Mouse hepatocyte synthesis and induction of the acute phase reactant: Serum amyloid P-component

In Vitro ◽  
1984 ◽  
Vol 20 (6) ◽  
pp. 505-511 ◽  
Author(s):  
Phong T. Le ◽  
Richard F. Mortensen
Keyword(s):  
Acute Phase ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
Mouse Hepatocyte ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Phase Reactant ◽  
Serum Amyloid P Component ◽  
Amyloid P

Serum amyloid P-component is an acute-phase reactant in the mouse

Nature ◽  
1979 ◽  
Vol 278 (5701) ◽  
pp. 259-261 ◽  
Author(s):  
M. B. PEPYS ◽  
MARILYN BALTZ ◽  
K. GOMER ◽  
A. J. S. DAVIES ◽  
M. DOENHOFF
Keyword(s):  
Acute Phase ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Phase Reactant ◽  
Serum Amyloid P Component ◽  
Amyloid P

Human Serum Amyloid P-Component (SAP) as an Acute Phase Reactant in the Female

Amyloidosis ◽  
1986 ◽  
pp. 87-97 ◽  
Author(s):  
Shunsuke Migita ◽  
Shigeru Hashimototo ◽  
Haruo Hisazumi ◽  
Mine Harada ◽  
Hiroaki Okabe
Keyword(s):  
Human Serum ◽  
Acute Phase ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Phase Reactant ◽  
Serum Amyloid P Component ◽  
Amyloid P

Receptor-mediated binding of the acute-phase reactant mouse serum amyloid P-component (SAP) to macrophages

1988 ◽  
Vol 117 (2) ◽  
pp. 239-252 ◽  
Author(s):  
Janya Siripont ◽  
Julie M. Tebo ◽  
Richard F. Mortensen
Keyword(s):  
Acute Phase ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
Mouse Serum ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Phase Reactant ◽  
Serum Amyloid P Component ◽  
Mouse Serum Amyloid ◽  
Amyloid P

IL-1 and IL-6 mediate increased production and synthesis by hepatocytes of acute-phase reactant mouse serum amyloid P-component (SAP)

Inflammation ◽  
1990 ◽  
Vol 14 (3) ◽  
pp. 297-313 ◽  
Author(s):  
Bih-Fen Lin ◽  
Nam-On Ku ◽  
Kamyar Zahedi ◽  
Alexander S. Whitehead ◽  
Richard F. Mortensen
Keyword(s):  
Acute Phase ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
Mouse Serum ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Phase Reactant ◽  
Serum Amyloid P Component ◽  
Mouse Serum Amyloid ◽  
Amyloid P

Quantitative Western blot assay for measurement of the murine acute phase reactant, serum amyloid P component

1986 ◽  
Vol 91 (2) ◽  
pp. 163-168 ◽  
Author(s):  
D.E. Griswold ◽  
L. Hillegass ◽  
L. Antell ◽  
A. Shatzman ◽  
N. Hanna
Keyword(s):  
Western Blot ◽  
Acute Phase ◽  
Acute Phase Reactant ◽  
Western Blot Assay ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Phase Reactant ◽  
Serum Amyloid P Component ◽  
Quantitative Western Blot ◽  
Amyloid P

Induction of Hepatocyte Synthesis of the Mouse Acute Phase Protein Serum Amyloid P-Component (SAP) by IL-1 and IL-6

2008 ◽  
Vol 557 (1) ◽  
pp. 534-535 ◽  
Author(s):  
BIH-FEN LIN ◽  
NAM-ON KU ◽  
KAMYAR ZAHEDI ◽  
ALEXANDER S. WHITEHEAD ◽  
RICHARD F. MORTENSEN
Keyword(s):  
Acute Phase ◽  
Acute Phase Protein ◽  
Serum Amyloid ◽  
Amyloid P Component ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Phase Protein ◽  
Amyloid P ◽  
Protein Serum

Further Studies on the Modulation of Blood Coagulation by Human Serum Amyloid P Component and Its Acute Phase Homologue C-Reactive Protein

1986 ◽  
Vol 55 (03) ◽  
pp. 406-409 ◽  
Author(s):  
B A Fiedel ◽  
Cecilia S L Ku
Keyword(s):  
Blood Coagulation ◽  
Acute Phase ◽  
Serum Amyloid ◽  
C Reactive Protein ◽  
Amyloid P Component ◽  
Reactive Protein ◽  
Serum Amyloid P ◽  
Serum Amyloid P Component ◽  
Amyloid P ◽  
Free Plasma

SummarySerum amyloid P component (SAP), and its acute phase homologue C-reactive protein (CRP), prolonged activated partial thromboplastin times (APTT) in cell free plasma when assayed at physiological concentrations in the presence of heparin. SAP also inhibited clot formation initiated through the extrinsic and terminal phases of coagulation in heparinized cell free plasma, an activity not shared with CRP. When CRP and SAP were similarly evaluated in whole blood using the thromboelastograph (TEG), CRP delayed the onset of coagulation and the initial rate of fibrin formation/polymerization; final clot patency was unaltered. SAP suppressed the anticoagulant activity of heparin in the TEG assay, unlike results obtained in heparinized cell free plasma, by facilitating a more rapid onset of coagulation, increasing the rate of fibrin formation/polymerization, and correcting clot patency. The data provided offer further evidence that these homologues can intercede in blood coagulation.

Sign in / Sign up

Export Citation Format

Share Document