Structural characterization of human recombinant and bone-derived bone sialoprotein. Functional implications for cell attachment and hydroxyapatite binding.

@article{Wuttke2001StructuralCO,
  title={Structural characterization of human recombinant and bone-derived bone sialoprotein. Functional implications for cell attachment and hydroxyapatite binding.},
  author={Martin Wuttke and Stefan M{\"u}ller and Dirk Nitsche and Mats Paulsson and Franz-Georg Hanisch and Patrik Maurer},
  journal={The Journal of biological chemistry},
  year={2001},
  volume={276 39},
  pages={36839-48}
}
Human bone sialoprotein (BSP) comprises 15% of the total noncollagenous proteins in bone and is thought to be involved in bone mineralization and remodeling. Recent data suggest a role for BSP in breast cancer and the development of bone metastases. We have produced full-length recombinant BSP in a human cell line and purified the protein from human bone… CONTINUE READING