Electric Fields and Inflammation: May the Force be with You

Integrins are a family of ubiquitous cell surface receptors comprising heterodimers of β and α chains that are required for cell adhesion and motility. Integrin-dependent adhesion and signaling is associated with major conformational changes in the ectodomain as it shifts from a low-affinity “bent”...

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Main Authors: Simon B. Brown, Ian Dransfield
Format: Article
Language:English
Published: Hindawi Limited 2008-01-01
Series:The Scientific World Journal
Online Access:http://dx.doi.org/10.1100/tsw.2008.158
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spelling doaj-752e5c538abc4aaaa6ed457888ed559a2020-11-24T21:30:48ZengHindawi LimitedThe Scientific World Journal1537-744X2008-01-0181280129410.1100/tsw.2008.158Electric Fields and Inflammation: May the Force be with YouSimon B. Brown0Ian Dransfield1MRC Centre for Inflammation Research, Queen's Medical Research Institute, University of Edinburgh, 47 Little France Crescent, Edinburgh, EH16 4TJ, UKMRC Centre for Inflammation Research, Queen's Medical Research Institute, University of Edinburgh, 47 Little France Crescent, Edinburgh, EH16 4TJ, UKIntegrins are a family of ubiquitous cell surface receptors comprising heterodimers of β and α chains that are required for cell adhesion and motility. Integrin-dependent adhesion and signaling is associated with major conformational changes in the ectodomain as it shifts from a low-affinity “bent” to a high-affinity “extended” structure. The ability of a cell to regulate dynamically the affinity or activation state of an integrin, and hence its binding to extracellular matrix or cell adhesion molecules, is assumed to be driven by intracellular signaling events transmitted by protein binding to the cytoplasmic tail. The binding of an integrin to its ligand can then transmit signals back into the cell to regulate the formation of a macromolecular focal adhesion complex that effectively anchors the cytoskeleton to the adhesion site. Many proteins have been reported to associate physically and functionally with integrins, leading to altered signaling events. A particularly intriguing molecular association exists between integrins and transmembrane proteins that gate the movement of charge, especially voltage-gated potassium channels, although the significance of this interaction is not understood. Although ample evidence indicates that the engagement of integrins can promote potassium efflux by both excitable and nonexcitable cells, we speculate the converse, that the activation state of integrins is dynamically regulated by changes in a transmembrane potential. In this way, direct-current electric fields generated at a site of tissue injury can promote the galvanotaxis or directed migration of cells involved in tissue repair and inflammation.http://dx.doi.org/10.1100/tsw.2008.158
collection DOAJ
language English
format Article
sources DOAJ
author Simon B. Brown
Ian Dransfield
spellingShingle Simon B. Brown
Ian Dransfield
Electric Fields and Inflammation: May the Force be with You
The Scientific World Journal
author_facet Simon B. Brown
Ian Dransfield
author_sort Simon B. Brown
title Electric Fields and Inflammation: May the Force be with You
title_short Electric Fields and Inflammation: May the Force be with You
title_full Electric Fields and Inflammation: May the Force be with You
title_fullStr Electric Fields and Inflammation: May the Force be with You
title_full_unstemmed Electric Fields and Inflammation: May the Force be with You
title_sort electric fields and inflammation: may the force be with you
publisher Hindawi Limited
series The Scientific World Journal
issn 1537-744X
publishDate 2008-01-01
description Integrins are a family of ubiquitous cell surface receptors comprising heterodimers of β and α chains that are required for cell adhesion and motility. Integrin-dependent adhesion and signaling is associated with major conformational changes in the ectodomain as it shifts from a low-affinity “bent” to a high-affinity “extended” structure. The ability of a cell to regulate dynamically the affinity or activation state of an integrin, and hence its binding to extracellular matrix or cell adhesion molecules, is assumed to be driven by intracellular signaling events transmitted by protein binding to the cytoplasmic tail. The binding of an integrin to its ligand can then transmit signals back into the cell to regulate the formation of a macromolecular focal adhesion complex that effectively anchors the cytoskeleton to the adhesion site. Many proteins have been reported to associate physically and functionally with integrins, leading to altered signaling events. A particularly intriguing molecular association exists between integrins and transmembrane proteins that gate the movement of charge, especially voltage-gated potassium channels, although the significance of this interaction is not understood. Although ample evidence indicates that the engagement of integrins can promote potassium efflux by both excitable and nonexcitable cells, we speculate the converse, that the activation state of integrins is dynamically regulated by changes in a transmembrane potential. In this way, direct-current electric fields generated at a site of tissue injury can promote the galvanotaxis or directed migration of cells involved in tissue repair and inflammation.
url http://dx.doi.org/10.1100/tsw.2008.158
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