rdf:type |
|
lifeskim:mentions |
umls-concept:C0004083,
umls-concept:C0033414,
umls-concept:C0034790,
umls-concept:C0039194,
umls-concept:C0439855,
umls-concept:C0542341,
umls-concept:C1417157,
umls-concept:C1515877,
umls-concept:C1519726,
umls-concept:C1719914,
umls-concept:C1879547,
umls-concept:C2828406
|
pubmed:issue |
2
|
pubmed:dateCreated |
2007-4-27
|
pubmed:abstractText |
We investigated the co-stimulatory role of a cell-surface protein, CD99. Co-ligation of CD99 and suboptimal CD3 induced T-cell activation to a level comparable to that obtained with optimal CD3 or CD3+CD28. We also noted concomitant enhancement of the earliest T-cell receptor (TCR) signaling events. In addition, co-ligation of CD99 and CD3 led to translocation of TCR complexes into the lipid raft, without concomitant migration of CD99 to the raft, and consequent enhancement of TCR zeta-mediated signal 1. These data demonstrate the unique properties of CD99 co-stimulation that distinguish this molecule from CD28 and other raft-resident co-stimulatory factors.
|
pubmed:language |
eng
|
pubmed:journal |
|
pubmed:citationSubset |
IM
|
pubmed:chemical |
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD,
http://linkedlifedata.com/resource/pubmed/chemical/Antigens, CD3,
http://linkedlifedata.com/resource/pubmed/chemical/CD99 protein, human,
http://linkedlifedata.com/resource/pubmed/chemical/Cell Adhesion Molecules,
http://linkedlifedata.com/resource/pubmed/chemical/Membrane Proteins,
http://linkedlifedata.com/resource/pubmed/chemical/Phosphotyrosine,
http://linkedlifedata.com/resource/pubmed/chemical/Receptors, Antigen, T-Cell,
http://linkedlifedata.com/resource/pubmed/chemical/antigen T cell receptor, zeta chain
|
pubmed:status |
MEDLINE
|
pubmed:month |
Apr
|
pubmed:issn |
1226-3613
|
pubmed:author |
|
pubmed:issnType |
Print
|
pubmed:day |
30
|
pubmed:volume |
39
|
pubmed:owner |
NLM
|
pubmed:authorsComplete |
Y
|
pubmed:pagination |
176-84
|
pubmed:dateRevised |
2010-9-1
|
pubmed:meshHeading |
pubmed-meshheading:17464179-Antigens, CD,
pubmed-meshheading:17464179-Antigens, CD3,
pubmed-meshheading:17464179-Cell Adhesion Molecules,
pubmed-meshheading:17464179-Down-Regulation,
pubmed-meshheading:17464179-Humans,
pubmed-meshheading:17464179-Jurkat Cells,
pubmed-meshheading:17464179-Lymphocyte Activation,
pubmed-meshheading:17464179-Membrane Microdomains,
pubmed-meshheading:17464179-Membrane Proteins,
pubmed-meshheading:17464179-Phosphorylation,
pubmed-meshheading:17464179-Phosphotyrosine,
pubmed-meshheading:17464179-Protein Transport,
pubmed-meshheading:17464179-Receptors, Antigen, T-Cell,
pubmed-meshheading:17464179-T-Lymphocytes
|
pubmed:year |
2007
|
pubmed:articleTitle |
CD99 activates T cells via a costimulatory function that promotes raft association of TCR complex and tyrosine phosphorylation of TCR zeta.
|
pubmed:affiliation |
Department of Pathology, Hallym University College of Medicine, Chuncheon 200-702, Korea.
|
pubmed:publicationType |
Journal Article,
Research Support, Non-U.S. Gov't
|