Adhesive properties of osteopontin: regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain.

@article{Senger1994AdhesivePO,
  title={Adhesive properties of osteopontin: regulation by a naturally occurring thrombin-cleavage in close proximity to the GRGDS cell-binding domain.},
  author={Donald R. Senger and Carole A. Perruzzi and A Papadopoulos-Sergiou and Livingston Van de Water},
  journal={Molecular biology of the cell},
  year={1994},
  volume={5 5},
  pages={565-74}
}
Osteopontin (OPN) is a secreted adhesive glycoprotein with a functional glycine-arginine-glycine-aspartate-serine (GRGDS) cell-binding domain. An interesting feature of OPN structure is the presence of a thrombin-cleavage site in close proximity to the GRGDS region. Cleavage of OPN by thrombin is likely to be of physiological importance, because cleavage of blood plasma OPN occurs naturally after activation of the blood coagulation pathway. To investigate functional consequences of OPN cleavage… CONTINUE READING
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