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dc.contributor.authorZhang, Fuming
dc.contributor.authorZhao, Jing
dc.contributor.authorLiu, Xinyue
dc.contributor.authorLinhardt, Robert J.
dc.date2020
dc.date.accessioned2022-06-27T15:42:23Z
dc.date.available2022-06-27T15:42:23Z
dc.date.issued2020-02-01
dc.identifier.citationInteractions between sclerostin and glycosaminoglycans, F. Zhang, J. Zhao, X. Liu, R. J. Linhardt, Glycoconjugate Journal, 37, 119–128, 2020.
dc.identifier.issn15734986
dc.identifier.issn2820080
dc.identifier.urihttps://doi.org/10.1007/s10719-019-09900-3
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5516
dc.descriptionGlycoconjugate Journal, 37, 119–128
dc.descriptionNote : if this item contains full text it may be a preprint, author manuscript, or a Gold OA copy that permits redistribution with a license such as CC BY. The final version is available through the publisher’s platform.
dc.description.abstractSclerostin (SOST) is a glycoprotein having many important functions in the regulation of bone formation as a key negative regulator of Wnt signaling in bone. Surface plasmon resonance (SPR), which allows for a direct quantitative analysis of the label-free molecular interactions in real-time, has been widely used for the biophysical characterization of glycosaminoglycan (GAG)-protein interactions. In the present study, we report kinetics, structural analysis and the effects of physiological conditions (e.g., salt concentrations, Ca2+ and Zn2+concentrations) on the interactions between GAGs and recombinant human (rh) and recombinant mouse (rm) SOST using SPR. SPR results revealed that both SOSTs bind heparin with high affinity (rhSOST-heparin, KD~36 nM and rmSOST-heparin, KD~77 nM) and the shortest oligosaccharide of heparin that effectively competes with full size heparin for SOST binding is octadecasaccharide (18mer). This heparin binding protein also interacts with other highly sulfated GAGs including, disulfated-dermatan sulfate and chondroitin sulfate E. In addition, liquid chromatography-mass spectrometry was used to characterize the structure of sulfated GAGs that bound to SOST.
dc.description.sponsorshipNational Institutes of Health
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s10719-019-09900-3
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofGlycoconjugate Journal
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleInteractions between sclerostin and glycosaminoglycans
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1007/s10719-019-09900-3
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1007/s10719-019-09900-3
dc.rights.holderIn Copyright : this Item is protected by copyright and/or related rights. You are free to use this Item in any way that is permitted by the copyright and related rights legislation that applies to your use. For other uses you need to obtain permission from the rights-holder(s). https://rightsstatements.org/page/InC/1.0/
dc.creator.identifierhttps://orcid.org/0000-0003-2219-5833
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)
rpi.description.pages119-128
rpi.description.volume37


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