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

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    Sammanfattning

    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.
    Originalspråkengelska
    Sidor (från-till)534-539
    TidskriftJournal of Biological Chemistry
    Volym284
    Utgåva1
    DOI
    StatusPublished - 2009

    Ämnesklassifikation (UKÄ)

    • Cell- och molekylärbiologi

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