scholarly journals Human serum amyloid P component, a circulating lectin with specificity for the cyclic 4,6-pyruvate acetal of galactose. Interactions with various bacteria

1985 ◽  
Vol 225 (1) ◽  
pp. 107-111 ◽  
Author(s):  
C R K Hind ◽  
P M Collins ◽  
M L Baltz ◽  
M B Pepys
Keyword(s):  
Xanthomonas Campestris ◽  
Group A Streptococcus ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Group A ◽  
Amyloid P ◽  
Specific Ligand

Serum amyloid P component (SAP), a normal plasma glycoprotein, has recently been shown to have Ca2+-dependent binding specificity for methyl 4,6-O-(1-carboxyethylidene)-beta-D-galactopyranoside (MO beta DG) [Hind, Collins, Renn, Cook, Caspi, Baltz & Pepys (1984) J. Exp. Med. 159, 1058-1069]. SAP was found to bind in vitro to Klebsiella rhinoscleromatis, the cell wall of which is known to contain this particular cyclic pyruvate acetal of galactose. SAP also bound in similar amounts (approx. 6000 molecules per organism) to group A Streptococcus pyogenes, but very much less was taken up on Xanthomonas campestris, which contains the 4,6-cyclic pyruvate acetal of mannose. No SAP bound to Escherichia coli, which contains the 4,6-cyclic pyruvate acetal of glucose, or to Streptococcus pneumoniae type 4, which contains the 2,3-cyclic pyruvate acetal of alpha- rather than beta-galactopyranoside, or to other organisms (Streptococcus agalactiae, Staphylococcus aureus and Staphylococcus epidermidis), the carbohydrate structures of which are less well characterized. Binding of SAP to those organisms which it did recognize was completely inhibited or reversed by millimolar concentrations of free MO beta DG. SAP, a human plasma protein, thus behaves as a lectin and may be a useful probe for its particular specific ligand in the cell walls of bacteria and other organisms.

scholarly journals Serum Amyloid P Component Prevents High-Density Lipoprotein-Mediated Neutralization of Lipopolysaccharide

2000 ◽  
Vol 68 (9) ◽  
pp. 4954-4960 ◽  
Author(s):  
Carla J. C. de Haas ◽  
Miriam J. J. G. Poppelier ◽  
Kok P. M. van Kessel ◽  
Jos A. G. van Strijp
Keyword(s):  
Magnetic Beads ◽  
High Density ◽  
Serum Amyloid ◽  
High Density Lipoproteins ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P ◽  
Lps Binding

ABSTRACT Lipopolysaccharide (LPS) is an amphipathic macromolecule that is highly aggregated in aqueous preparations. LPS-binding protein (LBP) catalyzes the transfer of single LPS molecules, segregated from an LPS aggregate, to high-density lipoproteins (HDL), which results in the neutralization of LPS. When fluorescein isothiocyanate-labeled LPS (FITC-LPS) is used, this transfer of LPS monomers to HDL can be measured as an increase in fluorescence due to dequenching of FITC-LPS. Recently, serum amyloid P component (SAP) was shown to neutralize LPS in vitro, although only in the presence of low concentrations of LBP. In this study, we show that SAP prevented HDL-mediated dequenching of FITC-LPS, even in the presence of high concentrations of LBP. Human bactericidal/permeability-increasing protein (BPI), a very potent LPS-binding and -neutralizing protein, also prevented HDL-mediated dequenching of FITC-LPS. Furthermore, SAP inhibited HDL-mediated neutralization of both rough and smooth LPS in a chemiluminescence assay quantifying the LPS-induced priming of neutrophils in human blood. SAP bound both isolated HDL and HDL in serum. Using HDL-coated magnetic beads prebound with SAP, we demonstrated that HDL-bound SAP prevented the binding of LPS to HDL. We suggest that SAP, by preventing LPS binding to HDL, plays a regulatory role, balancing the amount of LPS that, via HDL, is directed to the adrenal glands.

scholarly journals Multifaceted anti-amyloidogenic and pro-amyloidogenic effects of C-reactive protein and serum amyloid P component in vitro

2016 ◽  
Vol 6 (1) ◽  
Author(s):  
Daisaku Ozawa ◽  
Ryo Nomura ◽  
P. Patrizia Mangione ◽  
Kazuhiro Hasegawa ◽  
Tadakazu Okoshi ◽  
...  
Keyword(s):  
Serum Amyloid ◽  
C Reactive Protein ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P

scholarly journals Serum Amyloid P Component Binds to Influenza A Virus Haemagglutinin and Inhibits the Virus Infection In Vitro

1997 ◽  
Vol 46 (4) ◽  
pp. 331-337 ◽  
Author(s):  
O. ANDERSEN ◽  
K. VILSGAARD RAVN ◽  
I. JUUL SØRENSEN ◽  
G. JONSON ◽  
E. HOLM NIELSEN ◽  
...  
Keyword(s):  
Virus Infection ◽  
Influenza A Virus ◽  
Influenza A ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P ◽  
Virus Haemagglutinin

Glycosaminoglycans inhibit neurodegenerative effects of serum amyloid P component in vitro

2005 ◽  
Vol 46 (6) ◽  
pp. 471-477 ◽  
Author(s):  
Zoltán Urbányi ◽  
Erika Forrai ◽  
Miklós Sárvári ◽  
István Likó ◽  
János Illés ◽  
...  
Keyword(s):  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P
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