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dc.contributor.authorMusiime, Moses
dc.contributor.authorChang, Joan
dc.contributor.authorHansen, Uwe
dc.contributor.authorKadler, Karl E.
dc.contributor.authorZeltz, Cedric
dc.contributor.authorGullberg, Elon Donald
dc.date.accessioned2022-03-03T13:23:38Z
dc.date.available2022-03-03T13:23:38Z
dc.date.created2022-01-12T18:14:49Z
dc.date.issued2021
dc.identifier.issn2073-4409
dc.identifier.urihttps://hdl.handle.net/11250/2982847
dc.description.abstractWith the increased awareness about the importance of the composition, organization, and stiffness of the extracellular matrix (ECM) for tissue homeostasis, there is a renewed need to understand the details of how cells recognize, assemble and remodel the ECM during dynamic tissue reorganization events. Fibronectin (FN) and fibrillar collagens are major proteins in the ECM of interstitial matrices. Whereas FN is abundant in cell culture studies, it is often only transiently expressed in the acute phase of wound healing and tissue regeneration, by contrast fibrillar collagens form a persistent robust scaffold in healing and regenerating tissues. Historically fibrillar collagens in interstitial matrices were seen merely as structural building blocks. Cell anchorage to the collagen matrix was thought to be indirect and occurring via proteins like FN and cell surface-mediated collagen fibrillogenesis was believed to require a FN matrix. The isolation of four collagen-binding integrins have challenged this dogma, and we now know that cells anchor directly to monomeric forms of fibrillar collagens via the α1β1, α2β1, α10β1 and α11β1 integrins. The binding of these integrins to the mature fibrous collagen matrices is more controversial and depends on availability of integrin-binding sites. With increased awareness about the importance of characterizing the total integrin repertoire on cells, including the integrin collagen receptors, the idea of an absolute dependence on FN for cell-mediated collagen fibrillogenesis needs to be re-evaluated. We will summarize data suggesting that collagen-binding integrins in vitro and in vivo are perfectly well suited for nucleating and supporting collagen fibrillogenesis, independent of FN.en_US
dc.language.isoengen_US
dc.publisherMDPIen_US
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleCollagen Assembly at the Cell Surface: Dogmas Revisiteden_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.description.versionpublishedVersionen_US
dc.rights.holderCopyright 2021 by the authors.en_US
dc.source.articlenumber662en_US
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1
dc.identifier.doi10.3390/cells10030662
dc.identifier.cristin1979902
dc.source.journalCellsen_US
dc.relation.projectNorges forskningsråd: 223250en_US
dc.identifier.citationCells. 2021, 10 (3), 662.en_US
dc.source.volume10en_US
dc.source.issue3en_US


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Navngivelse 4.0 Internasjonal
Except where otherwise noted, this item's license is described as Navngivelse 4.0 Internasjonal