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A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions
We have raised an mAb to a previously undescribed 135-kD externally disposed integral membrane protein that is enriched in the intercellular junctional domain of cultured human umbilical vein endothelial cells. This protein localizes at the appositional surfaces of cells as they become confluent and...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1989
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189408/ https://www.ncbi.nlm.nih.gov/pubmed/2666561 |
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collection | PubMed |
description | We have raised an mAb to a previously undescribed 135-kD externally disposed integral membrane protein that is enriched in the intercellular junctional domain of cultured human umbilical vein endothelial cells. This protein localizes at the appositional surfaces of cells as they become confluent and is stably expressed in the junctional zones of confluent monolayers. This protein is expressed in situ on continuous endothelia of all blood vessels in all human tissues examined. Moreover, this protein, as determined by mAb immunocytochemistry, is not expressed by any other cell type. This protein may mediate endothelial-specific functions restricted to the intercellular domain. It may also serve as a unique cell surface marker for the identification and purification of human endothelial cells. |
format | Text |
id | pubmed-2189408 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1989 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21894082008-04-17 A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions J Exp Med Articles We have raised an mAb to a previously undescribed 135-kD externally disposed integral membrane protein that is enriched in the intercellular junctional domain of cultured human umbilical vein endothelial cells. This protein localizes at the appositional surfaces of cells as they become confluent and is stably expressed in the junctional zones of confluent monolayers. This protein is expressed in situ on continuous endothelia of all blood vessels in all human tissues examined. Moreover, this protein, as determined by mAb immunocytochemistry, is not expressed by any other cell type. This protein may mediate endothelial-specific functions restricted to the intercellular domain. It may also serve as a unique cell surface marker for the identification and purification of human endothelial cells. The Rockefeller University Press 1989-08-01 /pmc/articles/PMC2189408/ /pubmed/2666561 Text en This article is distributed under the terms of an Attribution–Noncommercial–Share Alike–No Mirror Sites license for the first six months after the publication date (see http://www.rupress.org/terms). After six months it is available under a Creative Commons License (Attribution–Noncommercial–Share Alike 4.0 Unported license, as described at http://creativecommons.org/licenses/by-nc-sa/4.0/). |
spellingShingle | Articles A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions |
title | A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions |
title_full | A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions |
title_fullStr | A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions |
title_full_unstemmed | A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions |
title_short | A human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions |
title_sort | human endothelial cell-restricted, externally disposed plasmalemmal protein enriched in intercellular junctions |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2189408/ https://www.ncbi.nlm.nih.gov/pubmed/2666561 |