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Endothelial Cells Promote Anti‐CD3‐Induced T‐cell Proliferation via Cell‐Cell Contact Mediated by LFA‐1 and CD2
Author(s) -
WESTPHAL J. R.,
WILLEMS H. W.,
TAX W. J. M.,
KOENE R. A. P.,
RUITER D. J.,
WAAL R. M. W.
Publication year - 1993
Publication title -
scandinavian journal of immunology
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.934
H-Index - 88
eISSN - 1365-3083
pISSN - 0300-9475
DOI - 10.1111/j.1365-3083.1993.tb02585.x
Subject(s) - t cell , cd3 , t cell receptor , microbiology and biotechnology , lymphocyte function associated antigen 1 , monoclonal antibody , cell adhesion molecule , cell adhesion , neural cell adhesion molecule , biology , cell–cell interaction , in vitro , chemistry , antibody , cell , antigen , immunology , intercellular adhesion molecule 1 , biochemistry , immune system , cd8
T‐cell activation requires not only T‐cell receptor (TCR) engagement and subsequent TCR/CD3 cross‐linking, but also one or more secondary activation signals generated by accessory cells (AC). We investigated the accessory function endothelial cells (EC) in an in vitro model for T‐cell activation where the first cross‐linking signal was delivered to peripheral human T lymphocytes by cither immobilized anti‐CD3 monoclonal antibody (MoAb) or by PHA. In a previous report, we showed that EC provided a potent costimulatory signal in this model system. We have now analysed the nature of the EC‐derived costirnulatory signal by testing whether EC could be substituted by cy lokines. by studying the effect of EC fixation and by testing the involvement of a number of adhesion molecules. Our findings indicate that EC accessory function is mediated mainly by membrane‐bound factors. The nature of these membrane‐bound factors was analysed by studying the inhibitory properties of a series of MoAbs directed against several adhesion molecules. Antibodies directed against CD44, E‐selectin, CD31, CD26, B7/BBI, VLA‐4 or VCAM‐1 were not inhibitory. However, an inhibition, was clearly observed with antibodies against LFA‐1 and CD2. Remarkably, this inhibition was not found with MoAbs to their respective counterstructures ICAM‐1 and LFA‐3. In summary, we postulate that both LFA‐l/ICAM‐1, and CD2 LFA‐3 interactions are involved in EC accessory function, although the role of the EC‐associated adhesion partners is not fully understood.