Serum amyloid A protein (SAA): a marker for liver allograft rejection in humans

1994 ◽  
Vol 72 (12) ◽  
pp. 1007-1011 ◽  
Author(s):  
G. Feussner ◽  
C. Stech ◽  
J. Dobmeyer ◽  
H. Schaefer ◽  
G. Otto ◽  
...  
Keyword(s):  
Allograft Rejection ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Liver Allograft ◽  
Amyloid A ◽  
Serum Amyloid A Protein

CHANGES IN SERUM AMYLOID A PROTEIN AND BETA-2-MICROGLOBULIN IN ASSOCIATION WITH LIVER ALLOGRAFT REJECTION

1984 ◽  
Vol 38 (5) ◽  
pp. 551-552 ◽  
Author(s):  
C. P.J. MAURY ◽  
K. HÖCKERSTEDT ◽  
A-M. TEPPO ◽  
I. LAUTENSCHLAGER ◽  
T. M. SCHEININ
Keyword(s):  
Allograft Rejection ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Liver Allograft ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Beta 2 ◽  
Beta 2 Microglobulin

Serum Amyloid A Protein: Not a Relevant Marker for Recognition of Cardiac Allograft Rejection

2004 ◽  
Vol 78 (6) ◽  
pp. 950-951 ◽  
Author(s):  
Emmanuelle Vermes ◽  
Matthias Kirsch ◽  
Titi Farrokhi ◽  
Daniel Loisance ◽  
Pascale Fanen ◽  
...  
Keyword(s):  
Allograft Rejection ◽  
Serum Amyloid A ◽  
Cardiac Allograft ◽  
Serum Amyloid ◽  
Cardiac Allograft Rejection ◽  
Amyloid A ◽  
Serum Amyloid A Protein

scholarly journals Serum amyloid A protein is a clinically useful indicator of acute renal allograft rejection

1997 ◽  
Vol 12 (1) ◽  
pp. 161-166 ◽  
Author(s):  
A. Hartmann ◽  
T. Eide ◽  
P. Fauchald ◽  
O. Bentdal ◽  
J. Harbert ◽  
...  
Keyword(s):  
Allograft Rejection ◽  
Serum Amyloid A ◽  
Renal Allograft ◽  
Serum Amyloid ◽  
Renal Allograft Rejection ◽  
Amyloid A ◽  
Acute Renal Allograft Rejection ◽  
Serum Amyloid A Protein

scholarly journals Serum Amyloid A Protein Monitoring for Early Prediction of Kidney Allograft Rejection

Nephron ◽  
1995 ◽  
Vol 70 (1) ◽  
pp. 112-113 ◽  
Author(s):  
Martin T. Časl ◽  
Goran Bulatović ◽  
Petar Orlić ◽  
Mirjana Sabljar-Matovinović
Keyword(s):  
Allograft Rejection ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Early Prediction ◽  
Kidney Allograft ◽  
Amyloid A ◽  
Serum Amyloid A Protein ◽  
Kidney Allograft Rejection

scholarly journals Aggregation of Mouse Serum Amyloid A Protein Was Promoted by Amyloid-Enhancing Factors with the More Genetically Homologous Serum Amyloid A

2021 ◽  
Vol 22 (3) ◽  
pp. 1036
Author(s):  
Xuguang Lin ◽  
Kenichi Watanabe ◽  
Masahiro Kuragano ◽  
Kiyotaka Tokuraku
Keyword(s):  
Amino Acid ◽  
Serum Amyloid A ◽  
Animal Species ◽  
Amino Acid Sequences ◽  
Serum Amyloid ◽  
Mouse Serum ◽  
Aa Amyloidosis ◽  
Basic Residue ◽  
Amyloid A ◽  
Serum Amyloid A Protein

Amyloid A (AA) amyloidosis is a condition in which amyloid fibrils characterized by a linear morphology and a cross-β structure accumulate and are deposited extracellularly in organs, resulting in chronic inflammatory diseases and infections. The incidence of AA amyloidosis is high in humans and several animal species. Serum amyloid A (SAA) is one of the most important precursor amyloid proteins and plays a vital step in AA amyloidosis. Amyloid enhancing factor (AEF) serves as a seed for fibril formation and shortens the onset of AA amyloidosis sharply. In this study, we examined whether AEFs extracted and purified from five animal species (camel, cat, cattle, goat, and mouse) could promote mouse SAA (mSAA) protein aggregation in vitro using quantum-dot (QD) nanoprobes to visualize the aggregation. The results showed that AEFs shortened and promoted mSAA aggregation. In addition, mouse and cat AEFs showed higher mSAA aggregation-promoting activity than the camel, cattle, and goat AEFs. Interestingly, homology analysis of SAA in these five animal species revealed a more similar amino acid sequence homology between mouse and cat than between other animal species. Furthermore, a detailed comparison of amino acid sequences suggested that it was important to mSAA aggregation-promoting activity that the 48th amino acid was a basic residue (Lys) and the 125th amino acid was an acidic residue (Asp or Glu). These data imply that AA amyloidosis exhibits higher transmission activity among animals carrying genetically homologous SAA gene, and may provide a new understanding of the pathogenesis of amyloidosis.

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