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dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorSterner, E.
dc.contributor.authorMasuko, S.
dc.contributor.authorLi, G.
dc.contributor.authorLi, L.
dc.contributor.authorGreen, D.E.
dc.contributor.authorOtto, N.J.
dc.contributor.authorXu, Y.
dc.contributor.authorDeAngelis, P.L.
dc.contributor.authorLiu, J.
dc.contributor.authorDordick, J.S.
dc.contributor.authorLinhardt, Robert J.
dc.identifier.citationFibroblast growth factor-based signaling through synthetic heparan sulfate block copolymers studied using high-cell density 3D cell printing, E. Sterner, S. Masuko, G. Li, L. Li, D. E. Green, N. J. Otto, Y. Xu, P. L. DeAngelis, J. Liu, J. S. Dordick, R. J. Linhardt, Journal of Biological Chemistry, 289, 9754–9765, 2014.
dc.descriptionJournal of Biological Chemistry, 289, 9754–9765
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.abstractFour well-defined heparan sulfate (HS) block copolymers containing S-domains (high sulfo group content) placed adjacent to N-domains (low sulfo group content) were chemoenzymatically synthesized and characterized. The domain lengths in these HS block co-polymers were ~40 saccharide units. Microtiter 96-well and three-dimensional cell-based microarray assays utilizing murine immortalized bone marrow (BaF3) cells were developed to evaluate the activity of these HS block co-polymers. Each recombinant BaF3 cell line expresses only a single type of fibroblast growth factor receptor (FGFR) but produces neither HS nor fibroblast growth factors (FGFs). In the presence of different FGFs, BaF3 cell proliferation showed clear differences for the four HS block co-polymers examined. These data were used to examine the two proposed signaling models, the symmetric FGF2-HS2-FGFR2 ternary complex model and the asymmetric FGF2-HS1-FGFR2 ternary complex model. In the symmetric FGF2-HS2-FGFR2 model, two acidic HS chains bind in a basic canyon located on the top face of the FGF2-FGFR2 protein complex. In this model the S-domains at the non-reducing ends of the two HS proteoglycan chains are proposed to interact with the FGF2-FGFR2 protein complex. In contrast, in the asymmetric FGF2-HS1-FGFR2 model, a single HS chain interacts with the FGF2-FGFR2 protein complex through a single S-domain that can be located at any position within an HS chain. Our data comparing a series of synthetically prepared HS block copolymers support a preference for the symmetric FGF2-HS2-FGFR2 ternary complex model.
dc.publisherThe American Society for Biochemistry and Molecular Biology (ASBMB) and Elsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.rightsAttribution 3.0 United States*
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleFibroblast growth factor-based signaling through synthetic heparan sulfate block copolymers studied using high-cell density 3D cell printingen_US
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.accessRightsOpen Access
dc.rights.holderCC BY : this license allows reusers to distribute, remix, adapt, and build upon the material in any medium or format, so long as attribution is given to the creator. The license allows for commercial use. Credit must be given to the authors and the original work must be properly cited.
dc.relation.departmentThe Linhardt Research Labs.
dc.relation.departmentThe Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS)

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CC BY — Creative Commons Attribution
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