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Research progress on the structure and function of endomucin
Endomucin is a type I integral membrane glycoprotein, which is expressed in venous and capillary endothelial cells. It consists of 261 amino acids with an extracellular domain that is highly O‐glycosylated at serine and threonine residues and has several potential N‐glycosylation sites. Endomucin pl...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
John Wiley and Sons Inc.
2021
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7824966/ https://www.ncbi.nlm.nih.gov/pubmed/33532708 http://dx.doi.org/10.1002/ame2.12142 |
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author | Zhang, Guoxin Yang, Xingjiu Gao, Ran |
author_facet | Zhang, Guoxin Yang, Xingjiu Gao, Ran |
author_sort | Zhang, Guoxin |
collection | PubMed |
description | Endomucin is a type I integral membrane glycoprotein, which is expressed in venous and capillary endothelial cells. It consists of 261 amino acids with an extracellular domain that is highly O‐glycosylated at serine and threonine residues and has several potential N‐glycosylation sites. Endomucin plays an important role in biological processes such as cell interaction, molecular cell signaling, angiogenesis and cell migration, and in recent years it has also been identified as an anti‐adhesion molecule and a marker of endothelial cells. While it has been shown to be involved in a number of physiological and pathological mechanisms, many of its functions remain unknown, and further study is needed. This article reviews research progress on the function of endomucin to date, in order to provide guidance for future studies. |
format | Online Article Text |
id | pubmed-7824966 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2021 |
publisher | John Wiley and Sons Inc. |
record_format | MEDLINE/PubMed |
spelling | pubmed-78249662021-02-01 Research progress on the structure and function of endomucin Zhang, Guoxin Yang, Xingjiu Gao, Ran Animal Model Exp Med Review Article Endomucin is a type I integral membrane glycoprotein, which is expressed in venous and capillary endothelial cells. It consists of 261 amino acids with an extracellular domain that is highly O‐glycosylated at serine and threonine residues and has several potential N‐glycosylation sites. Endomucin plays an important role in biological processes such as cell interaction, molecular cell signaling, angiogenesis and cell migration, and in recent years it has also been identified as an anti‐adhesion molecule and a marker of endothelial cells. While it has been shown to be involved in a number of physiological and pathological mechanisms, many of its functions remain unknown, and further study is needed. This article reviews research progress on the function of endomucin to date, in order to provide guidance for future studies. John Wiley and Sons Inc. 2021-01-15 /pmc/articles/PMC7824966/ /pubmed/33532708 http://dx.doi.org/10.1002/ame2.12142 Text en © 2021 The Authors. Animal Models and Experimental Medicine published by John Wiley & Sons Australia, Ltd on behalf of The Chinese Association for Laboratory Animal Sciences This is an open access article under the terms of the http://creativecommons.org/licenses/by/4.0/ License, which permits use, distribution and reproduction in any medium, provided the original work is properly cited. |
spellingShingle | Review Article Zhang, Guoxin Yang, Xingjiu Gao, Ran Research progress on the structure and function of endomucin |
title | Research progress on the structure and function of endomucin |
title_full | Research progress on the structure and function of endomucin |
title_fullStr | Research progress on the structure and function of endomucin |
title_full_unstemmed | Research progress on the structure and function of endomucin |
title_short | Research progress on the structure and function of endomucin |
title_sort | research progress on the structure and function of endomucin |
topic | Review Article |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC7824966/ https://www.ncbi.nlm.nih.gov/pubmed/33532708 http://dx.doi.org/10.1002/ame2.12142 |
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