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Homologous sequence in lumican and fibromodulin LRR 5-7 competes for collagen binding.

Kalamajski, Sebastian LU and Oldberg, Åke LU (2009) In Journal of Biological Chemistry 284(1). p.534-539
Abstract
Lumican and fibromodulin compete for collagen type I binding in vitro and fibromodulin-deficient mice have four-fold more lumican in tendons. These observations indicate that homologous sequences in lumican and fibromodulin bind to collagen type I. Here, we demonstrate that lumican binding to collagen type I is mediated mainly by Asp-213 in LRR 7. The mutation D213N in lumican impairs interaction with collagen, and the lumican fragment spanning LRRs 5-7 is an efficient inhibitor of collagen binding. Also, the lumican LRR 7 sequence-based synthetic peptide CYLDNNKC inhibits the binding to collagen. Homologous collagen-binding site in fibromodulin, located in LRRs 5-7, inhibits the binding of lumican to collagen, and the mutation E251Q in... (More)
Lumican and fibromodulin compete for collagen type I binding in vitro and fibromodulin-deficient mice have four-fold more lumican in tendons. These observations indicate that homologous sequences in lumican and fibromodulin bind to collagen type I. Here, we demonstrate that lumican binding to collagen type I is mediated mainly by Asp-213 in LRR 7. The mutation D213N in lumican impairs interaction with collagen, and the lumican fragment spanning LRRs 5-7 is an efficient inhibitor of collagen binding. Also, the lumican LRR 7 sequence-based synthetic peptide CYLDNNKC inhibits the binding to collagen. Homologous collagen-binding site in fibromodulin, located in LRRs 5-7, inhibits the binding of lumican to collagen, and the mutation E251Q in this fibromodulin fragment does not inhibit the lumican-collagen binding. Lumican, but not the the D213N mutation, lowers the melting point and affects the packing of collagen fibrils. (Less)
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author
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
284
issue
1
pages
534 - 539
publisher
ASBMB
external identifiers
  • wos:000261974800058
  • pmid:19008226
  • scopus:58649096818
ISSN
1083-351X
DOI
10.1074/jbc.M805721200
language
English
LU publication?
yes
id
62cce95b-d3de-4ac8-8a43-664663e13879 (old id 1271470)
alternative location
http://www.ncbi.nlm.nih.gov/pubmed/19008226?dopt=Abstract
date added to LUP
2008-12-04 15:37:27
date last changed
2017-10-22 03:53:40
@article{62cce95b-d3de-4ac8-8a43-664663e13879,
  abstract     = {Lumican and fibromodulin compete for collagen type I binding in vitro and fibromodulin-deficient mice have four-fold more lumican in tendons. These observations indicate that homologous sequences in lumican and fibromodulin bind to collagen type I. Here, we demonstrate that lumican binding to collagen type I is mediated mainly by Asp-213 in LRR 7. The mutation D213N in lumican impairs interaction with collagen, and the lumican fragment spanning LRRs 5-7 is an efficient inhibitor of collagen binding. Also, the lumican LRR 7 sequence-based synthetic peptide CYLDNNKC inhibits the binding to collagen. Homologous collagen-binding site in fibromodulin, located in LRRs 5-7, inhibits the binding of lumican to collagen, and the mutation E251Q in this fibromodulin fragment does not inhibit the lumican-collagen binding. Lumican, but not the the D213N mutation, lowers the melting point and affects the packing of collagen fibrils.},
  author       = {Kalamajski, Sebastian and Oldberg, Åke},
  issn         = {1083-351X},
  language     = {eng},
  number       = {1},
  pages        = {534--539},
  publisher    = {ASBMB},
  series       = {Journal of Biological Chemistry},
  title        = {Homologous sequence in lumican and fibromodulin LRR 5-7 competes for collagen binding.},
  url          = {http://dx.doi.org/10.1074/jbc.M805721200},
  volume       = {284},
  year         = {2009},
}