Linked Life Data

7365252

Source:http://linkedlifedata.com/resource/pubmed/id/7365252

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
5
pubmed:dateCreated
1980-6-27
pubmed:abstractText
A human mononuclear cell population, enriched with monocytes by adhering them to microexudate on Petri dishes previously used for fibroblast cultures was used in a homologous human system to form EA rosettes. IgG1, Fc, and subfragments of Fc representing the C gamma 2 and C gamma 3 domains were tested for their ability to inhibit rosette formation. Although Fc and IgG were equally effective in inhibiting rosette formation over the concentration range 10(-6) to 10(-5) M, all subfragments were inactive at these concentrations. At 10-fold higher concentrations the C gamma 2 fragment was still inactive; however, both the C gamma 3 fragments, pFc' and at C gamma 3, did show significant activity at this higher level. Reduction and alkylation diminished the inhibitory capacity of IgG 10-fold but had a lesser effect on Fc. In a parallel series of experiments the ability of IgG and Fc to inhibit granulocyte rosettes was found to be markedly diminished by reduction and alkylation in both cases. These experiments reveal differences between Fc receptors in different cells, confirm a role for the C gamma 3 homology region in monocyte Fc receptor recognition, but do suggest a requirement, either direct or indirect, for the C gamma 2 domain.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
AIM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
May
pubmed:issn
0022-1767
pubmed:author
pubmed:issnType
Print
pubmed:volume
124
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
2186-90
pubmed:dateRevised
2011-11-17
pubmed:meshHeading
pubmed:year
1980
pubmed:articleTitle
Structure and function of immunoglobulin domains. VIII. An analysis of the structural requirements in human IgG1 for binding to the Fc receptor of human monocytes.
pubmed:publicationType
Journal Article