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Serum amyloid P component binds to cell nuclei in vitro and to in vivo deposits of extracellular chromatin in systemic lupus erythematosus.

Breathnach, SM; Kofler, H; Sepp, N; Ashworth, J; Woodrow, D; Pepys, MB; Hintner, H; (1989) Serum amyloid P component binds to cell nuclei in vitro and to in vivo deposits of extracellular chromatin in systemic lupus erythematosus. J Exp Med , 170 (4) pp. 1433-1438.

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Abstract

Serum amyloid P component (SAP) is the single plasma protein that, from the milieu of whole normal human serum, undergoes specific calcium-dependent binding to isolated DNA and chromatin in vitro. We now report for the first time that SAP in whole serum also undergoes calcium-dependent binding to nuclei of epidermal cells in sections of normal human skin and to nuclei of fixed Hep-2 cells, a human epithelial cell line. Furthermore, and most importantly, SAP was detected in association with unusual globular dermal deposits of nuclear material in skin biopsies from two patients with systemic lupus erythematosus. This is the first evidence for binding of SAP to extracellular chromatin in vivo and supports the idea that SAP may have an important physiological role in the disposal of this material.

Type: Article
Title: Serum amyloid P component binds to cell nuclei in vitro and to in vivo deposits of extracellular chromatin in systemic lupus erythematosus.
Location: United States
Keywords: Cell Line, Cell Nucleus, Chromatin, Humans, In Vitro Techniques, Lupus Erythematosus, Systemic, Serum Amyloid P-Component, Skin
UCL classification: UCL > Provost and Vice Provost Offices
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine
UCL > Provost and Vice Provost Offices > School of Life and Medical Sciences > Faculty of Medical Sciences > Div of Medicine > Inflammation
URI: http://discovery.ucl.ac.uk/id/eprint/1552015
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