Linked Life Data

549780

Source:http://linkedlifedata.com/resource/pubmed/id/549780

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
12
pubmed:dateCreated
1980-10-27
pubmed:abstractText
Mouse peritoneal macrophages were charged with IgG molecules in monomeric (mIgG), heat-aggregated (agIgG) or antigen-complexed (acIgG) form. Upon exposure to 37 degrees C, all bound IgG ligand types are redistributed on the cell surface due to the mobilization of their corresponding Fc receptor (FcR). The major findings regarding the fate of FcR on macrophages bearing IgG ligands are as follows: (a) the FcR involved in the binding of cytophilic molecules has a slow movement on the cell membrane and forms patches but never caps, while the opsonic type of FcR is rapidly capped; (b) the mobility of IgG-binding sites was temperature-dependent and was affected differently by sodium azide; this metabolic inhibitor enhances the disappearance of mIgG from the cell surface but decreases the capping and the disappearance of polymeric ligands; (c) both FcR types are probably ingested when complexed with specific ligand, and consequently, the rebinding of homologous IgG molecules is reduced, the clearing induced by agIgG or acIgG binding being much more extensive; and (d) cells cleared of their opsonic types of FcR are able to regenerate the receptor molecules with 8 h of incubation at 37 degrees C.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Dec
pubmed:issn
0014-2980
pubmed:author
pubmed:issnType
Print
pubmed:volume
9
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
985-90
pubmed:dateRevised
2008-11-21
pubmed:meshHeading
pubmed:year
1979
pubmed:articleTitle
IgG-binding sites on macrophage cell membrane. II. Mobility of Fc receptors induced by the interaction with their corresponding IgG ligands.
pubmed:publicationType
Journal Article