Linked Life Data

2137491

Source:http://linkedlifedata.com/resource/pubmed/id/2137491

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
1990-3-23
pubmed:abstractText
In this report, we present data on the activation of different neutrophil effector functions by two distinct Fc-gamma receptors, FcRII and FcRIII. We and others have shown previously that IgG-dependent activation of phagocytosis and superoxide generation is mediated via FcRII. IgG-dependent exocytosis of granule proteins was assessed with Staphylococcus aureus Oxford opsonized with human IgG or with IgG-coated latex. Both anti-FcRII mAb and anti-FcRIII-F(ab')2 mAb inhibited this release, whereas the combination of these mAb inhibited this process more strongly than either mAb alone. This indicates that both FcRII and FcRIII are involved in IgG-dependent release of granule proteins. Cross-linking of the receptors by anti-FcR mAb and F(ab')2 fragments of goat-anti-mouse-Ig showed again that both FcRII and FcRIII mediate lysozyme release, whereas cross-linking of a control antigen (CD67) did not. By measuring the release of elastase and lactoferrin, we found that cross-linking of either FcRII or FcRIII induced release of both azurophilic and specific granules. Under these conditions, we did not measure any activation of the respiratory burst. When FcRIII was removed by treatment of neutrophils with glycosylphosphatidylinositol-specific phospholipase C, the lysozyme release induced by cross-linking of FcRIII was lower than the release from control neutrophils, whereas the release induced by cross-linking of FcRII was similar. Therefore, we conclude that IgG-dependent activation of neutrophils follows two distinct pathways: one via transmembrane FcRII, activating both the NADPH oxidase and the release of granule proteins (as was demonstrated previously by us and by others), and the other via phosphatidylinositol-linked FcRIII, activating exocytosis of granule proteins.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Feb
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:day
15
pubmed:volume
144
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
1432-7
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed-meshheading:2137491-Antibodies, Monoclonal, pubmed-meshheading:2137491-Antigens, Differentiation, pubmed-meshheading:2137491-Cell Degranulation, pubmed-meshheading:2137491-Enzyme Activation, pubmed-meshheading:2137491-Hemoglobinuria, Paroxysmal, pubmed-meshheading:2137491-Humans, pubmed-meshheading:2137491-Immunologic Techniques, pubmed-meshheading:2137491-Lactoferrin, pubmed-meshheading:2137491-Muramidase, pubmed-meshheading:2137491-NADH, NADPH Oxidoreductases, pubmed-meshheading:2137491-NADPH Oxidase, pubmed-meshheading:2137491-Neutrophils, pubmed-meshheading:2137491-Pancreatic Elastase, pubmed-meshheading:2137491-Phosphatidylinositols, pubmed-meshheading:2137491-Receptor Aggregation, pubmed-meshheading:2137491-Receptors, Fc, pubmed-meshheading:2137491-Receptors, IgG, pubmed-meshheading:2137491-Signal Transduction
pubmed:year
1990
pubmed:articleTitle
Phosphatidylinositol-linked FcRIII mediates exocytosis of neutrophil granule proteins, but does not mediate initiation of the respiratory burst.
pubmed:affiliation
Central Laboratory of the Netherlands Red Cross Blood Transfusion Service, Amsterdam.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't