Nucleosome core particles and DNA bind to the human glomerular basement membrane (GBM): role of the amyloid P component of the GBM

2000 ◽  
Vol 4 (1) ◽  
pp. 43-48
Author(s):  
T. Morioka ◽  
K. Joh ◽  
F. Shimizu ◽  
T. Oite
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Amyloid P Component ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Amyloid P ◽  
Core Particles

Role of Histone Tails in the Conformation and Interactions of Nucleosome Core Particles†

Biochemistry ◽  
2004 ◽  
Vol 43 (16) ◽  
pp. 4773-4780 ◽  
Author(s):  
Aurélie Bertin ◽  
Amélie Leforestier ◽  
Dominique Durand ◽  
Françoise Livolant
Keyword(s):  
Histone Tails ◽  
Nucleosome Core ◽  
Nucleosome Core Particles ◽  
Core Particles

AMYLOID P-COMPONENT IN HUMAN GLOMERULAR BASEMENT MEMBRANE

The Lancet ◽  
1980 ◽  
Vol 316 (8195) ◽  
pp. 606-609 ◽  
Author(s):  
R.F Dyck ◽  
C.M Lockwood ◽  
D Turner ◽  
D.J Evans ◽  
A.J Rees ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Amyloid P Component ◽  
Amyloid P

scholarly journals Pentraxin-chromatin interactions: serum amyloid P component specifically displaces H1-type histones and solubilizes native long chromatin.

1990 ◽  
Vol 172 (1) ◽  
pp. 13-18 ◽  
Author(s):  
P J Butler ◽  
G A Tennent ◽  
M B Pepys
Keyword(s):  
Normal Serum ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Nucleosome Core ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P ◽  
Core Particles

Pure serum amyloid P component (SAP) and native long chromatin, mixed together at wt/wt ratios between 1:1 and 1:2 in the presence of physiological concentrations of NaCl and calcium, both remained in solution, whereas each alone precipitates rapidly under these conditions. This solubilization accompanies the binding of SAP to chromatin and the displacement of H1-type histones, which are essential for condensation and higher order folding of chromatin. Such binding of SAP to chromatin is remarkable since displacement of H1 and H5 by salt alone requires approximately 0.5 M NaCl. SAP also bound to nucleosome core particles forming soluble complexes with an apparent stoichiometry of 1:2, a result that is compatible with attachment of SAP at the nucleosome dyad, the site of H1 in intact chromatin. SAP thus undergoes a specific, avid interaction with chromatin that promotes its solubilization and may thereby contribute to the physiological handling of chromatin released from cells in vivo. In contrast, C-reactive protein (CRP) did not bind significantly to either chromatin or to core particles at physiological ionic strength. Incubation of chromatin with either normal serum, or acute phase human serum containing raised levels of CRP, did not induce complement activation regardless of the presence of added SAP or CRP, nor was any cleavage of DNA observed.

scholarly journals Amyloid P-component is a constituent of normal human glomerular basement membrane.

1980 ◽  
Vol 152 (5) ◽  
pp. 1162-1174 ◽  
Author(s):  
R F Dyck ◽  
C M Lockwood ◽  
M Kershaw ◽  
N McHugh ◽  
V C Duance ◽  
...  
Keyword(s):  
Basement Membrane ◽  
Glomerular Basement Membrane ◽  
Cross Reactivity ◽  
Basement Membranes ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Covalently Linked ◽  
Amyloid P

Glomerular and other vascular basement membranes were found to contain an antigen that was immunochemically indistinguishable from serum amyloid P-component. There was no immunological cross-reactivity between antisera to serum amyloid P-component and to collagen types I, III, IV, or V. The amyloid P-component antigen was confined to the endothelial aspect, the lamina rara interna, of glomerular basement membrane. It could not be eluted by high-ionic-strength saline, EDTA, dithiothreitol, or either polar or nonpolar detergents, but was released into solution when isolated glomerular basement membrane was digested by highly purified bacterial collagenase. Most of these P-component molecules and their constituent polypeptide chains were of higher molecular weight and lower isoelectric point than serum amyloid P-component. These findings indicate that, as well as being a normal plasma protein and a universal constituent of amyloid deposits, P-component is also a normal matrix glycoprotein of basement membrane in which it is covalently linked to collagen and/or other matrix proteins. This may be relevant both to the pathogenesis of amyloidosis and to other aspects of physiology and pathology of basement membranes.

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