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J Biol Chem, Vol. 273, Issue 32, 20397-20403, August 7, 1998
From the Department of Cell and Molecular Biology, Section of
Connective Tissue Biology, Lund University, S-221 00 Lund, Sweden
Cartilage and tendon extracellular matrices are
composed of collagens, proteoglycans, and a number of noncollagenous
proteins. Cartilage oligomeric matrix protein (COMP) is a prominent
such protein, structurally related to the thrombospondins. We found that native COMP binds to collagen I/II and procollagen I/II and that
the interaction is dependent on the divalent cations
Zn2+ or Ni2+, whereas Ca2+,
Mg2+, and Mn2+ did not promote binding. Using a
solid phase assay, Scatchard analysis identified one class of binding
site with a dissociation constant (Kd) close to 1.5 nM in the presence of Zn2+. The results were
confirmed by studies using surface plasmon resonance. Furthermore,
metal chelate chromatography demonstrated that COMP bound
Zn2+ and Ni2+. Electron microscopy showed that
the interaction occurred at four defined sites on the 300-nm collagen
and procollagen molecules. Two were located close to each end, and two
at 126 and 206 nm, respectively, from the C-terminal. COMP interacted
via its C-terminal globular domain and significantly only in the
presence of Zn2+.
Cartilage Oligomeric Matrix Protein Shows High Affinity
Zinc-dependent Interaction with Triple Helical
Collagen
Copyright © 1998 by The American Society for Biochemistry and Molecular Biology, Inc.
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