Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
1980-9-26
pubmed:abstractText
Monoclonal IgG1 anti-SRBC has been used to study the binding of monomeric and aggregated IgG1 to Fc receptors on mouse macrophages. Aggregated IgG1 was found to bind to Fc receptors on two macrophage cell lines and on primary macrophages. It competes for binding with IgG2b and not IgG2a. Like the binding of IgG2b, the binding of IgG1 is unaltered at 4 degrees C and is insensitive to trypsin or cytochalasin B. Antigen-bound IgG1, like IgG2b and IgG2a, mediates phagocytosis. Variant macrophage cell lines selected for the loss of phagocytosis through the IgG2b receptor no longer phagocytize IgG1 bearing SRBC. Monomeric IgG1 did not bind to either macrophage lines or primary macrophages. We conclude from these experiments that antigen-activated IgG1 binds to the same receptor as IgG2b.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Aug
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:volume
125
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
631-3
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
IgG1 and IgG2b share the Fc receptor on mouse macrophages.
pubmed:publicationType
Journal Article, Research Support, U.S. Gov't, P.H.S., Research Support, U.S. Gov't, Non-P.H.S.