Linked Life Data

21683687

Source:http://linkedlifedata.com/resource/pubmed/id/21683687

Statements in which the resource exists as a subject.
PredicateObject
rdf:type
lifeskim:mentions
pubmed:issue
4
pubmed:dateCreated
2011-7-18
pubmed:abstractText
The high affinity IgE Fc receptor (Fc?RI) ? chain is well implicated as a signal amplifier through the immunoreceptor tyrosine-based activation motif (ITAM) in its C-terminal intracellular region. Our previous study, however, demonstrated that mutation in all of the three tyrosine residues within the Fc?RI? ITAM did not impair Fc?RI-induced cytokine production, suggesting a possible functional region other than the ITAM. To investigate the ITAM-independent mechanism by which Fc?RI? regulates Fc?RI-induced cytokine production, mouse mast cells expressing various Fc?RI? mutants were generated. We observed that truncation of the Fc?RI? C-terminus downstream of the ITAM resulted in a considerable decrease in Fc?RI-induced IL-6 production but not degranulation. Furthermore, mutagenesis of a single C-terminal aspartic acid (D234) to alanine (?-D234A) also significantly impaired IL-6 production. In addition, the similarity between the circular dichroism (CD) spectra of the wild type and ?-D234A suggests that the secondary structure of the Fc?RI? C-terminus was not affected by the D234A mutation. Consistently, we did not observe any effect of this mutation on Fc?RI-induced tyrosine phosphorylation of Fc?RI?. These observations strongly suggest a novel signaling pathway mediated by the cytoplasmic tail downstream of the Fc?RI? ITAM.
pubmed:language
eng
pubmed:journal
pubmed:citationSubset
IM
pubmed:chemical
pubmed:status
MEDLINE
pubmed:month
Jul
pubmed:issn
1090-2104
pubmed:author
pubmed:copyrightInfo
Copyright © 2011 Elsevier Inc. All rights reserved.
pubmed:issnType
Electronic
pubmed:day
15
pubmed:volume
410
pubmed:owner
NLM
pubmed:authorsComplete
Y
pubmed:pagination
744-8
pubmed:meshHeading
pubmed:year
2011
pubmed:articleTitle
Fc?RI-induced mast cell cytokine production critically involves an aspartic acid residue (D234) in the C-terminal intracellular domain of the Fc?RI? chain.
pubmed:affiliation
Division of Molecular Cell Immunology and Allergology, Nihon University Graduate School of Medical Science, Tokyo, Japan.
pubmed:publicationType
Journal Article, Research Support, Non-U.S. Gov't