scholarly journals Human serum amyloid A protein. Behaviour in aqueous and urea-containing solutions and antibody production

1989 ◽  
Vol 263 (2) ◽  
pp. 365-370 ◽  
Author(s):  
A F Strachan ◽  
E G Shephard ◽  
D U Bellstedt ◽  
G A Coetzee ◽  
D R van der Westhuyzen ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Gel Filtration ◽  
Density Lipoprotein ◽  
High Titre ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Buffer Solutions ◽  
Wide Range ◽  
Serum Amyloid A Protein

Human serum amyloid A protein (apo-SAA) can be prepared by gel filtration of delipidated acute-phase high-density lipoprotein in the presence of urea. The resultant apo-SAA is soluble (greater than 90% solubility) in a wide range of buffer solutions, with all of the six major isoforms of apo-SAA being equally soluble. In urea-containing solutions the isoforms behave qualitatively differently in various urea concentrations, probably reflecting subtle primary-structure variations. The higher-pI isoforms are only completely unfolded at greater than 7 M-urea. By immunizing with apo-SAA adsorbed to acid-treated bacteria (Salmonella minnesota R595), high-titre antibodies can easily be elicited in rabbits.

Comparative Study of Serum Amyloid A Protein and C-Reactive Protein in Disease

1985 ◽  
Vol 68 (2) ◽  
pp. 233-238 ◽  
Author(s):  
C. P. J. Maury
Keyword(s):  
Serum Amyloid A ◽  
Tissue Injury ◽  
Serum Amyloid ◽  
Response To Treatment ◽  
Surgical Trauma ◽  
C Reactive Protein ◽  
Reactive Protein ◽  
Amyloid A ◽  
Wide Range ◽  
Serum Amyloid A Protein

1. On the basis of results from 3000 parallel measurements of serum amyloid A protein (SAA) and C-reactive protein (CRP) in various clinical and experimental conditions, the relationship between these proteins was examined and the question of whether measurements of SAA can provide clinically useful information beyond that from CRP assays was evaluated. 2. The concentrations of SAA and CRP showed a close relationship in a wide range of clinical conditions and the general clinical impact of an elevated SAA or CRP level is similar. SAA was, however, more sensitive than CRP in reflecting inflammatory activity, and in some conditions characterized by normal or only slightly elevated CRP concentrations, measurements of SAA concentrations could be used for monitoring disease activity and response to treatment. 3. Marked variation in the ratios of SAA to CRP concentration occurred in response to different stimuli (e.g. surgical trauma/immunological tissue injury), suggesting the existence of independent, disease-specific pathways of regulation for the serum concentrations of SAA and CRP.

Detection of novel truncated forms of human serum amyloid A protein in human plasma

FEBS Letters ◽  
2003 ◽  
Vol 537 (1-3) ◽  
pp. 166-170 ◽  
Author(s):  
Urban A. Kiernan ◽  
Kemmons A. Tubbs ◽  
Dobrin Nedelkov ◽  
Eric E. Niederkofler ◽  
Randall W. Nelson
Keyword(s):  
Human Serum ◽  
Human Plasma ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Serum Amyloid A Protein

scholarly journals Phosphorylation of human serum amyloid A protein by protein kinase C

1988 ◽  
Vol 255 (1) ◽  
pp. 29-34 ◽  
Author(s):  
A E Nel ◽  
M C De Beer ◽  
E G Shephard ◽  
A F Strachan ◽  
M L Vandenplas ◽  
...  
Keyword(s):  
Protein Kinase C ◽  
Protein Kinase ◽  
Acute Phase ◽  
Serum Amyloid A ◽  
Density Lipoprotein ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Kinase C ◽  
Serum Amyloid A Protein

Monokine-induced hepatic secretion of serum amyloid A protein (apo-SAA), an acute-phase reactant, is followed by rapid association with high-density lipoprotein (HDL) in plasma. Plasma clearance of apo-SAA is more rapid than any of the other HDL apolipoproteins. It has been shown that, of the acute-phase HDL3 apolipoproteins, apo-SAA preferentially associates with neutrophil membranes. HDL apolipoproteins have been shown to activate protein kinase C in endothelial cells. We therefore investigated potential phosphorylation of HDL3 apolipoproteins by protein kinase C. Apo-SAA was the only apolipoprotein phosphorylated (Km = 12 mM). Phosphorylation of the apo-SAA-containing HDL3 particle was selective for the more basic isoforms of apo-SAA (pI 7.0, 7.4, 7.5 and 8.0), with more acidic isoforms being phosphorylated when delipidated acute-phase apolipoproteins were used as substrate. However, phosphorylation was not in itself responsible for the establishment of the apo-SAA isoforms.

Serum Amyloid A Protein Generates Preβ1 High-Density Lipoprotein from α-Migrating High-Density Lipoprotein†

Biochemistry ◽  
1999 ◽  
Vol 38 (51) ◽  
pp. 16958-16962 ◽  
Author(s):  
Takashi Miida ◽  
Toshiyuki Yamada ◽  
Toru Yamadera ◽  
Kazuyuki Ozaki ◽  
Koichi Inano ◽  
...  
Keyword(s):  
High Density Lipoprotein ◽  
Serum Amyloid A ◽  
Density Lipoprotein ◽  
High Density ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Serum Amyloid A Protein

scholarly journals Some properties of antisera to serum amyloid A protein (SAA): inhibition of precipitation by complexing of SAA to albumin.

1976 ◽  
Vol 144 (6) ◽  
pp. 1679-1682 ◽  
Author(s):  
E C Franklin
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Terminal Region ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Serum Component ◽  
Carboxy Terminal Region ◽  
Carboxy Terminal

Three potent rabbit antisera to human serum amyloid A protein (SAA) appear to be directed exclusibely to the carboxy terminal region not shared with the tissue amyloid A protein. Since binding to albumin completely blocks the reaction of these antisera with the antigen, and since SAA exists in serum complexed to albumin, the anti-SAA cannot be used to detect or quantitate this serum component. The possibility that similar problems will be encountered with immunoassays for molecules that exist complexed to other proteins is discussed.

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