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Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube

The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo im...

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Autores principales: Hey, Neil A, Meseguer, Marcos, Simón, Carlos, Smorodinsky, Nechama I, Wreschner, Daniel H, Ortíz, María Elena, Aplin, John D
Formato: Texto
Lenguaje:English
Publicado: BioMed Central 2003
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC151559/
https://www.ncbi.nlm.nih.gov/pubmed/12646057
http://dx.doi.org/10.1186/1477-7827-1-2
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author Hey, Neil A
Meseguer, Marcos
Simón, Carlos
Smorodinsky, Nechama I
Wreschner, Daniel H
Ortíz, María Elena
Aplin, John D
author_facet Hey, Neil A
Meseguer, Marcos
Simón, Carlos
Smorodinsky, Nechama I
Wreschner, Daniel H
Ortíz, María Elena
Aplin, John D
author_sort Hey, Neil A
collection PubMed
description The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo implantation, arising from the anti-adhesive property of MUC1. In previous work, we demonstrated alternatively spliced MUC1 variant forms in tumour cells. The variant MUC1/SEC lacks the transmembrane and cytoplasmic sequences found in the full-length variant. We now show that MUC1/SEC mRNA is present in endometrial carcinoma cell lines, endometrial tissue and primary cultured endometrial epithelial cells. The protein can be detected using isoform-specific antibodies in uterine flushings, suggesting release from endometrium in vivo. However, on the basis of immunolocalisation studies, MUC1/SEC also remains associated with the apical epithelial surface both in tissue and in cultured cells. Transmembrane MUC1 and MUC1/SEC are both strikingly localised to the apical surface of tubal epithelium. Thus MUC1 may contribute to the anti-adhesive character of the tubal surface, inhibiting ectopic implantation. The mechanism by which this barrier is overcome in endometrium at implantation is the subject of ongoing investigation.
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spelling pubmed-1515592003-03-18 Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube Hey, Neil A Meseguer, Marcos Simón, Carlos Smorodinsky, Nechama I Wreschner, Daniel H Ortíz, María Elena Aplin, John D Reprod Biol Endocrinol Research The cell surface mucin MUC1 is expressed by endometrial epithelial cells with increased abundance in the secretory phase of the menstrual cycle, when it is found both at the apical cell surface and in secretions. This suggests the presence of a maternal cell surface glycoprotein barrier to embryo implantation, arising from the anti-adhesive property of MUC1. In previous work, we demonstrated alternatively spliced MUC1 variant forms in tumour cells. The variant MUC1/SEC lacks the transmembrane and cytoplasmic sequences found in the full-length variant. We now show that MUC1/SEC mRNA is present in endometrial carcinoma cell lines, endometrial tissue and primary cultured endometrial epithelial cells. The protein can be detected using isoform-specific antibodies in uterine flushings, suggesting release from endometrium in vivo. However, on the basis of immunolocalisation studies, MUC1/SEC also remains associated with the apical epithelial surface both in tissue and in cultured cells. Transmembrane MUC1 and MUC1/SEC are both strikingly localised to the apical surface of tubal epithelium. Thus MUC1 may contribute to the anti-adhesive character of the tubal surface, inhibiting ectopic implantation. The mechanism by which this barrier is overcome in endometrium at implantation is the subject of ongoing investigation. BioMed Central 2003-01-30 /pmc/articles/PMC151559/ /pubmed/12646057 http://dx.doi.org/10.1186/1477-7827-1-2 Text en Copyright © 2003 Hey et al; licensee BioMed Central Ltd. This is an Open Access article: verbatim copying and redistribution of this article are permitted in all media for any purpose, provided this notice is preserved along with the article's original URL.
spellingShingle Research
Hey, Neil A
Meseguer, Marcos
Simón, Carlos
Smorodinsky, Nechama I
Wreschner, Daniel H
Ortíz, María Elena
Aplin, John D
Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube
title Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube
title_full Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube
title_fullStr Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube
title_full_unstemmed Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube
title_short Transmembrane and truncated (SEC) isoforms of MUC1 in the human endometrium and Fallopian tube
title_sort transmembrane and truncated (sec) isoforms of muc1 in the human endometrium and fallopian tube
topic Research
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC151559/
https://www.ncbi.nlm.nih.gov/pubmed/12646057
http://dx.doi.org/10.1186/1477-7827-1-2
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