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Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin

The cadherins are a family of homophilic adhesion molecules that play a vital role in the formation of cellular junctions and in tissue morphogenesis. Members of the integrin family are also involved in cell to cell adhesion, but bind heterophilically to immunoglobulin superfamily molecules such as...

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Detalles Bibliográficos
Autores principales: Higgins, Jonathan M.G., Mandlebrot, Didier A., Shaw, Sunil K., Russell, Gary J., Murphy, Elizabeth A., Chen, Yih-Tai, Nelson, W. James, Parker, Christina M., Brenner, Michael B.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1998
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132596/
https://www.ncbi.nlm.nih.gov/pubmed/9425167
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author Higgins, Jonathan M.G.
Mandlebrot, Didier A.
Shaw, Sunil K.
Russell, Gary J.
Murphy, Elizabeth A.
Chen, Yih-Tai
Nelson, W. James
Parker, Christina M.
Brenner, Michael B.
author_facet Higgins, Jonathan M.G.
Mandlebrot, Didier A.
Shaw, Sunil K.
Russell, Gary J.
Murphy, Elizabeth A.
Chen, Yih-Tai
Nelson, W. James
Parker, Christina M.
Brenner, Michael B.
author_sort Higgins, Jonathan M.G.
collection PubMed
description The cadherins are a family of homophilic adhesion molecules that play a vital role in the formation of cellular junctions and in tissue morphogenesis. Members of the integrin family are also involved in cell to cell adhesion, but bind heterophilically to immunoglobulin superfamily molecules such as intracellular adhesion molecule (ICAM)–1, vascular cell adhesion molecule (VCAM)–1, or mucosal addressin cell adhesion molecule (MadCAM)–1. Recently, an interaction between epithelial (E-) cadherin and the mucosal lymphocyte integrin, α(E)β(7), has been proposed. Here, we demonstrate that a human E-cadherin–Fc fusion protein binds directly to soluble recombinant α(E)β(7), and to α(E)β(7) solubilized from intraepithelial T lymphocytes. Furthermore, intraepithelial lymphocytes or transfected JY′ cells expressing the α(E)β(7) integrin adhere strongly to purified E-cadherin–Fc coated on plastic, and the adhesion can be inhibited by antibodies to α(E)β(7) or E-cadherin. The binding of α(E)β(7) integrin to cadherins is selective since cell adhesion to P-cadherin–Fc through α(E)β(7) requires >100-fold more fusion protein than to E-cadherin–Fc. Although the structure of the α(E)-chain is unique among integrins, the avidity of α(E)β(7) for E-cadherin can be regulated by divalent cations or phorbol myristate acetate. Cross-linking of the T cell receptor complex on intraepithelial lymphocytes increases the avidity of α(E)β(7) for E-cadherin, and may provide a mechanism for the adherence and activation of lymphocytes within the epithelium in the presence of specific foreign antigen. Thus, despite its dissimilarity to known integrin ligands, the specific molecular interaction demonstrated here indicates that E-cadherin is a direct counter receptor for the α(E)β(7) integrin.
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spelling pubmed-21325962008-05-01 Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin Higgins, Jonathan M.G. Mandlebrot, Didier A. Shaw, Sunil K. Russell, Gary J. Murphy, Elizabeth A. Chen, Yih-Tai Nelson, W. James Parker, Christina M. Brenner, Michael B. J Cell Biol Article The cadherins are a family of homophilic adhesion molecules that play a vital role in the formation of cellular junctions and in tissue morphogenesis. Members of the integrin family are also involved in cell to cell adhesion, but bind heterophilically to immunoglobulin superfamily molecules such as intracellular adhesion molecule (ICAM)–1, vascular cell adhesion molecule (VCAM)–1, or mucosal addressin cell adhesion molecule (MadCAM)–1. Recently, an interaction between epithelial (E-) cadherin and the mucosal lymphocyte integrin, α(E)β(7), has been proposed. Here, we demonstrate that a human E-cadherin–Fc fusion protein binds directly to soluble recombinant α(E)β(7), and to α(E)β(7) solubilized from intraepithelial T lymphocytes. Furthermore, intraepithelial lymphocytes or transfected JY′ cells expressing the α(E)β(7) integrin adhere strongly to purified E-cadherin–Fc coated on plastic, and the adhesion can be inhibited by antibodies to α(E)β(7) or E-cadherin. The binding of α(E)β(7) integrin to cadherins is selective since cell adhesion to P-cadherin–Fc through α(E)β(7) requires >100-fold more fusion protein than to E-cadherin–Fc. Although the structure of the α(E)-chain is unique among integrins, the avidity of α(E)β(7) for E-cadherin can be regulated by divalent cations or phorbol myristate acetate. Cross-linking of the T cell receptor complex on intraepithelial lymphocytes increases the avidity of α(E)β(7) for E-cadherin, and may provide a mechanism for the adherence and activation of lymphocytes within the epithelium in the presence of specific foreign antigen. Thus, despite its dissimilarity to known integrin ligands, the specific molecular interaction demonstrated here indicates that E-cadherin is a direct counter receptor for the α(E)β(7) integrin. The Rockefeller University Press 1998-01-12 /pmc/articles/PMC2132596/ /pubmed/9425167 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 Article
Higgins, Jonathan M.G.
Mandlebrot, Didier A.
Shaw, Sunil K.
Russell, Gary J.
Murphy, Elizabeth A.
Chen, Yih-Tai
Nelson, W. James
Parker, Christina M.
Brenner, Michael B.
Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin
title Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin
title_full Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin
title_fullStr Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin
title_full_unstemmed Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin
title_short Direct and Regulated Interaction of Integrin α(E)β(7) with E-Cadherin
title_sort direct and regulated interaction of integrin α(e)β(7) with e-cadherin
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132596/
https://www.ncbi.nlm.nih.gov/pubmed/9425167
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