Please use this identifier to cite or link to this item:
https://doi.org/10.21256/zhaw-22187Full metadata record
| DC Field | Value | Language |
|---|---|---|
| dc.contributor.author | Graham, Jenna | - |
| dc.contributor.author | Raghunath, Michael | - |
| dc.contributor.author | Vogel, Viola | - |
| dc.date.accessioned | 2021-03-26T15:18:18Z | - |
| dc.date.available | 2021-03-26T15:18:18Z | - |
| dc.date.issued | 2019-11 | - |
| dc.identifier.issn | 2047-4830 | de_CH |
| dc.identifier.issn | 2047-4849 | de_CH |
| dc.identifier.uri | https://digitalcollection.zhaw.ch/handle/11475/22187 | - |
| dc.description.abstract | Macromolecular crowding is used by tissue engineers to accelerate extracellular matrix assembly in vitro, however, most mechanistic studies focus on the impact of crowding on collagen fiber assembly and largely ignore the highly abundant provisional matrix protein fibronectin. We show that the accelerated collagen I assembly as induced by the neutral crowding molecule Ficoll is regulated by cell access to fibronectin. Ficoll treatment leads to significant increases in the amount of surface adherent fibronectin, which can readily be harvested by cells to speed up fibrillogenesis. FRET studies reveal that Ficoll crowding also upregulates the total amount of fibronectin fibers in a low-tension state through upregulating fibronectin assembly. Since un-stretched fibronectin fibers have more collagen binding sites to nucleate the onset of collagen fibrillogenesis, our data suggest that the Ficoll-induced upregulation of low-tension fibronectin fibers contributes to enhanced collagen assembly in crowded conditions. In contrast, chemical cross-linking of fibronectin to the glass substrate prior to cell seeding prevents early force mediated fibronectin harvesting from the substrate and suppresses upregulation of collagen I assembly in the presence of Ficoll, even though the crowded environment is known to drive enzymatic cleavage of procollagen and collagen fiber formation. To show that our findings can be exploited for tissue engineering applications, we demonstrate that the addition of supplemental fibronectin in the form of an adsorbed coating markedly improves the speed of tissue formation under crowding conditions. | de_CH |
| dc.language.iso | en | de_CH |
| dc.publisher | Royal Society of Chemistry | de_CH |
| dc.relation.ispartof | Biomaterials Science | de_CH |
| dc.rights | http://creativecommons.org/licenses/by/3.0/ | de_CH |
| dc.subject.ddc | 610.28: Biomedizin, Biomedizinische Technik | de_CH |
| dc.title | Fibrillar fibronectin plays a key role as nucleator of collagen I polymerization during macromolecular crowding-enhanced matrix assembly | de_CH |
| dc.type | Beitrag in wissenschaftlicher Zeitschrift | de_CH |
| dcterms.type | Text | de_CH |
| zhaw.departement | Life Sciences und Facility Management | de_CH |
| zhaw.organisationalunit | Institut für Chemie und Biotechnologie (ICBT) | de_CH |
| dc.identifier.doi | 10.1039/C9BM00868C | de_CH |
| dc.identifier.doi | 10.21256/zhaw-22187 | - |
| zhaw.funding.eu | No | de_CH |
| zhaw.issue | 11 | de_CH |
| zhaw.originated.zhaw | Yes | de_CH |
| zhaw.pages.end | 4535 | de_CH |
| zhaw.pages.start | 4519 | de_CH |
| zhaw.publication.status | publishedVersion | de_CH |
| zhaw.volume | 7 | de_CH |
| zhaw.publication.review | Peer review (Publikation) | de_CH |
| zhaw.author.additional | No | de_CH |
| zhaw.display.portrait | Yes | de_CH |
| Appears in collections: | Publikationen Life Sciences und Facility Management | |
Files in This Item:
| File | Description | Size | Format | |
|---|---|---|---|---|
| 2019_Graham-Raghunath-Vogel_Fibrillar-fibronectin-plays-a-key-role-as-nucleator-of-collagen-I-polymerization.pdf | 16.8 MB | Adobe PDF |  View/Open |
Show simple item record
Graham, J., Raghunath, M., & Vogel, V. (2019). Fibrillar fibronectin plays a key role as nucleator of collagen I polymerization during macromolecular crowding-enhanced matrix assembly. Biomaterials Science, 7(11), 4519–4535. https://doi.org/10.1039/C9BM00868C
Graham, J., Raghunath, M. and Vogel, V. (2019) ‘Fibrillar fibronectin plays a key role as nucleator of collagen I polymerization during macromolecular crowding-enhanced matrix assembly’, Biomaterials Science, 7(11), pp. 4519–4535. Available at: https://doi.org/10.1039/C9BM00868C.
J. Graham, M. Raghunath, and V. Vogel, “Fibrillar fibronectin plays a key role as nucleator of collagen I polymerization during macromolecular crowding-enhanced matrix assembly,” Biomaterials Science, vol. 7, no. 11, pp. 4519–4535, Nov. 2019, doi: 10.1039/C9BM00868C.
GRAHAM, Jenna, Michael RAGHUNATH und Viola VOGEL, 2019. Fibrillar fibronectin plays a key role as nucleator of collagen I polymerization during macromolecular crowding-enhanced matrix assembly. Biomaterials Science. November 2019. Bd. 7, Nr. 11, S. 4519–4535. DOI 10.1039/C9BM00868C
Graham, Jenna, Michael Raghunath, and Viola Vogel. 2019. “Fibrillar Fibronectin Plays a Key Role as Nucleator of Collagen I Polymerization during Macromolecular Crowding-Enhanced Matrix Assembly.” Biomaterials Science 7 (11): 4519–35. https://doi.org/10.1039/C9BM00868C.
Graham, Jenna, et al. “Fibrillar Fibronectin Plays a Key Role as Nucleator of Collagen I Polymerization during Macromolecular Crowding-Enhanced Matrix Assembly.” Biomaterials Science, vol. 7, no. 11, Nov. 2019, pp. 4519–35, https://doi.org/10.1039/C9BM00868C.
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