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dc.contributor.authorKubow, Kristopher E.en_US
dc.contributor.authorVukmirovic, Radmilaen_US
dc.contributor.authorZhe, Linen_US
dc.contributor.authorKlotzsch, Enricoen_US
dc.contributor.authorSmith, Michael L.en_US
dc.contributor.authorGourdon, Delphineen_US
dc.contributor.authorLuna, Sheilaen_US
dc.contributor.authorVogel, Violaen_US
dc.coverage.spatialEnglanden_US
dc.date2015-07-09
dc.date.accessioned2018-07-18T12:32:56Z
dc.date.available2018-07-18T12:32:56Z
dc.date.issued2015-08-14
dc.identifierhttps://www.ncbi.nlm.nih.gov/pubmed/26272817
dc.identifier.citationKubow, K. E. et al. Mechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrix. Nat. Commun. 6:8026 doi: 10.1038/ncomms9026 (2015).
dc.identifier.issn2041-1723
dc.identifier.urihttps://hdl.handle.net/2144/29968
dc.description.abstractDespite the crucial role of extracellular matrix (ECM) in directing cell fate in healthy and diseased tissues--particularly in development, wound healing, tissue regeneration and cancer--the mechanisms that direct the assembly and regulate hierarchical architectures of ECM are poorly understood. Collagen I matrix assembly in vivo requires active fibronectin (Fn) fibrillogenesis by cells. Here we exploit Fn-FRET probes as mechanical strain sensors and demonstrate that collagen I fibres preferentially co-localize with more-relaxed Fn fibrils in the ECM of fibroblasts in cell culture. Fibre stretch-assay studies reveal that collagen I's Fn-binding domain is responsible for the mechano-regulated interaction. Furthermore, we show that Fn-collagen interactions are reciprocal: relaxed Fn fibrils act as multivalent templates for collagen assembly, but once assembled, collagen fibres shield Fn fibres from being stretched by cellular traction forces. Thus, in addition to the well-recognized, force-regulated, cell-matrix interactions, forces also tune the interactions between different structural ECM components.en_US
dc.description.sponsorship233157 - European Research Council; PN2 EY016586 - NEI NIH HHSen_US
dc.format.extent8026en_US
dc.languageeng
dc.relation.ispartofNat Commun
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/
dc.subjectScience & technologyen_US
dc.subjectResonance energy transferen_US
dc.subjectBacterial adhesinsen_US
dc.subjectRigidity responseen_US
dc.subjectTissue repairen_US
dc.subjectCellen_US
dc.subjectFibrilsen_US
dc.subjectAnimalsen_US
dc.subjectAscorbic aciden_US
dc.subjectBiomechanical phenomenaen_US
dc.subjectCollagen type Ien_US
dc.subjectExtracellular matrixen_US
dc.subjectFibroblastsen_US
dc.subjectFibronectinsen_US
dc.subjectFluorescence resonance energy transferen_US
dc.subjectMiceen_US
dc.subjectNIH 3T3 cellsen_US
dc.titleMechanical forces regulate the interactions of fibronectin and collagen I in extracellular matrixen_US
dc.typeArticleen_US
dc.identifier.doi10.1038/ncomms9026
pubs.elements-sourcepubmeden_US
pubs.notesEmbargo: Not knownen_US
pubs.organisational-groupBoston Universityen_US
pubs.organisational-groupBoston University, College of Engineeringen_US
pubs.organisational-groupBoston University, College of Engineering, Department of Biomedical Engineeringen_US
pubs.publication-statusPublished onlineen_US


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