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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)
Please use this url to cite or link to this publication:
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
2025-04-04 15:28:17
@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}},
}