term>Enzyme Induction (drug effects)</term><term>Epithelium (enzymology)</term><term>Estrogens (pharmacology)</term><term>Female (MeSH)</term><term>Isoelectric Focusing (MeSH)</term><term>Male (MeSH)</term><term>Microscopy, Electron (MeSH)</term><term>Peroxidase (biosynthesis)</term><term>Peroxidase (metabolism)</term><term>Rats (MeSH)</term><term>Rats, Sprague-Dawley (MeSH)</term><term>Sperm-Ovum Interactions (physiology)</term></keywords><keywords scheme="MESH" type="chemical" qualifier="biosynthesis" xml:lang="en"><term>Peroxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="metabolism" xml:lang="en"><term>Peroxidase</term></keywords><keywords scheme="MESH" type="chemical" qualifier="pharmacology" xml:lang="en"><term>Estrogens</term></keywords><keywords scheme="MESH" qualifier="drug effects" xml:lang="en"><term>Endometrium</term><term>Enzyme Induction</term></keywords><keywords scheme="MESH" qualifier="enzymology" xml:lang="en"><term>Endometrium</term><term>Epithelium</term></keywords><keywords scheme="MESH" qualifier="physiology" xml:lang="en"><term>Sperm-Ovum Interactions</term></keywords><keywords scheme="MESH" qualifier="ultrastructure" xml:lang="en"><term>Endometrium</term></keywords><keywords scheme="MESH" xml:lang="en"><term>Animals</term><term>Female</term><term>Isoelectric Focusing</term><term>Male</term><term>Microscopy, Electron</term><term>Rats</term><term>Rats, Sprague-Dawley</term></keywords></textClass></profileDesc></teiHeader><front><div type="abstract" xml:lang="en">Estrogen induced peroxidase (EIP) activity revealed as a diaminobenzidine-H2O2 product in electron micrographs is apparent within cisternae of the RER and in large dilated apical vesicles, of which only a few have been seen to open into the uterine lumen. EIP activity is infrequently present in the trans cisternae of the rather diminutive Golgi complex in uterine epithelial cells from 12-72 h after treatment with estrogen. EIP activity is, however, prominent on the surface of microvilli of epithelial cells and as deposits in the lumen. Desalted uterine fluid (72 h) isolated by rotofor (Biorad) and analysed on isoelectric focusing gels that were stained with the diaminobenzidine-H2O2 reaction, reveal the existence of at least 6 peroxidase isoelectric variants with isoelectric points between pI 3.5 and pI 5.0. In similar preparations doubly-stained by diaminobenzidine-H2O2 and silver, peroxidase positive bands are enhanced, along with other isoelectric variants in the acidic pI range. In SDS-PAGE preparations, five prominent proteins ranging from 29-115 kD are present in 72 h uterine fluid. Luminal EIP coats the surface microvilli of the reproductive tract cells, and of viable spermatozoa incubated in uterine fluid. Peroxidase coated bacteria appear to be in the process of decay, and enzyme activity is present on the surface of most spermatozoa. It is not yet determined if EIP has bactericidal, spermicidal or capacitation functions.</div></front></TEI><pubmed><MedlineCitation Status="MEDLINE" Owner="NLM"><PMID Version="1">8087802</PMID><DateCompleted><Year>1994</Year><Month>10</Month><Day>19</Day></DateCompleted><DateRevised><Year>2018</Year><Month>11</Month><Day>30</Day></DateRevised><Article PubModel="Print"><Journal><ISSN IssnType="Print">1122-9497</ISSN><JournalIssue CitedMedium="Print"><Volume>26</Volume><Issue>3</Issue><PubDate><Year>1994</Year><Month>Jul</Month></PubDate></JournalIssue><Title>Journal of submicroscopic cytology and pathology</Title><ISOAbbreviation>J Submicrosc Cytol Pathol</ISOAbbreviation></Journal><ArticleTitle>Estrogen induced peroxidase secretion from the endometrial epithelium: a possible function for the luminal enzyme.</ArticleTitle><Pagination><MedlinePgn>405-14</MedlinePgn></Pagination><Abstract><AbstractText>Estrogen induced peroxidase (EIP) activity revealed as a diaminobenzidine-H2O2 product in electron micrographs is apparent within cisternae of the RER and in large dilated apical vesicles, of which only a few have been seen to open into the uterine lumen. EIP activity is infrequently present in the trans cisternae of the rather diminutive Golgi complex in uterine epithelial cells from 12-72 h after treatment with estrogen. EIP activity is, however, prominent on the surface of microvilli of epithelial cells and as deposits in the lumen. Desalted uterine fluid (72 h) isolated by rotofor (Biorad) and analysed on isoelectric focusing gels that were stained with the diaminobenzidine-H2O2 reaction, reveal the existence of at least 6 peroxidase isoelectric variants with isoelectric points between pI 3.5 and pI 5.0. In similar preparations doubly-stained by diaminobenzidine-H2O2 and silver, peroxidase positive bands are enhanced, along with other isoelectric variants in the acidic pI range. In SDS-PAGE preparations, five prominent proteins ranging from 29-115 kD are present in 72 h uterine fluid. Luminal EIP coats the surface microvilli of the reproductive tract cells, and of viable spermatozoa incubated in uterine fluid. Peroxidase coated bacteria appear to be in the process of decay, and enzyme activity is present on the surface of most spermatozoa. It is not yet determined if EIP has bactericidal, spermicidal or capacitation functions.