Homologous sequence in lumican and fibromodulin LRR 5-7 competes for collagen binding.
Author
Summary, in English
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.
Department/s
- Åke Oldberg´s group
Publishing year
2009
Language
English
Pages
534-539
Publication/Series
Journal of Biological Chemistry
Volume
284
Issue
1
Links
Document type
Journal article
Publisher
American Society for Biochemistry and Molecular Biology
Topic
- Cell and Molecular Biology
Status
Published
Research group
- Åke Oldberg´s group
ISBN/ISSN/Other
- ISSN: 1083-351X