The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex.

@article{Krumdieck1992ThePD,
  title={The proteoglycan decorin binds C1q and inhibits the activity of the C1 complex.},
  author={R Krumdieck and Magnus H{\"o}{\"o}k and Lawrence C. Rosenberg and John E. Volanakis},
  journal={Journal of immunology},
  year={1992},
  volume={149 11},
  pages={3695-701}
}
Decorin, a small collagen-binding dermatan sulfate proteoglycan, is widely distributed as a component of extracellular matrices. Using a solid phase binding assay, we showed that decorin bound C1q at physiologic pH and ionic strength. The interaction did not require divalent cations and was time and temperature dependent reaching equilibrium in 4 h at 37 degrees C. Binding was specific and saturable with an apparent dissociation constant of 7.6 x 10(-9) M. Decorin was shown to bind pepsin… CONTINUE READING
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