scholarly journals Antibodies to human serum amyloid P component eliminate visceral amyloid deposits

Nature ◽  
2010 ◽  
Vol 468 (7320) ◽  
pp. 93-97 ◽  
Author(s):  
Karl Bodin ◽  
Stephan Ellmerich ◽  
Melvyn C. Kahan ◽  
Glenys A. Tennent ◽  
Andrzej Loesch ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid Deposits ◽  
Amyloid P

scholarly journals Human serum amyloid P component is an invariant constituent of amyloid deposits and has a uniquely homogeneous glycostructure.

1994 ◽  
Vol 91 (12) ◽  
pp. 5602-5606 ◽  
Author(s):  
M. B. Pepys ◽  
T. W. Rademacher ◽  
S. Amatayakul-Chantler ◽  
P. Williams ◽  
G. E. Noble ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid Deposits ◽  
Amyloid P

scholarly journals X-ray crystallographic studies of human serum amyloid P-component (SAP)

1987 ◽  
Vol 43 (a1) ◽  
pp. C10-C10
Author(s):  
G. Oliva ◽  
B. P. O'Hara ◽  
S. Wood ◽  
H. White ◽  
M. B. Pepys ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
X Ray ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

Studies with Radiolabelled Serum Amyloid P Component Provide Evidence for Turnover and Regression of Amyloid Deposits In Vivo

1994 ◽  
Vol 87 (3) ◽  
pp. 289-295 ◽  
Author(s):  
Philip N. Hawkins
Keyword(s):  
Amyloid Fibrils ◽  
Specific Binding ◽  
Serum Amyloid ◽  
Poor Correlation ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid Deposits ◽  
Amyloid P

1. Quantitative scintigraphic and turnover studies, utilizing the specific binding affinity of serum amyloid P component for amyloid fibrils, have been developed as a tool for evaluating amyloid deposits in vivo. 2. Serial studies in over 300 patients have shown characteristic, diagnostic tissue distributions of amyloid in different types of amyloidosis. There is generally a poor correlation between quantity of amyloid and associated organ dysfunction. 3. Contrary to previous expectations, regression of amyloid has been demonstrated systematically for the first time: AA, AL and variant transthyretin-associated amyloid deposits often regress rapidly, and sometimes completely, if the supply of fibril protein precursors is substantially reduced.

Binding of serum amyloid P component to heparin in human serum

1994 ◽  
Vol 1201 (2) ◽  
pp. 143-148 ◽  
Author(s):  
X LI ◽  
K HATANAKA ◽  
L GUO ◽  
Y KITAMURA ◽  
A YAMAMOTO
Keyword(s):  
Human Serum ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

Form and folding of pentameric human serum Amyloid P component

2002 ◽  
Vol 217 (7-8) ◽  
Author(s):  
A. Janner
Keyword(s):  
Human Serum ◽  
Quaternary Structure ◽  
Point Group ◽  
Serum Amyloid ◽  
Molecular Forms ◽  
Golden Mean ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

AbstractThe molecular prismatic forms which enclose the tertiary and the quaternary structure of the human serum Amyloid P component show remarkable ratios expressible in terms of the golden mean. A scale-rotation crystallographic point group, leaving these forms invariant, allows to explain these golden mean proportions and to assign integer indices to the vertices of the molecular forms.

scholarly journals Binding specificity of serum amyloid P component for the pyruvate acetal of galactose.

1984 ◽  
Vol 159 (4) ◽  
pp. 1058-1069 ◽  
Author(s):  
C R Hind ◽  
P M Collins ◽  
D Renn ◽  
R B Cook ◽  
D Caspi ◽  
...  
Keyword(s):  
Amyloid Fibrils ◽  
Binding Specificity ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Calcium Dependent ◽  
Protein Ligands ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid Deposits ◽  
Amyloid P

Serum amyloid P component (SAP) is a normal plasma protein that is of interest because of its presence in amyloid deposits, its presence in normal human glomerular basement membrane, and its stable evolutionary conservation. It has calcium-dependent ligand-binding specificity for amyloid fibrils, fibronectin (Fn), C4-binding protein (C4bp), and agarose. Although the binding to agarose, a linear galactan hydrocolloid derived from some marine algae, is unlikely per se to be related to the physiological function of SAP, it does provide a model system in which to explore the precise ligand requirements of SAP. We report here that the amount of SAP from human, mouse, and plaice (Pleuronectes platessa L.) serum able to bind to agarose from different sources reflect precisely their pyruvate content. Methylation with diazomethane of the carboxyl groups in the pyruvate moiety of agarose completely abolishes SAP binding to agarose. The pyruvate in agarose exists as the 4,6-pyruvate acetal of beta-D-galactopyranose. We have therefore synthesized this galactoside, using a novel procedure, established its structure by analysis of its nuclear magnetic resonance spectra, and shown that it completely inhibits all known calcium-dependent binding reactions of SAP. The R isomer of the cyclic acetal, methyl 4,6-O-(1-carboxyethylidene)-beta-D-galactopyranoside (MO beta DG) was effective at millimolar concentration and was more potent than its noncyclic analogue, while pyruvate, D-galactose, and methyl beta-D-galactopyranoside were without effect. The autologous protein ligands of SAP presumably, therefore express a structural determinant(s) that stereochemically resembles MO beta DG. Availability of this specific, well-characterized, low molecular weight ligand for SAP should facilitate further investigation of the function of SAP and its role in physiological and pathophysiological processes.

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