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.
ASJC Scopus subject areas
Dugan, T. A., Yang, V. W. C., McQuillan, D. J., & Höök, M. (2003). Decorin binds fibrinogen in a Zn2+-dependent interaction. Journal of Biological Chemistry, 278(16), 13655-13662. https://doi.org/10.1074/jbc.M300171200