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dc.contributor.authorBansode, Sneha
dc.contributor.authorBashtanova, Uliana
dc.contributor.authorLi, Rui
dc.contributor.authorClark, Jonathan
dc.contributor.authorMüller, Karin H
dc.contributor.authorPuszkarska, Anna
dc.contributor.authorGoldberga, Ieva
dc.contributor.authorChetwood, Holly H
dc.contributor.authorReid, David G
dc.contributor.authorColwell, Lucy J
dc.contributor.authorSkepper, Jeremy N
dc.contributor.authorShanahan, Catherine M
dc.contributor.authorSchitter, Georg
dc.contributor.authorMesquida, Patrick
dc.contributor.authorDuer, Melinda J
dc.date.accessioned2020-03-29T01:38:10Z
dc.date.available2020-03-29T01:38:10Z
dc.date.issued2020-02-25
dc.identifier.issn2045-2322
dc.identifier.otherPMC7042214
dc.identifier.other32099005
dc.identifier.urihttps://www.repository.cam.ac.uk/handle/1810/303875
dc.description.abstractCollagen fibrils are central to the molecular organization of the extracellular matrix (ECM) and to defining the cellular microenvironment. Glycation of collagen fibrils is known to impact on cell adhesion and migration in the context of cancer and in model studies, glycation of collagen molecules has been shown to affect the binding of other ECM components to collagen. Here we use TEM to show that ribose-5-phosphate (R5P) glycation of collagen fibrils - potentially important in the microenvironment of actively dividing cells, such as cancer cells - disrupts the longitudinal ordering of the molecules in collagen fibrils and, using KFM and FLiM, that R5P-glycated collagen fibrils have a more negative surface charge than unglycated fibrils. Altered molecular arrangement can be expected to impact on the accessibility of cell adhesion sites and altered fibril surface charge on the integrity of the extracellular matrix structure surrounding glycated collagen fibrils. Both effects are highly relevant for cell adhesion and migration within the tumour microenvironment.
dc.languageeng
dc.rightsAttribution 4.0 International
dc.rights.urihttps://creativecommons.org/licenses/by/4.0/
dc.sourceessn: 2045-2322
dc.sourcenlmid: 101563288
dc.titleGlycation changes molecular organization and charge distribution in type I collagen fibrils.
dc.typeArticle
dc.date.updated2020-03-29T01:38:09Z
prism.issueIdentifier1
prism.publicationNameScientific reports
prism.volume10
dc.identifier.doi10.17863/CAM.50957
rioxxterms.versionofrecord10.1038/s41598-020-60250-9
rioxxterms.versionVoR
rioxxterms.licenseref.urihttps://creativecommons.org/licenses/by/4.0/
pubs.funder-project-idMedical Research Council (MR/M01066X/1)
pubs.funder-project-idAustrian Science Fund FWF (P 31238-N28)


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Attribution 4.0 International
Except where otherwise noted, this item's licence is described as Attribution 4.0 International