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    Characterization of osteoprotegerin binding to glycosaminoglycans by surface plasmon resonance: role in the interactions with receptor activator of nuclear factor kappaB ligand (RANKL) and RANK.

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    Authors
    Théoleyre, S
    Kwan Tat, S
    Vusio, P
    Blanchard, F
    Gallagher, John T
    Ricard-Blum, S
    Fortun, Y
    Padrines, M
    Rédini, F
    Heymann, D
    Affiliation
    INSERM, ERI 7, Nantes, F-44035, France.
    Issue Date
    2006-08-25
    
    Metadata
    Show full item record
    Abstract
    Osteoprotegerin (OPG) is a decoy receptor for receptor activator of nuclear factor kappaB ligand (RANKL), a key inducer of osteoclastogenesis via its receptor RANK. We previously showed that RANK, RANKL, and OPG are able to form a tertiary complex and that OPG must be also considered as a direct effector of osteoclast functions. As OPG contains a heparin-binding domain, the present study investigated the interactions between OPG and glycosaminoglycans (GAGs) by surface plasmon resonance and their involvement in the OPG functions. Kinetic data demonstrated that OPG binds to heparin with a high-affinity (KD: 0.28 nM) and that the pre-incubation of OPG with heparin inhibits in a dose-dependent manner the OPG binding to the complex RANK-RANKL. GAGs from different structure/origin (heparan sulfate, dermatan sulfate, and chondroitin sulfate) exert similar activity on OPG binding. The contribution of the sulfation pattern and the size of the oligosaccharide were determined in this inhibitory mechanism. The results demonstrated that sulfation is essential in the OPG-blocking function of GAGs since a totally desulfated heparin loses its capacity to bind and to block OPG binding to RANKL. Moreover, a decasaccharide is the minimal structure that totally inhibits the OPG binding to the complex RANK-RANKL. Western blot analysis performed in 293 cells surexpressing RANKL revealed that the pre-incubation of OPG with these GAGs strongly inhibits the OPG-induced decrease of membrane RANKL half-life. These data support an essential function of the related glycosaminoglycans heparin and heparan sulfate in the activity of the triad RANK-RANKL-OPG.
    Citation
    Characterization of osteoprotegerin binding to glycosaminoglycans by surface plasmon resonance: role in the interactions with receptor activator of nuclear factor kappaB ligand (RANKL) and RANK. 2006, 347 (2):460-7 Biochem. Biophys. Res. Commun.
    Journal
    Biochemical and Biophysical Research Communications
    URI
    http://hdl.handle.net/10541/72680
    DOI
    10.1016/j.bbrc.2006.06.120
    PubMed ID
    16828054
    Type
    Article
    Language
    en
    ISSN
    0006-291X
    ae974a485f413a2113503eed53cd6c53
    10.1016/j.bbrc.2006.06.120
    Scopus Count
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