Interactions of the extracellular matrix proteoglycans decorin and biglycan with C1q and collectins.

@article{Groeneveld2005InteractionsOT,
  title={Interactions of the extracellular matrix proteoglycans decorin and biglycan with C1q and collectins.},
  author={Tom W. L. Groeneveld and Melinda Oroszl{\'a}n and Rick T. Owens and Maria C. Faber-Krol and Astrid C. Bakker and G{\'e}rard J. Arlaud and David James McQuillan and Uday Kishore and Mohamed R. Daha and Anja Roos},
  journal={Journal of immunology},
  year={2005},
  volume={175 7},
  pages={4715-23}
}
Decorin and biglycan are closely related abundant extracellular matrix proteoglycans that have been shown to bind to C1q. Given the overall structural similarities between C1q and mannose-binding lectin (MBL), the two key recognition molecules of the classical and the lectin complement pathways, respectively, we have examined functional consequences of the interaction of C1q and MBL with decorin and biglycan. Recombinant forms of human decorin and biglycan bound C1q via both collagen and… CONTINUE READING