Erschienen in:
01.12.1999 | Paper Report
Serum amyloid P component prevents antinuclear autoimmunity
verfasst von:
Matthew Pickering
Erschienen in:
Arthritis Research & Therapy
|
Ausgabe 1/2000
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Excerpt
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, human SAP binds in vivo both to apoptotic cells, the surface blebs of which bear chromatin fragments, and to nuclear debris released by necrosis. SAP may therefore participate in the handling of chromatin exposed by cell death. To investigate the physiological role of SAP in vivo. …