Type IX collagen interacts with fibronectin providing an important molecular bridge in articular cartilage.

@article{Parsons2011TypeIC,
  title={Type IX collagen interacts with fibronectin providing an important molecular bridge in articular cartilage.},
  author={Philippa Parsons and Sophie J. Gilbert and Anne Vaughan-Thomas and David A. Sorrell and Rebecca Notman and Mark Bishop and Anthony J. Hayes and Deborah J. Mason and Victor C. Duance},
  journal={The Journal of biological chemistry},
  year={2011},
  volume={286 40},
  pages={34986-97}
}
Type IX collagen is covalently bound to the surface of type II collagen fibrils within the cartilage extracellular matrix. The N-terminal, globular noncollagenous domain (NC4) of the α1(IX) chain protrudes away from the surface of the fibrils into the surrounding matrix and is available for molecular interactions. To define these interactions, we used the NC4 domain in a yeast two-hybrid screen of a human chondrocyte cDNA library. 73% of the interacting clones encoded fibronectin. The… CONTINUE READING
Recent Discussions
This paper has been referenced on Twitter 1 time over the past 90 days. VIEW TWEETS
10 Citations
0 References
Similar Papers

Citations

Publications citing this paper.
Showing 1-10 of 10 extracted citations

Similar Papers

Loading similar papers…