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COMP acts as a catalyst in collagen fibrillogenesis

Halasz, Krisztina LU ; Kassner, Anja LU ; Mörgelin, Matthias LU and Heinegård, Dick LU (2007) In Journal of Biological Chemistry 282(43). p.31166-31173
Abstract
We have previously reported that COMP (cartilage oligomeric matrix protein) is prominent in cartilage but is also present in tendon and binds to collagens I and II with high affinity. Here we show that COMP influences the fibril formation of these collagens. Fibril formation in the presence of pentameric COMP was much faster, and the amount of collagen in fibrillar form was markedly increased. Monomeric COMP, lacking the N-terminal coiled-coil linker domain, decelerated fibrillogenesis. The data show that stimulation of collagen fibrillogenesis depends on the pentameric nature of COMP and not only on collagen binding. COMP interacts primarily with free collagen I and II molecules, bringing several molecules to close proximity, apparently... (More)
We have previously reported that COMP (cartilage oligomeric matrix protein) is prominent in cartilage but is also present in tendon and binds to collagens I and II with high affinity. Here we show that COMP influences the fibril formation of these collagens. Fibril formation in the presence of pentameric COMP was much faster, and the amount of collagen in fibrillar form was markedly increased. Monomeric COMP, lacking the N-terminal coiled-coil linker domain, decelerated fibrillogenesis. The data show that stimulation of collagen fibrillogenesis depends on the pentameric nature of COMP and not only on collagen binding. COMP interacts primarily with free collagen I and II molecules, bringing several molecules to close proximity, apparently promoting further assembly. These assemblies further join in discrete steps to a narrow distribution of completed fibril diameters of 149 +/- 16 nm with a banding pattern of 67 nm. COMP is not found associated with the mature fibril and dissociates from the collagen molecules or their early assemblies. However, a few COMP molecules are found bound to more loosely associated molecules at the tip/end of the growing fibril. Thus, COMP appears to catalyze the fibril formation by promoting early association of collagen molecules leading to increased rate of fibrillogenesis and more distinct organization of the fibrils. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
282
issue
43
pages
31166 - 31173
publisher
ASBMB
external identifiers
  • pmid:17716974
  • wos:000250309200006
  • scopus:35748950738
ISSN
1083-351X
DOI
10.1074/jbc.M705735200
language
English
LU publication?
yes
id
a93e384b-b5ed-4d17-ae5f-cdbdb653f9d3 (old id 1141748)
alternative location
http://www.ncbi.nlm.nih.gov/entrez/query.fcgi?cmd=Retrieve&db=PubMed&list_uids=17716974&dopt=Abstract
date added to LUP
2008-08-11 13:54:47
date last changed
2017-10-22 04:52:45
@article{a93e384b-b5ed-4d17-ae5f-cdbdb653f9d3,
  abstract     = {We have previously reported that COMP (cartilage oligomeric matrix protein) is prominent in cartilage but is also present in tendon and binds to collagens I and II with high affinity. Here we show that COMP influences the fibril formation of these collagens. Fibril formation in the presence of pentameric COMP was much faster, and the amount of collagen in fibrillar form was markedly increased. Monomeric COMP, lacking the N-terminal coiled-coil linker domain, decelerated fibrillogenesis. The data show that stimulation of collagen fibrillogenesis depends on the pentameric nature of COMP and not only on collagen binding. COMP interacts primarily with free collagen I and II molecules, bringing several molecules to close proximity, apparently promoting further assembly. These assemblies further join in discrete steps to a narrow distribution of completed fibril diameters of 149 +/- 16 nm with a banding pattern of 67 nm. COMP is not found associated with the mature fibril and dissociates from the collagen molecules or their early assemblies. However, a few COMP molecules are found bound to more loosely associated molecules at the tip/end of the growing fibril. Thus, COMP appears to catalyze the fibril formation by promoting early association of collagen molecules leading to increased rate of fibrillogenesis and more distinct organization of the fibrils.},
  author       = {Halasz, Krisztina and Kassner, Anja and Mörgelin, Matthias and Heinegård, Dick},
  issn         = {1083-351X},
  language     = {eng},
  number       = {43},
  pages        = {31166--31173},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {COMP acts as a catalyst in collagen fibrillogenesis},
  url          = {http://dx.doi.org/10.1074/jbc.M705735200},
  volume       = {282},
  year         = {2007},
}