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dc.contributor.authorZhang, Fuming
dc.contributor.authorLiang, Xinle
dc.contributor.authorPu, Dennis
dc.contributor.authorGeorge, Kasim I.
dc.contributor.authorHolland, Paul J.
dc.contributor.authorWalsh, Scott T.R.
dc.contributor.authorLinhardt, Robert J.
dc.date2012
dc.date.accessioned2022-06-23T04:11:25Z
dc.date.available2022-06-23T04:11:25Z
dc.date.issued2012-01-01
dc.identifier.citationBiophysical characterization of glycosaminoglycan-IL-7 interactions using SPR, F. Zhang, X. Liang, D. Pu, K. I. George, P. J. Holland, S. T. Walsh, R. J Linhardt, Biochemie, 94, 242-249, 2012.
dc.identifier.issn61831638
dc.identifier.issn3009084
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5272
dc.identifier.urihttps://doi.org/10.1016/j.biochi.2011.10.015
dc.descriptionBiochemie, 94, 242-249
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.abstractGlycosaminoglycans (GAGs) interact with a number of cytokines and growth factors thereby playing an essential role in the regulation of many physiological processes. These interactions are important for both normal signal transduction and the regulation of the tissue distribution of cytokines/growth factors. In the present study, we employed surface plasmon resonance (SPR) spectroscopy to dissect the binding interactions between GAGs and murine and human forms of interleukin-7 (IL-7). SPR results revealed that heparin binds with higher affinity to human IL-7 than murine IL-7 through a different kinetic mechanism. The optimal oligosaccharide length of heparin for the interactions to human and murine IL-7 involves a sequence larger than a tetrasaccharide. These results further demonstrate that while IL-7 is principally a heparin/heparan sulfate binding protein, it also interacts with dermatan sulfate, chondroitin sulfates C, D, and E, indicating that this cytokine preferentially interacts with GAGs having a higher degree of sulfation.
dc.description.sponsorshipNational Institutes of Health
dc.languageen_US
dc.language.isoENG
dc.publisherElsevier
dc.relation.ispartofThe Linhardt Research Labs Online Collection
dc.relation.ispartofRensselaer Polytechnic Institute, Troy, NY
dc.relation.ispartofBiochimie
dc.relation.urihttps://harc.rpi.edu/
dc.subjectBiology
dc.subjectChemistry and chemical biology
dc.subjectChemical and biological engineering
dc.subjectBiomedical engineering
dc.titleBiophysical characterization of glycosaminoglycan-IL-7 interactions using SPR
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1016/j.biochi.2011.10.015
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.pages242-249
rpi.description.volume94


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