ISSN:
1437-7799
Keywords:
Key words Nucleosome
;
Human GBM
;
Amyloid P component
;
Lupus nephritis
Source:
Springer Online Journal Archives 1860-2000
Topics:
Medicine
Notes:
Abstract Background. Tissue amyloid P component is a normal constituent of the human glomerular basement membrane (GBM) and is immunologically identical to the serum amyloid P component, a major DNA binding protein in serum. We postulate that DNA or nucleosome core particles could bind to human GBM via the amyloid P component. Methods. An immunofluorescence study was used to detect the amyloid P component of the GBM. An enzyme-linked immunosorbent assay system was used to test the binding capacity of calf thymus DNA and chicken erythrocyte nucleosome core particles to a preparation of human GBM. Results. Amyloid P component was detected along the capillary wall of the human glomerulus by immunofluorescence. DNA and nucleosome core particles bound to human GBM in a dose-dependent manner in the presence of Ca2+. Digestion of GBM with trypsin resulted in the reduction of binding of anti-serum amyloid P antibody, DNA, and nucleosome core particles to the GBM. Anti-serum amyloid P component (SAP) IgG blocked the binding of DNA and nucleosome core particles to the GBM. Conclusion. DNA and nucleosome core particles bind to the GBM through amyloid P components.
Type of Medium:
Electronic Resource
URL:
http://dx.doi.org/10.1007/s101570050060
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