</AbstractText></Abstract><AuthorList CompleteYN="Y"><Author ValidYN="Y"><LastName>Wang</LastName><ForeName>G</ForeName><Initials>G</Initials><AffiliationInfo><Affiliation>Department of Biology, Howard University, Washington, D.C. 20059.</Affiliation></AffiliationInfo></Author><Author ValidYN="Y"><LastName>Bhattacharyya</LastName><ForeName>N</ForeName><Initials>N</Initials></Author><Author ValidYN="Y"><LastName>Wilkerson</LastName><ForeName>C</ForeName><Initials>C</Initials></Author><Author ValidYN="Y"><LastName>Ramsammy</LastName><ForeName>R A</ForeName><Initials>RA</Initials></Author><Author ValidYN="Y"><LastName>Eatman</LastName><ForeName>E</ForeName><Initials>E</Initials></Author><Author ValidYN="Y"><LastName>Anderson</LastName><ForeName>W A</ForeName><Initials>WA</Initials></Author></AuthorList><Language>eng</Language><PublicationTypeList><PublicationType UI="D016428">Journal Article</PublicationType><PublicationType UI="D013487">Research Support, U.S. Gov't, P.H.S.</PublicationType></PublicationTypeList></Article><MedlineJournalInfo><Country>Italy</Country><MedlineTA>J Submicrosc Cytol Pathol</MedlineTA><NlmUniqueID>8804312</NlmUniqueID><ISSNLinking>1122-9497</ISSNLinking></MedlineJournalInfo><ChemicalList><Chemical><RegistryNumber>0</RegistryNumber><NameOfSubstance UI="D004967">Estrogens</NameOfSubstance></Chemical><Chemical><RegistryNumber>EC 1.11.1.7</RegistryNumber><NameOfSubstance UI="D009195">Peroxidase</NameOfSubstance></Chemical></ChemicalList><CitationSubset>IM</CitationSubset><MeshHeadingList><MeshHeading><DescriptorName UI="D000818" MajorTopicYN="N">Animals</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D004717" MajorTopicYN="N">Endometrium</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName><QualifierName UI="Q000201" MajorTopicYN="Y">enzymology</QualifierName><QualifierName UI="Q000648" MajorTopicYN="N">ultrastructure</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004790" MajorTopicYN="N">Enzyme Induction</DescriptorName><QualifierName UI="Q000187" MajorTopicYN="N">drug effects</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004848" MajorTopicYN="N">Epithelium</DescriptorName><QualifierName UI="Q000201" MajorTopicYN="N">enzymology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D004967" MajorTopicYN="N">Estrogens</DescriptorName><QualifierName UI="Q000494" MajorTopicYN="N">pharmacology</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D005260" MajorTopicYN="N">Female</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D007525" MajorTopicYN="N">Isoelectric Focusing</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008297" MajorTopicYN="N">Male</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D008854" MajorTopicYN="N">Microscopy, Electron</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D009195" MajorTopicYN="N">Peroxidase</DescriptorName><QualifierName UI="Q000096" MajorTopicYN="Y">biosynthesis</QualifierName><QualifierName UI="Q000378" MajorTopicYN="N">metabolism</QualifierName></MeshHeading><MeshHeading><DescriptorName UI="D051381" MajorTopicYN="N">Rats</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D017207" MajorTopicYN="N">Rats, Sprague-Dawley</DescriptorName></MeshHeading><MeshHeading><DescriptorName UI="D013084" MajorTopicYN="N">Sperm-Ovum Interactions</DescriptorName><QualifierName UI="Q000502" MajorTopicYN="N">physiology</QualifierName></MeshHeading></MeshHeadingList></MedlineCitation><PubmedData><History><PubMedPubDate PubStatus="pubmed"><Year>1994</Year><Month>7</Month><Day>1</Day></PubMedPubDate><PubMedPubDate PubStatus="medline"><Year>1994</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>1</Minute></PubMedPubDate><PubMedPubDate PubStatus="entrez"><Year>1994</Year><Month>7</Month><Day>1</Day><Hour>0</Hour><Minute>0</Minute></PubMedPubDate></History><PublicationStatus>ppublish</PublicationStatus><ArticleIdList><ArticleId IdType="pubmed">8087802</ArticleId></ArticleIdList></PubmedData></pubmed></record>Pour manipuler ce document sous Unix (Dilib)
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