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dc.rights.licenseCC BY — Creative Commons Attribution
dc.contributor.authorVorup-Jensen, T.
dc.contributor.authorChi, L.
dc.contributor.authorGjelstrup, L.C.
dc.contributor.authorJensen, U.B.
dc.contributor.authorJewett, C.A.
dc.contributor.authorXie, C.
dc.contributor.authorShimaoka, M.
dc.contributor.authorLinhardt, Robert J.
dc.contributor.authorSpringer, T.A.
dc.identifier.citationBinding Between the Integrin aXß2 (CD11c/CD18) and Heparin, T. Vorup-Jensen, L. Chi, L. C. Gjelstrup, U. B. Jensen, C. A. Jewett, C. Xie, M. Shimaoka, R. J. Linhardt, T. A. Springer, Journal of Biological Chemistry, 282, 30869-30877, 2007.
dc.descriptionJournal of Biological Chemistry, 282, 30869-30877
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.abstractThe interactions between cell surface receptors and sulfated glucosamineglycans serve ubiquitous roles in cell adhesion and receptor signaling. Heparin, a highly sulfated polymer of uronic acids and glucosamine, binds strongly to the integrin receptor alphaXbeta2 (p150,95, CD11c/CD18). Here, we analyze the structural motifs within heparin that constitute high affinity binding sites for the I domain of integrin alphaXbeta2. Heparin oligomers with chain lengths of 10 saccharide residues or higher provide strong inhibition of the binding by the alphaX I domain to the complement fragment iC3b. By contrast, smaller oligomers or the synthetic heparinoid fondaparinux were not able to block the binding. Semipurified heparin oligomers with 12 saccharide residues identified the fully sulfated species as the most potent antagonist of iC3b, with a 1.3 microM affinity for the alphaX I domain. In studies of direct binding by the alphaX I domain to immobilized heparin, we found that the interaction is conformationally regulated and requires Mg2+. Furthermore, the fully sulfated heparin fragment induced conformational change in the ectodomain of the alphaXbeta2 receptor, also demonstrating allosteric linkage between heparin binding and integrin conformation.
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.titleBinding Between the Integrin aXß2 (CD11c/CD18) and Heparinen_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
Except where otherwise noted, this item's license is described as CC BY — Creative Commons Attribution