Characterization of the acute phase serum protein response in pigs

1994 ◽  
Vol 15 (1) ◽  
pp. 672-676 ◽  
Author(s):  
Fermín Lampreave ◽  
Nieves González-Ramón ◽  
Silvio Martínez-Ayensa ◽  
Miguel-Angel Hernández ◽  
Hans-Kristian Lorenzo ◽  
...  
Keyword(s):  
Serum Protein ◽  
Acute Phase ◽  
Protein Response ◽  
Acute Phase Serum

scholarly journals Characterization of the contributions of Hp-MMP 9 to the serum acute phase protein response of lipopolysaccharide challenged calves

2014 ◽  
Vol 10 (1) ◽  
Author(s):  
Charles A Hinds ◽  
Andrew J Niehaus ◽  
Christopher Premanandan ◽  
Paivi J Rajala-Schultz ◽  
Donald M Rings ◽  
...  
Keyword(s):  
Acute Phase ◽  
Acute Phase Protein ◽  
Acute Phase Protein Response ◽  
Phase Protein ◽  
Protein Response

scholarly journals Isolation and characterization of bovine haptoglobin from acute phase sera

1991 ◽  
Vol 266 (18) ◽  
pp. 11833-11837
Author(s):  
M. Morimatsu ◽  
B. Syuto ◽  
N. Shimada ◽  
T. Fujinaga ◽  
S. Yamamoto ◽  
...  
Keyword(s):  
Acute Phase ◽  
Isolation And Characterization

scholarly journals Correction: Effects of vaccination on acute-phase protein response in broiler chicken

PLoS ONE ◽  
2020 ◽  
Vol 15 (3) ◽  
pp. e0230949
Author(s):  
Arash Janmohammadi ◽  
Nariman Sheikhi ◽  
Hadi Haghbin Nazarpak ◽  
Gholamreza Nikbakht Brujeni
Keyword(s):  
Acute Phase ◽  
Broiler Chicken ◽  
Acute Phase Protein ◽  
Acute Phase Protein Response ◽  
Phase Protein ◽  
Protein Response

scholarly journals Rabbit and rat C-reactive proteins bind apolipoprotein B-containing lipoproteins.

1984 ◽  
Vol 159 (2) ◽  
pp. 604-616 ◽  
Author(s):  
I F Rowe ◽  
A K Soutar ◽  
I M Trayner ◽  
M L Baltz ◽  
F C de Beer ◽  
...  
Keyword(s):  
Acute Phase ◽  
Apolipoprotein B ◽  
Low Density Lipoprotein ◽  
Density Lipoprotein ◽  
Plasma Lipoproteins ◽  
Free Form ◽  
Low Density ◽  
Serum Samples ◽  
Acute Phase Serum

Immobilized rabbit and rat C-reactive protein (CRP) were found to selectively bind apolipoprotein B (apoB)-containing lipoproteins (low density lipoprotein, LDL and very low density lipoprotein, VLDL) from whole serum in a manner similar to that previously reported with human CRP. In acute phase human serum the CRP is in a free form, not complexed with lipoprotein or any other macromolecular ligand, and in acute phase serum from most rabbits fed on a normal diet the rabbit CRP was also free. However, in acute phase serum or heparinized plasma from hypercholesterolemic rabbits part or all of the CRP was found by gel filtration and immunoelectrophoretic techniques to be complexed with beta-VLDL, an abnormal apoB-containing plasma lipoprotein present in these animals. The presence of extent in different serum samples of CRP complexed with lipoprotein correlated closely with the serum apoB concentration. The formation of complexes between native, unaggregated rabbit CRP in solution and apoB-containing lipoproteins was readily demonstrable experimentally both with the isolated proteins and in whole serum. In all cases these interactions were calcium-dependent and inhibitable by free phosphoryl choline. The present findings extend earlier work in man and the rabbit and indicate that among the C-reactive proteins from different species, which are structurally highly conserved, the capacity for selective binding to apoB-containing plasma lipoproteins is also a constant feature. These interactions may therefore be related to the in vivo function of CRP in all species and this function may in turn be relevant to pathological conditions, such as atherosclerosis, in which lipoproteins are important.

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