Taipei Medical University

A B C D E F G H I J K L M N O P Q R S T U V W X Y Z
Dugan TA
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------>journal_name=Journal of Biological Chemistry
------>paper_name=Decorin Binds Fibrinogen in a Zn2+-dependent interaction
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------>fullAbstract=We have previously shown that decorin, a member of the small leucine-rich proteoglycan family of extracellular matrix proteoglycans/glycoproteins is a Zn(2+) metalloprotein at physiological Zn(2+) concentrations (Yang, V. W-C., LaBrenz, S. R., Rosenberg, L. C., McQuillan, D., and Hook, M. (1999) J. Biol. Chem. 274, 12454-12460). We now report that the decorin proteoglycan binds fibrinogen in the presence of Zn(2+). 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 K(D) of 1.7 x 10(-6) m, as determined from fluorescence polarization data. Furthermore, we show that Zn(2+) 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 Zn(2+)-dependent manner. Thus, Zn(2+) appears to play a pivotal role in the interactions and biological function of decorin.
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------>authors2=Yang WCV
------>authors3=McQuillan JD
------>authors4=Höök M
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------>authors=Dugan TA
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------>updateTitle=Decorin binds fibrinogen in a Zn2+-dependent interaction.
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------>no=16
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------>publish_year=2003
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A B C D E F G H I J K L M N O P Q R S T U V W X Y Z