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Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein.

ABSTRACT: 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.

SUBMITTER: Little WC

PROVIDER: S-EPMC2790870 | biostudies-other | 2009 Dec

REPOSITORIES: biostudies-other

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Stretched extracellular matrix proteins turn fouling and are functionally rescued by the chaperones albumin and casein.

Little William C WC Schwartlander Ruth R Smith Michael L ML Gourdon Delphine D Vogel Viola V

Nano letters 20091201 12

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 ...[more]

PMID: 19743815

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