IL-6 plays a critical role in the synergistic induction of human serum amyloid A (SAA) gene when stimulated with proinflammatory cytokines as analyzed with an SAA isoform real-time quantitative RT-PCR assay system

2004 ◽  
Vol 314 (2) ◽  
pp. 363-369 ◽  
Author(s):  
Keisuke Hagihara ◽  
Teppei Nishikawa ◽  
Tomoyasu Isobe ◽  
Jian Song ◽  
Yasuhiro Sugamata ◽  
...  
Keyword(s):  
Human Serum ◽  
Real Time ◽  
Proinflammatory Cytokines ◽  
Serum Amyloid A ◽  
Critical Role ◽  
Serum Amyloid ◽  
Rt Pcr ◽  
Pcr Assay ◽  
Amyloid A ◽  
Synergistic Induction

Genetic Isofocusing Variant of Human Serum Amyloid A

1991 ◽  
pp. 20-23
Author(s):  
A. Steinmetz ◽  
H. Vitt ◽  
S. Motzny ◽  
H. Kaffarnik
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

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.

Structural requirements of glycosaminoglycans for facilitating amyloid fibril formation of human serum amyloid A

Amyloid ◽  
2016 ◽  
Vol 23 (2) ◽  
pp. 67-75 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Aki Yamamoto ◽  
Shiori Watanabe ◽  
Sanae Takahashi ◽  
...  
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Amyloid Fibril ◽  
Fibril Formation ◽  
Serum Amyloid ◽  
Structural Requirements ◽  
Amyloid A ◽  
Amyloid Fibril Formation

Effect of amino acid variations in the central region of human serum amyloid A on the amyloidogenic properties

2014 ◽  
Vol 444 (1) ◽  
pp. 92-97 ◽  
Author(s):  
Hiroka Takase ◽  
Masafumi Tanaka ◽  
Sachiko Miyagawa ◽  
Toshiyuki Yamada ◽  
Takahiro Mukai
Keyword(s):  
Amino Acid ◽  
Human Serum ◽  
Central Region ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

Evaluation of a commercially available human serum amyloid A (SAA) turbidometric immunoassay for determination of equine SAA concentrations

2006 ◽  
Vol 172 (2) ◽  
pp. 315-319 ◽  
Author(s):  
S. Jacobsen ◽  
M. Kjelgaard-Hansen ◽  
H. Hagbard Petersen ◽  
A.L. Jensen
Keyword(s):  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A

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
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