CD99 activates T cells via a costimulatory function that promotes raft association of TCR complex and tyrosine phosphorylation of TCR zeta
Experimental & Molecular Medicine
; : 176-184, 2007.
Article
in English
| WPRIM (Western Pacific)
| ID: wpr-90615
Responsible library:
WPRO
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.
Full text:
Available
Database:
WPRIM (Western Pacific)
Main subject:
Phosphorylation
/
Lymphocyte Activation
/
Receptors, Antigen, T-Cell
/
T-Lymphocytes
/
Antigens, CD
/
Cell Adhesion Molecules
/
Down-Regulation
/
CD3 Complex
/
Phosphotyrosine
/
Jurkat Cells
Limits:
Humans
Language:
English
Journal:
Experimental & Molecular Medicine
Year:
2007
Document type:
Article