Evaluation of goose serum amyloid a acute phase response by enzyme-linked immunosorbent assay

2007 ◽  
Vol 55 (3) ◽  
pp. 349-357 ◽  
Author(s):  
Beáta Kovács ◽  
Mathilda Toussaint ◽  
E. Gruys ◽  
Ibolya Fábián ◽  
L. Szilágyi ◽  
...  
Keyword(s):  
Acute Phase ◽  
Pasteurella Multocida ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Enzyme Linked Immunosorbent Assay ◽  
Common Disease ◽  
Post Inoculation ◽  
Secondary Amyloidosis ◽  
Phase Reaction ◽  
Amyloid A

Serum amyloid A (SAA) is of interest as the circulating precursor of amyloid A protein, the fibrillar component of AA (secondary) amyloid deposits, and also as an extremely sensitive and rapid major acute phase protein. Serum concentrations of acute phase proteins (APPs) provide valuable information about the diagnosis and prognosis of various diseases, and thus the relevance of APPs for monitoring the health status of domestic animals is widely accepted. More importantly, the measurement of SAA concentration assists in assessing the prognosis in secondary amyloidosis, which is a common disease of geese, affecting an increasing number of animals. In the present study we introduce a highly sensitive goose-specific ELISA method for measuring SAA concentration in goose serum or plasma samples. Samples were taken from geese of the Landes Grey and Hungarian White breeds, which were stimulated for an acute phase reaction by administration of a commercially available fowl cholera vaccine containing inactivated Pasteurella multocida . Strong and characteristically rapid acute phase responses were measured in both breeds, peaking at approximately 24 h after inoculation. The maximum SAA concentration was 1200 μg/ml. At 72 h post-inoculation, the concentrations returned to pre-inoculation values. There was significantly (p = 0.004) less intense response in the control groups; however, a very mild increase of SAA levels was detected due to the stress inevitably caused by the sampling procedure.

scholarly journals Adenoviral expression of murine serum amyloid A proteins to study amyloid fibrillogenesis

1998 ◽  
Vol 332 (3) ◽  
pp. 721-728 ◽  
Author(s):  
Mark S. KINDY ◽  
Amy R. KING ◽  
Jin YU ◽  
Connie GERARDOT ◽  
Joel WHITLEY ◽  
...  
Keyword(s):  
Acute Phase ◽  
Half Life ◽  
Serum Amyloid A ◽  
Amyloid Fibrils ◽  
Serum Amyloid ◽  
Vector System ◽  
High Density Lipoproteins ◽  
Secondary Amyloidosis ◽  
Amyloid A ◽  
J Protein

Serum amyloid A (SAA) proteins are one of the most inducible acute-phase reactants and are precursors of secondary amyloidosis. In the mouse, SAA1 and SAA2 are induced in approximately equal quantities in response to amyloid induction models. These two isotypes differ in only 9 of 103 amino acid residues; however, only SAA2 is selectively deposited into amyloid fibrils. SAA expression in the CE/J mouse species is an exception in that gene duplication did not occur and the CE/J variant is a hybrid molecule sharing features of SAA1 and SAA2. However, even though it is more closely related to SAA2 it is not deposited as amyloid fibrils. We have developed an adenoviral vector system to overexpress SAA proteins in cell culture to determine the ability of these proteins to form amyloid fibrils, and to study the structural features in relation to amyloid formation. Both the SAA2 and CE/J SAA proteins were synthesized in large quantities and purified to homogeneity. Electron microscopic analysis of the SAA proteins revealed that the SAA2 protein was capable of forming amyloid fibrils, whereas the CE/J SAA was incapable. Radiolabelled SAAs were associated with normal or acute-phase high-density lipoproteins (HDLs); we examined them for their clearance from the circulation. In normal mice, SAA2 had a half-life of 70 min and CE/J SAA had a half-life of 120 min; however, in amyloid mice 50% of the SAA2 cleared in 55 min, compared with 135 min for the CE/J protein. When the SAA proteins were associated with acute-phase HDLs, SAA2 clearance was decreased to 60 min in normal mice compared with 30 min in amyloidogenic mice. Both normal and acute-phase HDLs were capable of depositing SAA2 into preformed amyloid fibrils, whereas the CE/J protein did not become associated with amyloid fibrils. This established approach opens the doors for large-scale SAA production and for the examination of specific amino acids involved in the fibrillogenic capability of the SAA2 molecule in vitro and in vivo.

scholarly journals Acute-phase response protein serum amyloid A stimulates renal tubule formation: studies in vitro and in vivo

2009 ◽  
Vol 296 (6) ◽  
pp. F1355-F1363 ◽  
Author(s):  
Katherine J. Kelly ◽  
Barbara Kluve-Beckerman ◽  
Jesus H. Dominguez
Keyword(s):  
Acute Phase ◽  
Serum Amyloid A ◽  
Ischemia Reperfusion Injury ◽  
Ischemia Reperfusion ◽  
Serum Amyloid ◽  
Phase Reaction ◽  
Tubule Formation ◽  
Amyloid A ◽  
Serum Amyloid A Protein

Serum amyloid A protein (SAA) surges 1,000-fold in the blood of acute-phase animals, and yet its function during these acute events remains unknown. We report herein that SAA stimulates a developmental program in cultured NRK-52E cells that culminates in differentiated and functional tubules that feature a proximal tubule phenotype. We also found strong SAA expression in states of tubule formation (in utero stage) and regeneration (recovery from ischemia-reperfusion injury). These data lend support to a novel view of a more localized renal acute-phase reaction, where renal SAA may act as a paracrine or autocrine molecule that promotes tubule formation during development and repair.

scholarly journals Serum amyloid A is a chemoattractant: induction of migration, adhesion, and tissue infiltration of monocytes and polymorphonuclear leukocytes.

