Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D.

@article{Christensen2010OsteopontinIC,
  title={Osteopontin is cleaved at multiple sites close to its integrin-binding motifs in milk and is a novel substrate for plasmin and cathepsin D.},
  author={Brian Christensen and Lotte Schack and Eva Kl{\"a}ning and Esben Skipper S\orensen},
  journal={The Journal of biological chemistry},
  year={2010},
  volume={285 11},
  pages={7929-37}
}
Osteopontin (OPN) is a highly modified integrin-binding protein present in most tissues and body fluids where it has been implicated in numerous biological processes. A significant regulation of OPN function is mediated through phosphorylation and proteolytic processing. Proteolytic cleavage by thrombin and matrix metalloproteinases close to the integrin… CONTINUE READING