Background: Collagen cross-linking mechanisms must be regulated to obtain tissue-specific collagen fiber properties. Results: Deficiency in collagen-associated protein fibromodulin leads to excessively cross-linked specific domain of collagen. Conclusion: Fibromodulin modulates site-specific cross-linking of collagen. Significance: This is the first report showing that a collagen-associated protein can modulate cross-linking of specific collagen domains. © 2014 by The American Society for Biochemistry and Molecular Biology, Inc.
CITATION STYLE
Kalamajski, S., Liu, C., Tillgren, V., Rubin, K., Oldberg, Å., Rai, J., … Eyre, D. R. (2014). Increased c-telopeptide cross-linking of tendon type i collagen in fibromodulin-deficient mice. Journal of Biological Chemistry, 289(27), 18873–18879. https://doi.org/10.1074/jbc.M114.572941
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