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dc.contributor.authorSterner, Eric
dc.contributor.authorMeli, Luciana
dc.contributor.authorKwon, Seok Joon
dc.contributor.authorDordick, Jonathan S.
dc.contributor.authorLinhardt, Robert J.
dc.date2013
dc.date.accessioned2022-06-27T16:06:07Z
dc.date.available2022-06-27T16:06:07Z
dc.date.issued2013-12-17
dc.identifier.citationFGF-FGFR signaling mediated through glycosaminoglycans in microtiter plate and cell-based microarray platforms, E. Sterner, L. Meli, J. S. Dordick, R. J. Linhardt, Biochemistry, 52, 9009−9019, 2013.
dc.identifier.issn15204995
dc.identifier.issn62960
dc.identifier.urihttps://doi.org/10.1021/bi401284r
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5700
dc.descriptionBiochemistry, 52, 9009−9019
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.abstractFibroblast growth factor (FGF) signals cell growth through its interaction with a fibroblast growth factor receptor (FGFR) and a glycosaminoglycn (GAG) coreceptor. Here, we examine the signaling of five different FGFs (1, 2, 6, 8, and 8b) through FGFR3c. A small library of GAG and GAG-derivative coreceptors are screened to understand better the structure–activity relationship of these coreceptors on signaling. Initially, data were collected in a microtiter plate well-based cell proliferation assay. In an effort to reduce reagent requirements and improve assay throughput, a cell-based microarray platform was developed. In this cell-based microarray, FGFR3c-expressing cells were printed in alginate hydrogel droplets of ∼30 nL and incubated with FGF and GAG. Heparin was the most effective GAG coreceptor for all FGFs studied. Other GAGs, such as 2-O-desulfated heparin and chondroitin sulfate B, were also effective coreceptors. Signaling by FGF 8 and FGF 8b showed the widest tolerance for coreceptor structure. Finally, this on-chip cell-based microarray provides comparable data to a microtiter plate well-based assay, demonstrating that the coreceptor assay can be converted into a high-throughput assay.
dc.description.urihttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/bi401284r
dc.languageen_US
dc.language.isoENG
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochemistry
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleFGF-FGFR signaling mediated through glycosaminoglycans in microtiter plate and cell-based microarray platforms
dc.typeArticle
dcterms.accessRightshttps://login.libproxy.rpi.edu/login?url=https://doi.org/10.1021/bi401284r
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/bi401284r
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.pages9009-9019
rpi.description.volume52


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