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dc.contributor.authorHadjialirezaei, Soosan
dc.contributor.authorPicco, Gianfranco
dc.contributor.authorBeatson, Richard
dc.contributor.authorBurchell, Joy
dc.contributor.authorStokke, Bjørn Torger
dc.contributor.authorSletmoen, Marit
dc.date.accessioned2017-10-26T07:22:18Z
dc.date.available2017-10-26T07:22:18Z
dc.date.created2017-10-09T13:25:33Z
dc.date.issued2017
dc.identifier.issn1932-6203
dc.identifier.urihttp://hdl.handle.net/11250/2462240
dc.description.abstractCarbohydrate–protein interactions govern many crucial processes in biological systems including cell recognition events. We have used the sensitive force probe optical tweezers to quantify the interactions occurring between MGL lectins and MUC1 carrying the cancer-associated glycan antigens mucins Tn and STn. Unbinding forces of 7.6±1.1 pN and 7.1±1.1 pN were determined for the MUC1(Tn)—MGL and MUC1(STn)—MGL interactions, at a force loading rate of ~40 pN/s. The interaction strength increased with increasing force loading rate, to 27.1±4.4 and 36.9±3.6 pN at a force loading rate of ~ 310 pN/s. No interactions were detected between MGL and MUC1(ST), a glycoform of MUC1 also expressed by breast carcinoma cells. Interestingly, this glycan (ST) can be found on proteins expressed by normal cells, although in this case not on MUC1. Additionally, GalNAc decorated polyethylene glycol displayed similar rupture forces as observed for MUC1(Tn) and MUC1(STn) when forced to unbind from MGL, indicating that GalNAc is an essential group in these interactions. Since the STn glycan decoration is more frequently found on the surface of carcinomas than the Tn glycan, the binding of MUC1 carrying STn to MGL may be more physiologically relevant and may be in part responsible for some of the characteristics of STn expressing tumours.nb_NO
dc.language.isoengnb_NO
dc.publisherPublic Library of Sciencenb_NO
dc.rightsNavngivelse 4.0 Internasjonal*
dc.rights.urihttp://creativecommons.org/licenses/by/4.0/deed.no*
dc.titleInteractions between the breast cancer-associated MUC1 mucins and C-type lectin characterized by optical tweezersnb_NO
dc.typeJournal articlenb_NO
dc.typePeer reviewednb_NO
dc.description.versionpublishedVersionnb_NO
dc.source.journalPLoS ONEnb_NO
dc.identifier.doi10.1371/journal.pone.0175323
dc.identifier.cristin1503374
dc.description.localcode© 2017 Hadjialirezaei et al. This is an open access article distributed under the terms of the Creative Commons Attribution License, which permits unrestricted use, distribution, and reproduction in any medium, provided the original author and source are credited.nb_NO
cristin.unitcode194,66,20,0
cristin.unitcode194,66,15,0
cristin.unitnameInstitutt for fysikk
cristin.unitnameInstitutt for bioteknologi og matvitenskap
cristin.ispublishedtrue
cristin.fulltextoriginal
cristin.qualitycode1


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