TY - JOUR
T1 - Decorin binds fibrinogen in a Zn2+-dependent interaction
AU - Dugan, Tracey A.
AU - Yang, Vivian W C
AU - McQuillan, David J.
AU - Höök, Magnus
PY - 2003/4/18
Y1 - 2003/4/18
N2 - 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.
AB - 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.
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U2 - 10.1074/jbc.M300171200
DO - 10.1074/jbc.M300171200
M3 - Article
C2 - 12582160
AN - SCOPUS:0037853148
SN - 0021-9258
VL - 278
SP - 13655
EP - 13662
JO - Journal of Biological Chemistry
JF - Journal of Biological Chemistry
IS - 16
ER -