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    Characterization of the interaction between Robo1 and heparin/glycosaminoglycans

    Author
    Zhang, Fuming; Moniz, Heather A.; Walcott, Benjamin; Moremen, Kelley W.; Linhardt, Robert J.; Wang, Lianchun
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    CHARACTERIZATION OF THE INTERACTION BETWEEN ROBO1 AND HEPARIN.pdf (830.6Kb)
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    Date Issued
    2013-12-01
    Subject
    Biology; Chemistry and chemical biology; Chemical and biological engineering; Biomedical engineering
    Degree
    Terms of Use
    In 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/;
    Full Citation
    Characterization of the interaction between Robo1 and heparin/glycosaminoglycans, F. Zhang, H. A. Moniz, B. Walcott, K. W. Moremen, R. J. Linhardt, L. Wang, Biochemie, 95, 2345-2353, 2013.
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    URI
    https://hdl.handle.net/20.500.13015/5334; https://doi.org/10.1016/j.biochi.2013.08.018
    Abstract
    Roundabout 1 (Robo1) is the cognate receptor for secreted axon guidance molecule, Slits, which function to direct cellular migration during neuronal development and angiogenesis. The Slit2–Robo1 signaling is modulated by heparan sulfate, a sulfated linear polysaccharide that is abundantly expressed on the cell surface and in the extracellular matrix. Biochemical studies have further shown that heparan sulfate binds to both Slit2 and Robo1 facilitating the ligand–receptor interaction. The structural requirements for heparan sulfate interaction with Robo1 remain unknown. In this report, surface plasmon resonance (SPR) spectroscopy was used to examine the interaction between Robo1 and heparin and other GAGs and determined that heparin binds to Robo1 with an affinity of ∼650 nM. SPR solution competition studies with chemically modified heparins further determined that although all sulfo groups on heparin are important for the Robo1–heparin interaction, the N-sulfo and 6-O-sulfo groups are essential for the Robo1–heparin binding. Examination of differently sized heparin oligosaccharides and different GAGs also demonstrated that Robo1 prefers to bind full-length heparin chains and that GAGs with higher sulfation levels show increased Robo1 binding affinities.;
    Description
    Biochemie, 95, 2345-2353; Note : 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.
    Department
    The Linhardt Research Labs.; The Shirley Ann Jackson, Ph.D. Center for Biotechnology and Interdisciplinary Studies (CBIS);
    Publisher
    Elsevier
    Relationships
    The Linhardt Research Labs Online Collection; Rensselaer Polytechnic Institute, Troy, NY; Biochimie; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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