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Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM

Integrins can exist in different functional states with low or high binding capacity for particular ligands. We previously provided evidence that the integrin α6β1, on mouse eggs and on α6-transfected cells, interacted with the disintegrin domain of the sperm surface protein ADAM 2 (fertilin β). In...

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Autores principales: Chen, M.S., Almeida, E.A.C., Huovila, A.-P.J., Takahashi, Y., Shaw, L.M., Mercurio, A.M., White, J.M.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1999
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132920/
https://www.ncbi.nlm.nih.gov/pubmed/9971748
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author Chen, M.S.
Almeida, E.A.C.
Huovila, A.-P.J.
Takahashi, Y.
Shaw, L.M.
Mercurio, A.M.
White, J.M.
author_facet Chen, M.S.
Almeida, E.A.C.
Huovila, A.-P.J.
Takahashi, Y.
Shaw, L.M.
Mercurio, A.M.
White, J.M.
author_sort Chen, M.S.
collection PubMed
description Integrins can exist in different functional states with low or high binding capacity for particular ligands. We previously provided evidence that the integrin α6β1, on mouse eggs and on α6-transfected cells, interacted with the disintegrin domain of the sperm surface protein ADAM 2 (fertilin β). In the present study we tested the hypothesis that different states of α6β1 interact with fertilin and laminin, an extracellular matrix ligand for α6β1. Using α6-transfected cells we found that treatments (e.g., with phorbol myristate acetate or MnCl(2)) that increased adhesion to laminin inhibited sperm binding. Conversely, treatments that inhibited laminin adhesion increased sperm binding. Next, we compared the ability of fluorescent beads coated with either fertilin β or with the laminin E8 fragment to bind to eggs. In Ca(2+)-containing media, fertilin β beads bound to eggs via an interaction mediated by the disintegrin loop of fertilin β and by the α6 integrin subunit. In Ca(2+)-containing media, laminin E8 beads did not bind to eggs. Treatment of eggs with phorbol myristate acetate or with the actin disrupting agent, latrunculin A, inhibited fertilin bead binding, but did not induce laminin E8 bead binding. Treatment of eggs with Mn(2+) dramatically increased laminin E8 bead binding, and inhibited fertilin bead binding. Our results provide the first evidence that different states of an integrin (α6β1) can interact with an extracellular matrix ligand (laminin) or a membrane-anchored cell surface ligand (ADAM 2).
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spelling pubmed-21329202008-05-01 Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM Chen, M.S. Almeida, E.A.C. Huovila, A.-P.J. Takahashi, Y. Shaw, L.M. Mercurio, A.M. White, J.M. J Cell Biol Regular Articles Integrins can exist in different functional states with low or high binding capacity for particular ligands. We previously provided evidence that the integrin α6β1, on mouse eggs and on α6-transfected cells, interacted with the disintegrin domain of the sperm surface protein ADAM 2 (fertilin β). In the present study we tested the hypothesis that different states of α6β1 interact with fertilin and laminin, an extracellular matrix ligand for α6β1. Using α6-transfected cells we found that treatments (e.g., with phorbol myristate acetate or MnCl(2)) that increased adhesion to laminin inhibited sperm binding. Conversely, treatments that inhibited laminin adhesion increased sperm binding. Next, we compared the ability of fluorescent beads coated with either fertilin β or with the laminin E8 fragment to bind to eggs. In Ca(2+)-containing media, fertilin β beads bound to eggs via an interaction mediated by the disintegrin loop of fertilin β and by the α6 integrin subunit. In Ca(2+)-containing media, laminin E8 beads did not bind to eggs. Treatment of eggs with phorbol myristate acetate or with the actin disrupting agent, latrunculin A, inhibited fertilin bead binding, but did not induce laminin E8 bead binding. Treatment of eggs with Mn(2+) dramatically increased laminin E8 bead binding, and inhibited fertilin bead binding. Our results provide the first evidence that different states of an integrin (α6β1) can interact with an extracellular matrix ligand (laminin) or a membrane-anchored cell surface ligand (ADAM 2). The Rockefeller University Press 1999-02-08 /pmc/articles/PMC2132920/ /pubmed/9971748 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 Regular Articles
Chen, M.S.
Almeida, E.A.C.
Huovila, A.-P.J.
Takahashi, Y.
Shaw, L.M.
Mercurio, A.M.
White, J.M.
Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM
title Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM
title_full Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM
title_fullStr Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM
title_full_unstemmed Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM
title_short Evidence that Distinct States of the Integrin α6β1 Interact with Laminin and an ADAM
title_sort evidence that distinct states of the integrin α6β1 interact with laminin and an adam
topic Regular Articles
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132920/
https://www.ncbi.nlm.nih.gov/pubmed/9971748
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