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Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen

Rosenberg, Krisztina; Olsson, Henric; Mörgelin, Matthias LU and Heinegård, Dick LU (1998) In Journal of Biological Chemistry 273(32). p.20397-20403
Abstract
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+... (More)
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+. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
273
issue
32
pages
20397 - 20403
publisher
ASBMB
external identifiers
  • pmid:9685393
  • scopus:0032493665
ISSN
1083-351X
language
English
LU publication?
yes
id
452333b5-b9a0-4747-8227-d750188a6551 (old id 1113499)
alternative location
http://www.jbc.org/cgi/content/full/273/32/20397
date added to LUP
2008-07-15 11:11:17
date last changed
2017-07-02 03:29:42
@article{452333b5-b9a0-4747-8227-d750188a6551,
  abstract     = {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+.},
  author       = {Rosenberg, Krisztina and Olsson, Henric and Mörgelin, Matthias and Heinegård, Dick},
  issn         = {1083-351X},
  language     = {eng},
  number       = {32},
  pages        = {20397--20403},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen},
  volume       = {273},
  year         = {1998},
}