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Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells
The mechanism of cell complex formation between lymphocytes and stromal cells was investigated. We found that lymphoid lines of both T and B lineages could form cell complexes with stromal cells from the thymus as well as bone marrow but not with macrophages or typical fibroblast lines. Formation of...
Formato: | Texto |
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Lenguaje: | English |
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The Rockefeller University Press
1991
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Acceso en línea: | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118781/ https://www.ncbi.nlm.nih.gov/pubmed/1988540 |
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collection | PubMed |
description | The mechanism of cell complex formation between lymphocytes and stromal cells was investigated. We found that lymphoid lines of both T and B lineages could form cell complexes with stromal cells from the thymus as well as bone marrow but not with macrophages or typical fibroblast lines. Formation of these cell complexes is temperature dependent and requires the presence of Mg2+, active cellular metabolism, and microfilament assembly of cytoskeleton. We raised an antiserum against a thymic stromal cell clone (BATE-2) in rats and found that, after absorption, this serum could effectively block cell complex formation between lymphocytes and stromal cells from both thymus and bone marrow. An efficient blocking was obtained only when the antiserum was added at the initial stage of cell interaction. From the blocking experiments and the SDS-PAGE analysis of immunoprecipitated materials from the stromal cell surface, we identified a unique 107-kD glycoprotein on the stromal cells as a molecule for mediating stromal cell-lymphocyte interaction. This is further supported by the findings that an antiserum raised in hamsters against the excised gel band corresponding to 107 kD, which specifically immunoprecipitated the 107-kD molecule, effectively blocked the lymphocyte-stromal cell interaction. The possible function of this molecule in hematolymphoid development is discussed. |
format | Text |
id | pubmed-2118781 |
institution | National Center for Biotechnology Information |
language | English |
publishDate | 1991 |
publisher | The Rockefeller University Press |
record_format | MEDLINE/PubMed |
spelling | pubmed-21187812008-04-17 Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells J Exp Med Articles The mechanism of cell complex formation between lymphocytes and stromal cells was investigated. We found that lymphoid lines of both T and B lineages could form cell complexes with stromal cells from the thymus as well as bone marrow but not with macrophages or typical fibroblast lines. Formation of these cell complexes is temperature dependent and requires the presence of Mg2+, active cellular metabolism, and microfilament assembly of cytoskeleton. We raised an antiserum against a thymic stromal cell clone (BATE-2) in rats and found that, after absorption, this serum could effectively block cell complex formation between lymphocytes and stromal cells from both thymus and bone marrow. An efficient blocking was obtained only when the antiserum was added at the initial stage of cell interaction. From the blocking experiments and the SDS-PAGE analysis of immunoprecipitated materials from the stromal cell surface, we identified a unique 107-kD glycoprotein on the stromal cells as a molecule for mediating stromal cell-lymphocyte interaction. This is further supported by the findings that an antiserum raised in hamsters against the excised gel band corresponding to 107 kD, which specifically immunoprecipitated the 107-kD molecule, effectively blocked the lymphocyte-stromal cell interaction. The possible function of this molecule in hematolymphoid development is discussed. The Rockefeller University Press 1991-02-01 /pmc/articles/PMC2118781/ /pubmed/1988540 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 Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells |
title | Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells |
title_full | Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells |
title_fullStr | Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells |
title_full_unstemmed | Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells |
title_short | Identification of a 107-kD glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells |
title_sort | identification of a 107-kd glycoprotein that mediates adhesion between stromal cells and hematolymphoid cells |
topic | Articles |
url | https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2118781/ https://www.ncbi.nlm.nih.gov/pubmed/1988540 |