Source:http://linkedlifedata.com/resource/pubmed/id/15549775
Switch to
Predicate | Object |
---|---|
rdf:type | |
lifeskim:mentions | |
pubmed:issue |
12
|
pubmed:dateCreated |
2004-12-1
|
pubmed:abstractText |
Altered peptide ligands derived from T cell-reactive self antigens have been shown to be protective therapeutic agents in animal models of autoimmunity. In this study we identified several altered peptide ligands derived from the type 1 diabetes-associated autoantigen human glutamic acid decarboxylase 65 (hGAD65) epitope that were capable of antagonizing a subset of a panel of human CD4(+) GAD65 (555-567)-responsive T cell clones derived from a diabetic individual. While no altered peptide ligand was able to antagonize all six clones in the T cell panel, a single-substituted peptide of isoleucine to methionine at position 561, which resides at the TCR contact p5 position, was able to antagonize five out of the six hGAD65-responsive clones. In a mixed T cell culture system we observed that altered peptide ligand-mediated antagonism is inhibited in a dose-dependent manner by the presence of non-antagonizable hGAD65 (555-567)-responsive T cells. From an analysis of the cytokines present in the mixed T cell cultures, interleukin-2 was sufficient to inhibit altered peptide ligand-induced antagonism. The inhibition of altered peptide ligand-mediated antagonism of self-antigen-responsive T cells by non-antagonizable T cells has implications in altered peptide ligand therapy where T cell antagonism is the goal.
|
pubmed:grant | |
pubmed:language |
eng
|
pubmed:journal | |
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Epitopes,
http://linkedlifedata.com/resource/pubmed/chemical/Glutamate Decarboxylase,
http://linkedlifedata.com/resource/pubmed/chemical/Interleukin-2,
http://linkedlifedata.com/resource/pubmed/chemical/Isoenzymes,
http://linkedlifedata.com/resource/pubmed/chemical/Ligands,
http://linkedlifedata.com/resource/pubmed/chemical/Peptide Fragments,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/glutamate decarboxylase 2
|
pubmed:status |
MEDLINE
|
pubmed:month |
Dec
|
pubmed:issn |
0014-2980
|
pubmed:author | |
pubmed:issnType |
Print
|
pubmed:volume |
34
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
3337-45
|
pubmed:dateRevised |
2007-11-14
|
pubmed:meshHeading |
pubmed-meshheading:15549775-Autoimmunity,
pubmed-meshheading:15549775-CD4-Positive T-Lymphocytes,
pubmed-meshheading:15549775-Diabetes Mellitus, Type 1,
pubmed-meshheading:15549775-Epitopes,
pubmed-meshheading:15549775-Glutamate Decarboxylase,
pubmed-meshheading:15549775-Humans,
pubmed-meshheading:15549775-Interleukin-2,
pubmed-meshheading:15549775-Isoenzymes,
pubmed-meshheading:15549775-Ligands,
pubmed-meshheading:15549775-Peptide Fragments,
pubmed-meshheading:15549775-Receptors, Antigen, T-Cell,
pubmed-meshheading:15549775-T-Lymphocyte Subsets
|
pubmed:year |
2004
|
pubmed:articleTitle |
Inhibition of altered peptide ligand-mediated antagonism of human GAD65-responsive CD4+ T cells by non-antagonizable T cells.
|
pubmed:affiliation |
Benaroya Research Institute at Virginia Mason, Seattle, USA. jgebe@benaroyaresearch.org
|
pubmed:publicationType |
Journal Article,
Research Support, U.S. Gov't, P.H.S.
|