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  Fibronectin promotes directional persistence in fibroblast migration through interactions with both its cell-binding and heparin-binding domains

Missirlis, D., Haraszti, T., Kessler, H., & Spatz, J. (2017). Fibronectin promotes directional persistence in fibroblast migration through interactions with both its cell-binding and heparin-binding domains. Scientific Reports, 7: 3711, pp. 1-16. doi:10.1038/s41598-017-03701-0.

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Item Permalink: http://hdl.handle.net/11858/00-001M-0000-002D-C840-A Version Permalink: http://hdl.handle.net/11858/00-001M-0000-002E-5E1E-7
Genre: Journal Article

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 Creators:
Missirlis, Dimitris1, 2, Author              
Haraszti, Tamas1, 2, Author              
Kessler, Horst, Author
Spatz, Joachim1, 2, Author
Affiliations:
1Cellular Biophysics, Max Planck Institute for Medical Research, Max Planck Society, ou_2364731              
2Biophysical Chemistry, Institute of Physical Chemistry, University of Heidelberg, 69120 Heidelberg, Germany, ou_persistent22              

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Free keywords: Extracellular matrix ; Integrins
 Abstract: The precise mechanisms through which insoluble, cell-adhesive ligands induce and regulate directional cell migration remain obscure. We recently demonstrated that elevated surface density of physically adsorbed plasma fibronectin (FN) promotes high directional persistence in fibroblast migration. While cell-FN association through integrins α5β1 and αvβ3 was necessary, substrates that selectively engaged these integrins did not support the phenotype. We here show that high directional persistence necessitates a combination of the cell-binding and C-terminal heparin-binding domains of FN, but does not require the engagement of syndecan-4 or integrin α4β1. FN treatment with various fixation agents indicated that associated changes in fibroblast motility were due to biochemical changes, rather than alterations in its physical state. The nature of the coating determined the ability of fibroblasts to assemble endogenous or exogenous FN, while FN fibrillogenesis played a minor, but significant, role in regulating directionality. Interestingly, knockdown of cellular FN abolished cell motility altogether, demonstrating a requirement for intracellular processes in enabling fibroblast migration on FN. Lastly, kinase inhibition experiments revealed that regulation of cell speed and directional persistence are decoupled. Hence, we have identified factors that render full-length FN a promoter of directional migration and discuss the possible, relevant mechanisms.

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Language(s): eng - English
 Dates: 2017-01-092017-05-082017-06-16
 Publication Status: Published online
 Pages: 16
 Publishing info: -
 Table of Contents: -
 Rev. Method: Peer
 Identifiers: DOI: 10.1038/s41598-017-03701-0
 Degree: -

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Title: Scientific Reports
  Abbreviation : Sci. Rep.
Source Genre: Journal
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Publ. Info: London, UK : Nature Publishing Group
Pages: - Volume / Issue: 7 Sequence Number: 3711 Start / End Page: 1 - 16 Identifier: ISSN: 2045-2322
CoNE: https://pure.mpg.de/cone/journals/resource/2045-2322