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Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication

Wounding of skin activates epidermal cell migration over exposed dermal collagen and fibronectin and over laminin 5 secreted into the provisional basement membrane. Gap junctional intercellular communication (GJIC) has been proposed to integrate the individual motile cells into a synchronized colony...

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Detalles Bibliográficos
Autores principales: Lampe, Paul D., Nguyen, Beth P., Gil, Susana, Usui, Marcia, Olerud, John, Takada, Yoshikazu, Carter, William G.
Formato: Texto
Lenguaje:English
Publicado: The Rockefeller University Press 1998
Materias:
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132974/
https://www.ncbi.nlm.nih.gov/pubmed/9852164
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author Lampe, Paul D.
Nguyen, Beth P.
Gil, Susana
Usui, Marcia
Olerud, John
Takada, Yoshikazu
Carter, William G.
author_facet Lampe, Paul D.
Nguyen, Beth P.
Gil, Susana
Usui, Marcia
Olerud, John
Takada, Yoshikazu
Carter, William G.
author_sort Lampe, Paul D.
collection PubMed
description Wounding of skin activates epidermal cell migration over exposed dermal collagen and fibronectin and over laminin 5 secreted into the provisional basement membrane. Gap junctional intercellular communication (GJIC) has been proposed to integrate the individual motile cells into a synchronized colony. We found that outgrowths of human keratinocytes in wounds or epibole cultures display parallel changes in the expression of laminin 5, integrin α3β1, E-cadherin, and the gap junctional protein connexin 43. Adhesion of keratinocytes on laminin 5, collagen, and fibronectin was found to differentially regulate GJIC. When keratinocytes were adhered on laminin 5, both structural (assembly of connexin 43 in gap junctions) and functional (dye transfer) assays showed a two- to threefold increase compared with collagen and five- to eightfold over fibronectin. Based on studies with immobilized integrin antibody and integrin-transfected Chinese hamster ovary cells, the interaction of integrin α3β1 with laminin 5 was sufficient to promote GJIC. Mapping of intermediate steps in the pathway linking α3β1–laminin 5 interactions to GJIC indicated that protein trafficking and Rho signaling were both required. We suggest that adhesion of epithelial cells to laminin 5 in the basement membrane via α3β1 promotes GJIC that integrates individual cells into synchronized epiboles.
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spelling pubmed-21329742008-05-01 Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication Lampe, Paul D. Nguyen, Beth P. Gil, Susana Usui, Marcia Olerud, John Takada, Yoshikazu Carter, William G. J Cell Biol Article Wounding of skin activates epidermal cell migration over exposed dermal collagen and fibronectin and over laminin 5 secreted into the provisional basement membrane. Gap junctional intercellular communication (GJIC) has been proposed to integrate the individual motile cells into a synchronized colony. We found that outgrowths of human keratinocytes in wounds or epibole cultures display parallel changes in the expression of laminin 5, integrin α3β1, E-cadherin, and the gap junctional protein connexin 43. Adhesion of keratinocytes on laminin 5, collagen, and fibronectin was found to differentially regulate GJIC. When keratinocytes were adhered on laminin 5, both structural (assembly of connexin 43 in gap junctions) and functional (dye transfer) assays showed a two- to threefold increase compared with collagen and five- to eightfold over fibronectin. Based on studies with immobilized integrin antibody and integrin-transfected Chinese hamster ovary cells, the interaction of integrin α3β1 with laminin 5 was sufficient to promote GJIC. Mapping of intermediate steps in the pathway linking α3β1–laminin 5 interactions to GJIC indicated that protein trafficking and Rho signaling were both required. We suggest that adhesion of epithelial cells to laminin 5 in the basement membrane via α3β1 promotes GJIC that integrates individual cells into synchronized epiboles. The Rockefeller University Press 1998-12-14 /pmc/articles/PMC2132974/ /pubmed/9852164 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
Lampe, Paul D.
Nguyen, Beth P.
Gil, Susana
Usui, Marcia
Olerud, John
Takada, Yoshikazu
Carter, William G.
Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication
title Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication
title_full Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication
title_fullStr Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication
title_full_unstemmed Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication
title_short Cellular Interaction of Integrin α3β1 with Laminin 5 Promotes Gap Junctional Communication
title_sort cellular interaction of integrin α3β1 with laminin 5 promotes gap junctional communication
topic Article
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2132974/
https://www.ncbi.nlm.nih.gov/pubmed/9852164
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