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dc.contributor.authorZhang, Fuming
dc.contributor.authorMcLellan, Jason S.
dc.contributor.authorAyala, Alondra M.
dc.contributor.authorLeahy, Daniel J.
dc.contributor.authorLinhardt, Robert J.
dc.date2007
dc.date.accessioned2022-06-23T03:58:48Z
dc.date.available2022-06-23T03:58:48Z
dc.date.issued2007-04-03
dc.identifier.citationKinetic and Structural Studies on Interactions between Heparin/Heparan Sulfate and Proteins of the Hedgehog Signaling Pathway, F. Zhang, J. S. McLellan, A. M. A. Jiménez, D. J. Leahy, R. J. Linhardt, Biochemistry, 46, 3933-3941, 2007.
dc.identifier.issn62960
dc.identifier.urihttps://hdl.handle.net/20.500.13015/5205
dc.identifier.urihttps://doi.org/10.1021/bi6025424
dc.descriptionBiochemistry, 46, 3933-3941
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.abstractHeparan sulfate (HS) proteoglycans (PGs) interact with a number of extracellular signaling proteins, thereby playing an essential role in the regulation of many physiological processes. These interactions are important for both normal signal transduction and regulation of the tissue distribution of signaling molecules. In this study, we use surface plasmon resonance (SPR) to study interactions of HS and structurally related heparin with proteins in the Hedgehog signaling pathway. SPR analysis shows that heparin binds with different affinities to active fragments of the proteins Hedgehog (Hh), Interference Hedgehog (Ihog), Cam-related/Down-regulated by Oncogenes (CDO), and Sonic Hedgehog (Shh). Solution competition studies show that the minimum size of a heparin oligosaccharide capable of interacting with Ihog is larger than a tetrasaccharide and for interacting with Shh is larger than an octasaccharide. In comparison with heparin, Ihog and Shh exhibited a lower affinity for HS than for heparin, and CDO and Hh exhibit negligible binding to HS. This study clearly demonstrates Shh and Ihog are heparin and HS binding proteins and that both molecules preferentially bind heparin or HS having a high level of sulfation.
dc.description.sponsorshipNational Heart, Lung, and Blood Institute
dc.languageen_US
dc.language.isoENG
dc.publisherAmerican Chemical Society (ACS)
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.titleKinetic and Structural Studies on Interactions between Heparin/Heparan Sulfate and Proteins of the Hedgehog Signaling Pathway
dc.typeArticle
dcterms.accessRightsA full text version is available in DSpace@RPI
dcterms.isPartOfJournal
dcterms.isVersionOfhttps://doi.org/10.1021/bi6025424
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.pages3933-3941
rpi.description.volume46


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