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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
and
organization
publishing date
type
Contribution to journal
publication status
published
subject
in
Journal of Biological Chemistry
volume
284
issue
1
pages
534 - 539
publisher
American Society for Biochemistry and Molecular Biology
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
2016-04-01 12:27:16
date last changed
2022-03-13 18:05:55
@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    = {{American Society for Biochemistry and Molecular Biology}},
  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}},
  doi          = {{10.1074/jbc.M805721200}},
  volume       = {{284}},
  year         = {{2009}},
}