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dc.contributor.authorCoron, Abba Elizabeth
dc.contributor.authorFonseca, Davi de Miranda
dc.contributor.authorSharma, Animesh
dc.contributor.authorSlupphaug, Geir
dc.contributor.authorStrand, Berit Løkensgard
dc.contributor.authorRokstad, Anne Mari A.
dc.date.accessioned2022-11-25T07:56:37Z
dc.date.available2022-11-25T07:56:37Z
dc.date.created2022-11-14T08:52:28Z
dc.date.issued2022
dc.identifier.issn2590-0064
dc.identifier.urihttps://hdl.handle.net/11250/3033994
dc.description.abstractProtein adsorption to biomaterial surfaces is considered a determining factor for the host response. Here we detail the protein adsorption profiles of alginate hydrogel microspheres relevant for cell therapy using mass spectrometry (MS)-based proteomics. The investigated microspheres include sulfated alginate (SA), high G alginate (HiG), and poly-l-lysine coated alginate (AP), which previously have been shown to exhibit different inflammatory and fibrotic responses. The biological significance was assessed in lepirudin-anticoagulated human whole blood (hWB) by functional analysis of the acute phase responses (complement and coagulation). Proteomic profiling revealed distinct signatures for the microspheres, wherein Ingenuity Pathway Analysis identified complement and coagulation as the top enriched canonical pathways. The levels of complement and coagulation activators and inhibitors were distinctly different, which was reflected in the functional hWB analyses: SA was highly enriched with inhibitory factors of complement and coagulation (e.g., C1 inhibitor, factor H, antithrombin-III, heparin cofactor 2), other heparin-binding proteins and factors promoting fibrinolysis (factor XII, plasma kallikrein), conforming to an anti-inflammatory and anti-fibrotic profile. HiG enriched moderate levels of complement inhibitors, conforming to a low-inflammatory and pro-fibrotic profile. AP showed the most prominent enrichment of complement activators (e.g., C3, properdin, C-reactive protein) and low levels of inhibitors, conforming to a pro-inflammatory and highly pro-fibrotic profile. In conclusion, the extensive enrichment of inhibitory acute phase proteins on SA could be a determining factor for its reduced host response. The interactions between the plasma proteins and hydrogel surfaces shown herein point to proteomics as an important supplement to existing in vitro and in vivo methods for designing biocompatible alginate-based hydrogels.en_US
dc.description.abstractMS-proteomics provides insight into the host responses towards alginate microspheresen_US
dc.language.isoengen_US
dc.publisherElsevieren_US
dc.relation.urihttps://www.sciencedirect.com/science/article/pii/S2590006422002885?via%3Dihub
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleMS-proteomics provides insight into the host responses towards alginate microspheresen_US
dc.title.alternativeMS-proteomics provides insight into the host responses towards alginate microspheresen_US
dc.typeJournal articleen_US
dc.typePeer revieweden_US
dc.description.versionpublishedVersionen_US
dc.source.journalMaterials Today Bioen_US
dc.identifier.doi10.1016/j.mtbio.2022.100490
dc.identifier.cristin2073148
dc.relation.projectNorges teknisk-naturvitenskapelige universitet: Faculty of Natural Scienceen_US
dc.relation.projectSamarbeidsorganet mellom Helse Midt-Norge og NTNU: 46056819en_US
dc.relation.projectNorges teknisk-naturvitenskapelige universitet: NTNU health "Tailored biomaterials"en_US
dc.relation.projectNorges forskningsråd: 223255en_US
cristin.ispublishedfalse
cristin.fulltextoriginal
cristin.qualitycode1


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