1994 ◽  
Vol 180 (1) ◽  
pp. 203-209 ◽  
Author(s):  
R Badolato ◽  
J M Wang ◽  
W J Murphy ◽  
A R Lloyd ◽  
D F Michiel ◽  
...  
Keyword(s):  
Acute Phase ◽  
Polymorphonuclear Leukocytes ◽  
Serum Amyloid A ◽  
High Density ◽  
Serum Amyloid ◽  
High Density Lipoproteins ◽  
Secondary Amyloidosis ◽  
Polymorphonuclear Cells ◽  
Amyloid A ◽  
Cell Adhesion Molecule 1

Serum amyloid A (SAA) is an acute phase protein that in the blood is bound to high density lipoproteins; SAA is secreted mainly by hepatocytes, and its concentration increases in the blood up to 1000 times during an inflammatory response. At present, its biological function is unclear. Since some forms of secondary amyloidosis are caused by deposition in tissues of peptides derived from the SAA and leukocytes seem to be involved in this process, we investigated the effect of human SAA on human monocytes and polymorphonuclear cells (PMN). When recombinant human SAA (rSAA) was used at concentrations corresponding to those found during the acute phase (> 0.8 microM), it induced directional migration of monocytes and polymorphonuclear leukocytes. Preincubation of rSAA with high density lipoproteins blocked this chemoattractant activity for both monocytes and PMN. rSAA also regulated the expression of the adhesion proteins CD11b and leukocyte cell adhesion molecule 1 and induced the adhesion of PMN and monocytes to umbilical cord vein endothelial cell monolayers. When subcutaneously injected into mice, rSAA recruited PMN and monocytes at the injection site. On the basis of these data, we suggest that SAA may participate in enhancing the migration of monocytes and PMN to inflamed tissues during an acute phase response.

scholarly journals Investigation of the solubility and the potentials for purification of serum amyloid A (SAA) from equine acute phase serum – a pilot study

2013 ◽  
Vol 6 (1) ◽  
Author(s):  
Michelle B Christensen ◽  
Jens Christian Sørensen ◽  
Stine Jacobsen ◽  
Mads Kjelgaard-Hansen
Keyword(s):  
Pilot Study ◽  
Acute Phase ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Acute Phase Serum

scholarly journals Regulation of rabbit acute phase protein biosynthesis by monokines

1988 ◽  
Vol 253 (3) ◽  
pp. 851-857 ◽  
Author(s):  
A Mackiewicz ◽  
M K Ganapathi ◽  
D Schultz ◽  
D Samols ◽  
J Reese ◽  
...  
Keyword(s):  
Acute Phase ◽  
Serum Amyloid A ◽  
Interleukin 1 ◽  
Serum Amyloid ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Amyloid A ◽  
Primary Hepatocyte Cultures ◽  
Dose Dependent ◽  
Necrosis Factor

We defined the acute phase behaviour of a number of rabbit plasma proteins in studies (in vivo) and studied the effects of monokine preparations on their synthesis by rabbit primary hepatocyte cultures. Following turpentine injection, increased serum levels of C-reactive protein, serum amyloid A protein, haptoglobin, ceruloplasmin, and decreased concentrations of albumin were observed. In contrast to what is observed in man, concentrations of alpha 2-macroglobulin and transferrin were increased. Co-culture of primary hepatocyte cultures with lipopolysaccharide-activated human peripheral blood monocytes or incubation with conditioned medium prepared from lipopolysaccharide-activated human or rabbit monocytes resulted in dose-dependent induction of serum amyloid A, haptoglobin, ceruloplasmin and transferrin and depression of albumin synthesis, while C-reactive protein synthesis and mRNA levels remained unchanged. A variety of interleukin-1 preparations induced dose-dependent increases in the synthesis and secretion of serum amyloid A, haptoglobin, ceruloplasmin and transferrin and decreased albumin synthesis. Human recombinant tumour necrosis factor (cachectin) induced a dose-dependent increase in synthesis of haptoglobin and ceruloplasmin. In general, human interleukin-1 was more potent than mouse interleukin-1 and tumour necrosis factor. None of the monokines we studied had an effect on C-reactive protein synthesis or mRNA levels. These data confirm that C-reactive protein, serum amyloid A, haptoglobin and ceruloplasmin display acute phase behaviour in the rabbit, and demonstrate that, in contrast to their behaviour in man, alpha 2M and transferrin are positive acute phase proteins in this species. While both interleukin-1 and tumour necrosis factor regulate biosynthesis of a number of these acute phase proteins in rabbit primary hepatocyte cultures, neither of these monokines induced C-reactive protein synthesis. Comparison of these findings with those in human hepatoma cell lines, in which interleukin-1 does not induce serum amyloid A synthesis, suggests that the effect of interleukin-1 on serum amyloid A synthesis may be indirect.

In search of the “LINK”: Acute Phase Serum Amyloid A

2011 ◽  
Vol 216 (2) ◽  
pp. 266-268
Author(s):  
Sidika Karakas ◽  
Rami Mortada ◽  
Clinical Fellow
Keyword(s):  
Acute Phase ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Acute Phase Serum
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