The Dermatan Sulfate Proteoglycan Decorin Modulates α2β1 Integrin and the Vimentin Intermediate Filament System during Collagen Synthesis

@inproceedings{Jungmann2012TheDS,
  title={The Dermatan Sulfate Proteoglycan Decorin Modulates α2β1 Integrin and the Vimentin Intermediate Filament System during Collagen Synthesis},
  author={Oliver Jungmann and Katerina Nikolovska and Christian M. Stock and J Schulz and Beate Eckes and Christoph Riethm{\"u}ller and Rick T. Owens and Renato V Iozzo and Daniela G. Seidler},
  booktitle={PloS one},
  year={2012}
}
Decorin, a small leucine-rich proteoglycan harboring a dermatan sulfate chain at its N-terminus, is involved in regulating matrix organization and cell signaling. Loss of the dermatan sulfate of decorin leads to an Ehlers-Danlos syndrome characterized by delayed wound healing. Decorin-null (Dcn(-/-)) mice display a phenotype similar to that of EDS patients. The fibrillar collagen phenotype of Dcn(-/-) mice could be rescued in vitro by decorin but not with decorin lacking the glycosaminoglycan… CONTINUE READING
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