Homologous sequence in lumican and fibromodulin leucine-rich repeat 5-7 competes for collagen binding.
J Biol Chem
; 284(1): 534-539, 2009 Jan 02.
Article
em En
| MEDLINE
| ID: mdl-19008226
ABSTRACT
Lumican and fibromodulin compete for collagen type I binding in vitro, and fibromodulin-deficient mice have 4-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 leucine-rich repeat (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 D213N mutation, lowers the melting point and affects the packing of collagen fibrils.
Texto completo:
1
Coleções:
01-internacional
Base de dados:
MEDLINE
Assunto principal:
Peptídeos
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Proteoglicanas de Sulfatos de Condroitina
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Proteoglicanas
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Proteínas da Matriz Extracelular
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Colágeno Tipo I
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Sulfato de Queratano
Limite:
Animals
/
Humans
Idioma:
En
Revista:
J Biol Chem
Ano de publicação:
2009
Tipo de documento:
Article