scholarly journals Human Serum Amyloid P Component Protects againstEscherichia coliO157:H7 Shiga Toxin 2 In Vivo: Therapeutic Implications for Hemolytic‐Uremic Syndrome

2006 ◽  
Vol 193 (8) ◽  
pp. 1120-1124 ◽  
Author(s):  
Glen D. Armstrong ◽  
George L. Mulvey ◽  
Paola Marcato ◽  
Thomas P. Griener ◽  
Melvyn C. Kahan ◽  
...  
Keyword(s):  
Human Serum ◽  
Shiga Toxin ◽  
Amyloid P Component ◽  
Therapeutic Implications ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Shiga Toxin 2 ◽  
Uremic Syndrome ◽  
Amyloid P

scholarly journals Protection of Human Podocytes from Shiga Toxin 2-Induced Phosphorylation of Mitogen-Activated Protein Kinases and Apoptosis by Human Serum Amyloid P Component

2014 ◽  
Vol 82 (5) ◽  
pp. 1872-1879 ◽  
Author(s):  
Anne K. Dettmar ◽  
Elisabeth Binder ◽  
Friederike R. Greiner ◽  
Max C. Liebau ◽  
Christine E. Kurschat ◽  
...  
Keyword(s):  
Human Serum ◽  
Protein Kinases ◽  
Shiga Toxin ◽  
Mitogen Activated Protein Kinases ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Mitogen Activated Protein ◽  
Shiga Toxin 2 ◽  
Amyloid P

ABSTRACTHemolytic uremic syndrome (HUS) is mainly induced by Shiga toxin 2 (Stx2)-producingEscherichia coli. Proteinuria can occur in the early phase of the disease, and its persistence determines the renal prognosis. Stx2 may injure podocytes and induce proteinuria. Human serum amyloid P component (SAP), a member of the pentraxin family, has been shown to protect against Stx2-induced lethality in micein vivo, presumably by specific binding to the toxin. We therefore tested the hypothesis that SAP can protect against Stx2-induced injury of human podocytes. To elucidate the mechanisms underlying podocyte injury in HUS-associated proteinuria, we assessed Stx2-induced activation of mitogen-activated protein kinases (MAPKs) and apoptosis in immortalized human podocytes and evaluated the impact of SAP on Stx2-induced damage. Human podocytes express Stx2-binding globotriaosylceramide 3. Stx2 applied to cultured podocytes was internalized and then activated p38α MAPK and c-Jun N-terminal kinase (JNK), important signaling steps in cell differentiation and apoptosis. Stx2 also activated caspase 3, resulting in an increased level of apoptosis. Coincubation of podocytes with SAP and Stx2 mitigated the effects of Stx2 and induced upregulation of antiapoptotic Bcl2. These data suggest that podocytes are a target of Stx2 and that SAP protects podocytes against Stx2-induced injury. SAP may therefore be a useful therapeutic option.

scholarly journals Lipopolysaccharide Renders Transgenic Mice Expressing Human Serum Amyloid P Component Sensitive to Shiga Toxin 2

PLoS ONE ◽  
2011 ◽  
Vol 6 (6) ◽  
pp. e21457 ◽  
Author(s):  
Thomas P. Griener ◽  
Jonathan G. Strecker ◽  
Romney M. Humphries ◽  
George L. Mulvey ◽  
Carmen Fuentealba ◽  
...  
Keyword(s):  
Transgenic Mice ◽  
Human Serum ◽  
Shiga Toxin ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Shiga Toxin 2 ◽  
Amyloid P

scholarly journals Serum Amyloid P Component Is the Shiga Toxin 2-neutralizing Factor in Human Blood

2001 ◽  
Vol 276 (45) ◽  
pp. 41576-41579 ◽  
Author(s):  
Tsuyoshi Kimura ◽  
Shinobu Tani ◽  
Yoh-ichi Matsumoto ◽  
Tae Takeda
Keyword(s):  
Human Blood ◽  
Shiga Toxin ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Shiga Toxin 2 ◽  
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.

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
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