Decorin binds fibrinogen in a Zn2+-dependent interaction

Tracey A. Dugan, Vivian W.C. Yang, David J. McQuillan, Magnus Höök

    Research output: Contribution to journalArticlepeer-review

    33 Scopus citations

    Abstract

    We have previously shown that decorin, a member of the small leucine-rich proteoglycan family of extracellular matrix proteoglycans/glycoproteins is a Zn2+ metalloprotein at physiological Zn2+ concentrations (Yang, V. W-C., LaBrenz, S. R., Rosenberg, L. C., McQuillan, D., and Höök, M. (1999) J. Biol. Chem. 274, 12454-12460). We now report that the decorin proteoglycan binds fibrinogen in the presence of Zn2+. The fibrinogen-binding site is located in the N-terminal domain of the decorin core protein and a 45-amino acid peptide representing this domain binds to the fibrinogen D fragment with an apparent KD of 1.7 × 10-6 M, as determined from fluorescence polarization data. Furthermore, we show that Zn2+ promotes the self-association of decorin. The N-terminal domain of the core protein also mediates this activity. The results of solid-phase binding assays and gel filtration chromatography suggest that the N-terminal domain of decorin, when present at low micromolar concentrations, forms an oligomer in a Zn2+-dependent manner. Thus, Zn2+ appears to play a pivotal role in the interactions and biological function of decorin.

    Original languageEnglish (US)
    Pages (from-to)13655-13662
    Number of pages8
    JournalJournal of Biological Chemistry
    Volume278
    Issue number16
    DOIs
    StatePublished - Apr 18 2003

    ASJC Scopus subject areas

    • Biochemistry
    • Molecular Biology
    • Cell Biology

    Fingerprint

    Dive into the research topics of 'Decorin binds fibrinogen in a Zn2+-dependent interaction'. Together they form a unique fingerprint.

    Cite this