Linked Life Data

20937257

Source:http://linkedlifedata.com/resource/pubmed/id/20937257

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
2
pubmed:dateCreated
2010-11-15
pubmed:abstractText
Engagement of Fc? receptors on leukocytes by immune complexes induces both cytokine production and immune complex internalization. The relationship between these processes is unclear. In many disease states, Fc? receptors encounter their ligands in deposited forms that cannot be readily internalized. In this study, we examined the kinetics of ERK1/2 phosphorylation and TNF-? secretion in primary human monocytes in response to soluble heat-aggregated IgG or surface-bound IgG, to mimic soluble immune complexes and tissue-deposited IgG, respectively. Soluble aggregated IgG induced transient signaling, leading to peak phosphorylation of ERK1/2 by 15 min and peak TNF-? levels by 1h, whereas surface-bound IgG caused sustained responses over the course of several hours. Treatment with the vacuolar ATPase inhibitor bafilomycin led to increased persistence of ERK1/2 phosphorylation in response to aggregated IgG. When monocytes were incubated with both soluble aggregated IgG and surface-bound IgG simultaneously, ERK1/2 phosphorylation was transient. These results suggest that Fc? receptor internalization is an important step in termination of inflammatory signaling, and that small immune complexes can exert an overall down-modulatory effect when encountered in the presence of immobilized IgG.
pubmed:grant
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Nov
pubmed:issn
1090-2104
pubmed:author
pubmed:copyrightInfo
Copyright © 2010 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
12
pubmed:volume
402
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
301-4
pubmed:meshHeading
pubmed:year
2010
pubmed:articleTitle
ERK phosphorylation and tumor necrosis factor-alpha production by monocytes are persistent in response to immobilized IgG.
pubmed:affiliation
Department of Immunology, University of Toronto, Medical Sciences Building, 1 King’s College Circle, Toronto, Ontario, Canada.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't