Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein

[Image: see text] While evidence is mounting that cells exploit protein unfolding for mechanochemical signal conversion (mechanotransduction), what mechanisms are in place to deal with the unwanted consequences of exposing hydrophobic residues upon force-induced protein unfolding? Here, we show that...

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Autores principales: Little, William C., Schwartlander, Ruth, Smith, Michael L., Gourdon, Delphine, Vogel, Viola
Formato: Texto
Lenguaje:English
Publicado: American Chemical Society 2009
Acceso en línea:https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2790870/
https://www.ncbi.nlm.nih.gov/pubmed/19743815
http://dx.doi.org/10.1021/nl902365z
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author Little, William C.
Schwartlander, Ruth
Smith, Michael L.
Gourdon, Delphine
Vogel, Viola
author_facet Little, William C.
Schwartlander, Ruth
Smith, Michael L.
Gourdon, Delphine
Vogel, Viola
author_sort Little, William C.
collection PubMed
description [Image: see text] While evidence is mounting that cells exploit protein unfolding for mechanochemical signal conversion (mechanotransduction), what mechanisms are in place to deal with the unwanted consequences of exposing hydrophobic residues upon force-induced protein unfolding? Here, we show that mechanical chaperones exist that can transiently bind to hydrophobic residues that are freshly exposed by mechanical force. The stretch-upregulated binding of albumin or casein to fibronectin fibers is reversible and does not inhibit fiber contraction once the tension is released.
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spelling pubmed-27908702009-12-09 Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein Little, William C. Schwartlander, Ruth Smith, Michael L. Gourdon, Delphine Vogel, Viola Nano Lett [Image: see text] While evidence is mounting that cells exploit protein unfolding for mechanochemical signal conversion (mechanotransduction), what mechanisms are in place to deal with the unwanted consequences of exposing hydrophobic residues upon force-induced protein unfolding? Here, we show that mechanical chaperones exist that can transiently bind to hydrophobic residues that are freshly exposed by mechanical force. The stretch-upregulated binding of albumin or casein to fibronectin fibers is reversible and does not inhibit fiber contraction once the tension is released. American Chemical Society 2009-09-10 2009-12-09 /pmc/articles/PMC2790870/ /pubmed/19743815 http://dx.doi.org/10.1021/nl902365z Text en Copyright © 2009 American Chemical Society http://pubs.acs.org This is an open-access article distributed under the ACS AuthorChoice Terms & Conditions. Any use of this article, must conform to the terms of that license which are available at http://pubs.acs.org.
spellingShingle Little, William C.
Schwartlander, Ruth
Smith, Michael L.
Gourdon, Delphine
Vogel, Viola
Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein
title Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein
title_full Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein
title_fullStr Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein
title_full_unstemmed Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein
title_short Stretched Extracellular Matrix Proteins Turn Fouling and Are Functionally Rescued by the Chaperones Albumin and Casein
title_sort stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein
url https://www.ncbi.nlm.nih.gov/pmc/articles/PMC2790870/
https://www.ncbi.nlm.nih.gov/pubmed/19743815
http://dx.doi.org/10.1021/nl902365z
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