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Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family
In the present study, we showed that activation of human CD4 T cells can be induced by anti-CD3 and collagen in a serum-free system. This activation was inhibited by the addition of peptides containing the RGD or Gly-Pro-X sequences. Significantly, we demonstrated that both the 1F7 (CD26) structure...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1990
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188344/ https://www.ncbi.nlm.nih.gov/pubmed/2165129 |
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collection | PubMed |
description | In the present study, we showed that activation of human CD4 T cells can be induced by anti-CD3 and collagen in a serum-free system. This activation was inhibited by the addition of peptides containing the RGD or Gly-Pro-X sequences. Significantly, we demonstrated that both the 1F7 (CD26) structure and the VLA integrin family, particularly the VLA- 3 complex, contribute to the functional interaction between collagen and CD4 cells since anti-1F7 and anti-VLA-3 specifically inhibited this collagen-induced CD4 cell activation. Biochemical studies showed that the 1F7 structure is not a member of the VLA integrin family. These results thus indicated that two different families of antigens serve as functional collagen receptors for CD4 T cell activation. |
format | Text |
id | pubmed-2188344 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1990 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21883442008-04-17 Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family J Exp Med Articles In the present study, we showed that activation of human CD4 T cells can be induced by anti-CD3 and collagen in a serum-free system. This activation was inhibited by the addition of peptides containing the RGD or Gly-Pro-X sequences. Significantly, we demonstrated that both the 1F7 (CD26) structure and the VLA integrin family, particularly the VLA- 3 complex, contribute to the functional interaction between collagen and CD4 cells since anti-1F7 and anti-VLA-3 specifically inhibited this collagen-induced CD4 cell activation. Biochemical studies showed that the 1F7 structure is not a member of the VLA integrin family. These results thus indicated that two different families of antigens serve as functional collagen receptors for CD4 T cell activation. The Rockefeller University Press 1990-08-01 /pmc/articles/PMC2188344/ /pubmed/2165129 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 Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family |
title | Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family |
title_full | Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family |
title_fullStr | Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family |
title_full_unstemmed | Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family |
title_short | Human CD4 helper T cell activation: functional involvement of two distinct collagen receptors, 1F7 and VLA integrin family |
title_sort | human cd4 helper t cell activation: functional involvement of two distinct collagen receptors, 1f7 and vla integrin family |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2188344/ https://www.ncbi.nlm.nih.gov/pubmed/2165129 |