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    Oversulfated chondroitin sulfate interaction with heparin-binding proteins: New insights into adverse reactions from contaminated heparins

    Author
    Li, Boyangzi; Suwan, Jiraporn; Martin, Jeffrey G.; Zhang, Fuming; Zhang, Zhenqing; Hoppensteadt, Debra; Clark, Melanie; Fareed, Jawed; Linhardt, Robert J.
    ORCID
    https://orcid.org/0000-0003-2219-5833
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    OVERSULFATED CHONDROITIN SULFATE INTERACTION WITH HEPARIN BINDING.pdf (1.421Mb)
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    Date Issued
    2009-08-01
    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
    Oversulfated chondroitin sulfate interaction with heparin-binding proteins: New insights into adverse reactions from contaminated heparins, B. Li, J.Suwan, J.G. Martin, F. Zhang, Z. Zhang, D. Hoppensteadt, M. Clark, J. Fareed, R.J. Linhardt, Biochemical Pharmacology, 78, 292–300, 2009.
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    URI
    https://hdl.handle.net/20.500.13015/5146; https://doi.org/10.1016/j.bcp.2009.04.012
    Abstract
    An oversulfated chondroitin sulfate (OSCS) was identified as a contaminant to pharmaceutical heparin and severe anaphylactoid reactions were ascribed to this contaminant. An examination of the biochemistry underlying both the anticoagulant activity and the toxic effects of oversulfated chondroitin sulfate was undertaken. This study demonstrates that the anticoagulant activity of this oversulfated chondroitin sulfate is primarily dependent on heparin cofactor II mediated inhibition of thrombin. Heparin and oversulfated chondroitin sulfate binding to coagulation, kinin-kallikrein and complement proteins were studied by surface plasmon resonance. While oversulfated chondroitin sulfate binds tightly to antithrombin III, unlike heparin, OSCS does not induce antithrombin III to undergo the conformational change required for its inactivation of thrombin and factor Xa. In contrast to heparin, oversulfated chondroitin sulfate tightly binds factor XIIa suggesting a biochemical mechanism for the factor XIIa-based enhancement of vasoactive bradykinin production.;
    Description
    Biochemical Pharmacology, 78, 292–300; 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; Biochemical Pharmacology; https://harc.rpi.edu/;
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    A full text version is available in DSpace@RPI;
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