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Predicate | Object |
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rdf:type | |
lifeskim:mentions | |
pubmed:issue |
5
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pubmed:dateCreated |
1998-12-3
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pubmed:abstractText |
Serum amyloid A (SAA) is an acute phase reactant whose levels in the blood rise as part of the body's response to stress and inflammation. Previous studies have suggested that SAA may carry an anti-inflammatory potential. We evaluated the effects of SAA on human neutrophils activated by N-formyl-methionyl-leucyl-phenylalanine (fMLP) in vitro. At concentrations higher than 10 microg/mL, SAA inhibited neutrophil myeloperoxidase (MPO) release. This effect was located in the N-terminal--that is, amino acid residues 1-14--of the SAA molecule. Directed neutrophil migration was inhibited at the same SAA concentrations. Several amino acid residues (1-14, 15-104, 83-104) contributed to this effect. Neutrophil O2- production was inhibited at low concentrations of SAA (0.1 to 1 microg/ml) and was stimulated at concentrations higher than 50 microg/mL. Neutrophil O2- production induced by phorbol myristate acetate (PMA) and O2- generated by the xanthine-xanthine oxidase reaction were not affected by SAA. These results add to previous data suggesting that SAA, at concentrations recorded in the serum during inflammation, modulates neutrophil function; thus it may play a role in the down-regulation of the inflammatory process.
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pubmed:language |
eng
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pubmed:journal | |
pubmed:citationSubset |
AIM
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pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/N-Formylmethionine...,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Peroxidase,
http://linkedlifedata.com/resource/pubmed/chemical/Recombinant Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Serum Amyloid A Protein,
http://linkedlifedata.com/resource/pubmed/chemical/Superoxides
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pubmed:status |
MEDLINE
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pubmed:month |
Nov
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pubmed:issn |
0022-2143
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pubmed:author | |
pubmed:issnType |
Print
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pubmed:volume |
132
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pubmed:owner |
NLM
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pubmed:authorsComplete |
Y
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pubmed:pagination |
414-20
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pubmed:dateRevised |
2006-11-15
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pubmed:meshHeading |
pubmed-meshheading:9823935-Adult,
pubmed-meshheading:9823935-Cell Degranulation,
pubmed-meshheading:9823935-Chemotaxis, Leukocyte,
pubmed-meshheading:9823935-Dose-Response Relationship, Drug,
pubmed-meshheading:9823935-Female,
pubmed-meshheading:9823935-Humans,
pubmed-meshheading:9823935-Male,
pubmed-meshheading:9823935-N-Formylmethionine Leucyl-Phenylalanine,
pubmed-meshheading:9823935-Neutrophil Activation,
pubmed-meshheading:9823935-Neutrophils,
pubmed-meshheading:9823935-Peptide Fragments,
pubmed-meshheading:9823935-Peroxidase,
pubmed-meshheading:9823935-Recombinant Proteins,
pubmed-meshheading:9823935-Serum Amyloid A Protein,
pubmed-meshheading:9823935-Superoxides
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pubmed:year |
1998
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pubmed:articleTitle |
Effect of serum amyloid A on selected in vitro functions of isolated human neutrophils.
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pubmed:affiliation |
Hematology Unit, Hadassah University Hospital, Mount Scopus, Jerusalem, Israel.
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pubmed:publicationType |
Journal Article,
In Vitro,
Research Support, Non-U.S. Gov't
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