» Articles » PMID: 19743815

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

Overview
Journal Nano Lett
Specialty Biotechnology
Date 2009 Sep 12
PMID 19743815
Citations 19
Authors
Affiliations
Soon will be listed here.
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.

Citing Articles

RASSF1A controls tissue stiffness and cancer stem-like cells in lung adenocarcinoma.

Pankova D, Jiang Y, Chatzifrangkeskou M, Vendrell I, Buzzelli J, Ryan A EMBO J. 2019; 38(13):e100532.

PMID: 31268606 PMC: 6600643. DOI: 10.15252/embj.2018100532.


Fibronectin fiber creep under constant force loading.

Bradshaw M, Hoffmann G, Wong J, Smith M Acta Biomater. 2019; 88:78-85.

PMID: 30780000 PMC: 6777959. DOI: 10.1016/j.actbio.2019.02.022.


Profiling the Serum Protein Corona of Fibrillar Human Islet Amyloid Polypeptide.

Pilkington E, Gustafsson O, Xing Y, Hernandez-Fernaud J, Zampronio C, Kakinen A ACS Nano. 2018; 12(6):6066-6078.

PMID: 29746093 PMC: 6239983. DOI: 10.1021/acsnano.8b02346.


Novel peptide probes to assess the tensional state of fibronectin fibers in cancer.

Arnoldini S, Moscaroli A, Chabria M, Hilbert M, Hertig S, Schibli R Nat Commun. 2017; 8(1):1793.

PMID: 29176724 PMC: 5702617. DOI: 10.1038/s41467-017-01846-0.


Walking the Line: A Fibronectin Fiber-Guided Assay to Probe Early Steps of (Lymph)angiogenesis.

Mitsi M, Schulz M, Gousopoulos E, Ochsenbein A, Detmar M, Vogel V PLoS One. 2015; 10(12):e0145210.

PMID: 26689200 PMC: 4686943. DOI: 10.1371/journal.pone.0145210.


References
1.
Hong D, Hagihara Y, Kato H, Goto Y . Flexible loop of beta 2-glycoprotein I domain V specifically interacts with hydrophobic ligands. Biochemistry. 2001; 40(27):8092-100. DOI: 10.1021/bi010196v. View

2.
Fernandez J, Li H . Force-clamp spectroscopy monitors the folding trajectory of a single protein. Science. 2004; 303(5664):1674-8. DOI: 10.1126/science.1092497. View

3.
Karuri N, Lin Z, Rye H, Schwarzbauer J . Probing the conformation of the fibronectin III1-2 domain by fluorescence resonance energy transfer. J Biol Chem. 2008; 284(6):3445-52. PMC: 2635030. DOI: 10.1074/jbc.M805025200. View

4.
Bethell R, Gray N, Penn C . The kinetics of the acid-induced conformational change of influenza virus haemagglutinin can be followed using 1,1'-bis(4-anilino-5-naphthalenesulphonic acid). Biochem Biophys Res Commun. 1995; 206(1):355-61. DOI: 10.1006/bbrc.1995.1049. View

5.
Smith M, Gourdon D, Little W, Kubow K, Eguiluz R, Luna-Morris S . Force-induced unfolding of fibronectin in the extracellular matrix of living cells. PLoS Biol. 2007; 5(10):e268. PMC: 1994993. DOI: 10.1371/journal.pbio.0050268. View