The distribution of amyloid P component in normal human cervix

1983 ◽  
Vol 43 (1) ◽  
pp. 63-66 ◽  
Author(s):  
S. J. Clayton ◽  
F. Walker
1989 ◽  
Vol 157 (1) ◽  
pp. 11-14 ◽  
Author(s):  
Richard Herriot ◽  
Frederick Walker

Nature ◽  
1981 ◽  
Vol 293 (5834) ◽  
pp. 652-654 ◽  
Author(s):  
S. M. Breathnach ◽  
Susan M. Melrose ◽  
B. Bhogal ◽  
F. C. de Beer ◽  
R. F. Dyck ◽  
...  

Placenta ◽  
1985 ◽  
Vol 6 (6) ◽  
pp. 551-554 ◽  
Author(s):  
A.M. Khan ◽  
F. Walker

1983 ◽  
Vol 80 (2) ◽  
pp. 86-90 ◽  
Author(s):  
Stephen M. Breathnach ◽  
Susan M. Melrose ◽  
Balbir Bhogal ◽  
Frederick C. De Beer ◽  
Martin M. Black ◽  
...  

1989 ◽  
Vol 170 (4) ◽  
pp. 1433-1438 ◽  
Author(s):  
S M Breathnach ◽  
H Kofler ◽  
N Sepp ◽  
J Ashworth ◽  
D Woodrow ◽  
...  

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.


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