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Sebastian Kalamajski

Assistant researcher

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

Author

  • Sebastian Kalamajski
  • Åke Oldberg

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

Document type

Journal article

Publisher

ASBMB

Topic

  • Cell and Molecular Biology

Status

Published

Research group

  • Åke Oldberg´s group

ISBN/ISSN/Other

  • ISSN: 1083-351X