Linked Life Data

9252455

Source:http://linkedlifedata.com/resource/pubmed/id/9252455

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
1 Pt 1
pubmed:dateCreated
1997-9-3
pubmed:abstractText
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.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
0002-9513
pubmed:author
pubmed:issnType
Print
pubmed:volume
273
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
C179-87
pubmed:dateRevised
2006-11-15
pubmed:meshHeading
pubmed-meshheading:9252455-Animals, pubmed-meshheading:9252455-Antibodies, Monoclonal, pubmed-meshheading:9252455-Antigens, CD29, pubmed-meshheading:9252455-Apolipoproteins, pubmed-meshheading:9252455-Calcium, pubmed-meshheading:9252455-Cell Adhesion, pubmed-meshheading:9252455-Cell Line, pubmed-meshheading:9252455-Extracellular Matrix, pubmed-meshheading:9252455-Flow Cytometry, pubmed-meshheading:9252455-Humans, pubmed-meshheading:9252455-Kinetics, pubmed-meshheading:9252455-Mast Cells, pubmed-meshheading:9252455-Mice, pubmed-meshheading:9252455-Oligopeptides, pubmed-meshheading:9252455-Peptide Fragments, pubmed-meshheading:9252455-Protein Binding, pubmed-meshheading:9252455-Protein Precursors, pubmed-meshheading:9252455-Recombinant Proteins, pubmed-meshheading:9252455-Serum Amyloid A Protein
pubmed:year
1997
pubmed:articleTitle
Extracellular matrix-anchored serum amyloid A preferentially induces mast cell adhesion.
pubmed:affiliation
Department of Medicine, Meir General Hospital, Kfar-Saba, Israel.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't