Serum amyloid P component controls chromatin degradation and prevents antinuclear autoimmunity

@article{Bickerstaff1999SerumAP,
  title={Serum amyloid P component controls chromatin degradation and prevents antinuclear autoimmunity},
  author={Mcm Bickerstaff and M. Botto and W. Hutchinson and J. Herbert and G. Tennent and A. Bybee and D. A. Mitchell and H. Cook and P. Butler and M. Walport and M. Pepys},
  journal={Nature Medicine},
  year={1999},
  volume={5},
  pages={694-697}
}
  • Mcm Bickerstaff, M. Botto, +8 authors M. Pepys
  • Published 1999
  • Medicine
  • Nature Medicine
  • Serum amyloid P component (SAP), a highly conserved plasma protein named for its universal presence in amyloid deposits, is the single normal circulating protein that shows specific calcium-dependent binding to DNA and chromatin in physiological conditions. The avid binding of SAP displaces H1-type histones and thereby solubilizes native long chromatin, which is otherwise profoundly insoluble at the physiological ionic strength of extracellular fluids. Furthermore, SAP binds in vivo both to… CONTINUE READING
    Chromatin-Independent Binding of Serum Amyloid P Component to Apoptotic Cells
    • 140
    • PDF
    Nucleosomes Are Exposed at the Cell Surface in Apoptosis1
    • 215
    • PDF

    References

    Publications referenced by this paper.
    SHOWING 1-10 OF 30 REFERENCES