A study of extracellular matrix-cell adhesion peptidic epitopes related to human serum amyloid A (SAA)

1999 ◽  
Vol 6 (2-3) ◽  
pp. 99-108
Author(s):  
Liana Preciado-Patt ◽  
Rami Hershkovitz ◽  
Ofer Lider ◽  
Susanne Feiertag ◽  
Günther Jung ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Cell Adhesion ◽  
Human Serum ◽  
Serum Amyloid A ◽  
Serum Amyloid ◽  
Amyloid A ◽  
Matrix Cell

Extracellular matrix-anchored serum amyloid A preferentially induces mast cell adhesion

1997 ◽  
Vol 273 (1) ◽  
pp. C179-C187 ◽  
Author(s):  
R. Hershkoviz ◽  
L. Preciado-Patt ◽  
O. Lider ◽  
M. Fridkin ◽  
J. Dastych ◽  
...  
Keyword(s):  
Extracellular Matrix ◽  
Mast Cell ◽  
Cell Adhesion ◽  
Amino Acid ◽  
Mast Cells ◽  
Serum Amyloid A ◽  
Immune Cell ◽  
Serum Amyloid ◽  
Amino Acid Residues ◽  
Amyloid A

Mast cells are known to accumulate in various inflammatory processes, some of which are known to be associated with increased local and systemic levels of acute-phase reactants such as serum amyloid A (SAA) or with amyloid deposition. The mechanism(s) by which mast cells are recruited to these sites, however, has not been fully elucidated. It has recently been shown that SAA interacts with extracellular matrix (ECM) components and thereby acts as a chemoattractant and regulator of immune cell migration. On the basis of these observations, we examined the effect of SAA on mast cell adhesion to ECM, an essential step in cellular transmigration. We could first demonstrate strong specific binding of recombinant human SAA (rSAA) to murine mast cells using flow cytometry. Moreover, radiolabeled rSAA was found to bind, in a saturable manner, to mast cells, reaching a binding affinity of 10(-8) M. When immobilized by preincubation with ECM, SAA or its proteolytically degraded amyloid A fragment (amino acid residues 2-82), which contains RGD-related adhesion motif but not the COOH-terminal portion of SAA (amino acid residues 77-104), induced the adhesion of resting mast cells to ECM or laminin. SAA and AA, in soluble or immobilized forms, did not activate mast cells to release mediators. Mast cell adhesion to the immobilized ECM-SAA complex appeared to occur through an integrin recognition, inasmuch as adhesion was calcium dependent and could be blocked by an RGD-containing peptide or by anti-CD29 monoclonal antibody. Genistein also inhibited adhesion, indicating that tyrosine kinase activity was involved. These data suggest that SAA bound to ECM may serve as an important inducer of mast cell adhesion, thus regulating mast cell recruitment and accumulation at these sites, which in turn could potentiate further pathology.

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
Sign in / Sign up

Export Citation Format

Share Document