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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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; ; and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
273
issue
32
pages
20397 - 20403
publisher
American Society for Biochemistry and Molecular Biology
external identifiers
  • pmid:9685393
  • scopus:0032493665
ISSN
1083-351X
language
English
LU publication?
yes
additional info
The information about affiliations in this record was updated in December 2015. The record was previously connected to the following departments: Division of Infection Medicine (BMC) (013024020), Connective Tissue Biology (013230151)
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
2016-04-01 11:41:45
date last changed
2025-10-14 12:47:14
@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    = {{American Society for Biochemistry and Molecular Biology}},
  series       = {{Journal of Biological Chemistry}},
  title        = {{Cartilage oligomeric matrix protein shows high affinity zinc-dependent interaction with triple helical collagen}},
  url          = {{http://www.jbc.org/cgi/content/full/273/32/20397}},
  volume       = {{273}},
  year         = {{1998}},
}