Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment.

@article{Winnemller1992InteractionsBT,
  title={Interactions between thrombospondin and the small proteoglycan decorin: interference with cell attachment.},
  author={M Winnem{\"o}ller and P Sch{\"o}n and Peter Vischer and Hans Kresse},
  journal={European journal of cell biology},
  year={1992},
  volume={59 1},
  pages={47-55}
}
Decorin, a ubiquitous small interstitial dermatan sulfate proteoglycan, interacts with several extracellular matrix components, e.g., with type I collagen and fibronectin. Using a solid phase assay it is shown that the intact proteoglycan as well as its glycosaminoglycan-free core protein exhibits with KD values of about 5 nM and 2 nM, respectively, high affinity binding also to thrombospondin. However, the polysaccharide chain was required for an interaction with Sepharose-bound thrombospondin… CONTINUE READING

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