In vitro Evaluation of an Enhanced Human Serum Amyloid A (SAA2 ) Promoter-Regulated Soluble TNF Receptor Fusion Protein for Anti-Inflammatory Gene Therapy

2001 ◽  
Vol 53 (6) ◽  
pp. 588-595 ◽  
Author(s):  
M. Rygg ◽  
C. M. Uhlar ◽  
C. Thorn ◽  
L. E. Jensen ◽  
D. J. Gaughan ◽  
...  
Keyword(s):  
Gene Therapy ◽  
Fusion Protein ◽  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Tnf Receptor ◽  
In Vitro Evaluation ◽  
Amyloid A ◽  
Soluble Tnf Receptor

Abstract 226: Serum Amyloid A Isoforms and the Capacity to Mediate Cholesterol Efflux

2014 ◽  
Vol 34 (suppl_1) ◽  
Author(s):  
Hussein Yassine ◽  
Olgica Trenchevska ◽  
Chad Borges ◽  
Dobrin Nedelkov ◽  
Randall W Nelson ◽  
...  
Keyword(s):  
Cholesterol Efflux ◽  
Serum Amyloid A ◽  
Hdl Cholesterol ◽  
Acute Phase Reactant ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Cholesterol Levels ◽  
Acute Phase Reactant Protein

Serum Amyloid A (SAA) is an acute phase reactant protein that exists in multiple isoforms, can form HDL, and participates in cholesterol efflux. In vitro studies suggest that the SAA 2.1 isoform has an increased capacity to mediate cholesterol efflux compared to the other isoforms. We examined SAA isoforms using a novel mass spectrometric immunoassay (MSIA) and HDL’s cholesterol efflux capacity (via ABCA-1 and SR-BI) in samples from 59 subjects with (n=33) and without type 2 diabetes (n=26). SAA 1.1 levels were detectable in 58, SAA 2.1 in 14 and SAA 2.2 in 36 of the 59 subjects. SAA 2.1 levels significantly correlated with SR-BI cholesterol efflux (r=0.71, p=0.01, n=14), but not ABCA-1 mediated efflux (r=0.1, P=0.1). This correlation was not explained by changes in HDL phospholipids, Apo A-I or HDL cholesterol levels. In contrast, SAA 2.2 or 1.1 levels did not correlate with changes in SR-BI or ABCA-1 mediated efflux. Although the SAA 2.1 isoform is less frequently detected in plasma, our data confirm that it is closely linked with HDL mediated cholesterol efflux, particularly that is SR-BI mediated.

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
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