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GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing
There are many molecules that define regulatory T cells (Tregs) phenotypically and functionally. Glycoprotein A repetitions predominant (GARP) is a transmembrane protein containing leucine rich repeats. Recently, GARP is found to express highly on the surface of activated Tregs. The combination of G...
Autores principales: | , , |
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Formato: | Online Artículo Texto |
Lenguaje: | English |
Publicado: |
Impact Journals LLC
2016
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Materias: | |
Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5173174/ https://www.ncbi.nlm.nih.gov/pubmed/27095576 http://dx.doi.org/10.18632/oncotarget.8753 |
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author | Sun, Liping Jin, Hao Li, Hui |
author_facet | Sun, Liping Jin, Hao Li, Hui |
author_sort | Sun, Liping |
collection | PubMed |
description | There are many molecules that define regulatory T cells (Tregs) phenotypically and functionally. Glycoprotein A repetitions predominant (GARP) is a transmembrane protein containing leucine rich repeats. Recently, GARP is found to express highly on the surface of activated Tregs. The combination of GARP and other surface molecules isolates Tregs with higher purity. Besides, GARP is a cell surface molecule of Tregs that maintains their regulatory function and homeosatsis. GARP has also been proved to promote the activation and secretion of transforming growth factor β (TGF-β). Moreover, its potential value in cancer immunotherapy is also discussed in this work. |
format | Online Article Text |
id | pubmed-5173174 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 2016 |
publisher | Impact Journals LLC |
record_format | MEDLINE/PubMed |
spelling | pubmed-51731742016-12-23 GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing Sun, Liping Jin, Hao Li, Hui Oncotarget Review There are many molecules that define regulatory T cells (Tregs) phenotypically and functionally. Glycoprotein A repetitions predominant (GARP) is a transmembrane protein containing leucine rich repeats. Recently, GARP is found to express highly on the surface of activated Tregs. The combination of GARP and other surface molecules isolates Tregs with higher purity. Besides, GARP is a cell surface molecule of Tregs that maintains their regulatory function and homeosatsis. GARP has also been proved to promote the activation and secretion of transforming growth factor β (TGF-β). Moreover, its potential value in cancer immunotherapy is also discussed in this work. Impact Journals LLC 2016-04-15 /pmc/articles/PMC5173174/ /pubmed/27095576 http://dx.doi.org/10.18632/oncotarget.8753 Text en Copyright: © 2016 Sun et al. http://creativecommons.org/licenses/by/2.5/ This is an open-access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited. |
spellingShingle | Review Sun, Liping Jin, Hao Li, Hui GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing |
title | GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing |
title_full | GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing |
title_fullStr | GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing |
title_full_unstemmed | GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing |
title_short | GARP: a surface molecule of regulatory T cells that is involved in the regulatory function and TGF-β releasing |
title_sort | garp: a surface molecule of regulatory t cells that is involved in the regulatory function and tgf-β releasing |
topic | Review |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC5173174/ https://www.ncbi.nlm.nih.gov/pubmed/27095576 http://dx.doi.org/10.18632/oncotarget.8753 |
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