CD99 activates T cells via a costimulatory function that promotes raft association of TCR complex and tyrosine phosphorylation of TCR zeta.
- Author:
Kwon Ik OH
1
;
Byoung Kwon KIM
;
Young Larn BAN
;
Eun Young CHOI
;
Kyeong Cheon JUNG
;
Im Soon LEE
;
Seong Hoe PARK
Author Information
1. Department of Pathology, Hallym University College of Medicine, Chuncheon 200-702, Korea.
- Publication Type:Original Article ; Research Support, Non-U.S. Gov't
- Keywords:
antigens;
lymphocyte activation;
receptors, antigen, T-cell;
signal transduction;
T lymphocytes
- MeSH:
Antigens, CD/*immunology;
Antigens, CD3/immunology;
Cell Adhesion Molecules/*immunology;
Down-Regulation;
Humans;
Jurkat Cells;
Lymphocyte Activation/*immunology;
Membrane Microdomains/*immunology;
Membrane Proteins/*immunology;
Phosphorylation;
Phosphotyrosine/*metabolism;
Protein Transport;
Receptors, Antigen, T-Cell/*immunology;
T-Lymphocytes/*immunology
- From:Experimental & Molecular Medicine
2007;39(2):176-184
- CountryRepublic of Korea
- Language:English
-
Abstract:
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.
