| First Author | Berg NN | Year | 1995 |
| Journal | J Immunol | Volume | 155 |
| Issue | 4 | Pages | 1694-702 |
| PubMed ID | 7636228 | Mgi Jnum | J:28062 |
| Mgi Id | MGI:75692 | Doi | 10.4049/jimmunol.155.4.1694 |
| Citation | Berg NN, et al. (1995) Characterization of intercellular adhesion molecule-1 (ICAM-1)-augmented degranulation by cytotoxic T cells. ICAM-1 and anti-CD3 must be co-localized for optimal adhesion and stimulation. J Immunol 155(4):1694-702 |
| abstractText | Purified intercellular adhesion molecule-1 (ICAM-1), a ligand of the LFA-1, was used to analyze the contribution of ICAM-1 to the activation of CTL. ICAM-1 facilitates degranulation when co-immobilized with substimulatory amounts of anti-CD3. This facilitated response is most likely mediated through LFA-1, since Abs to this molecule significantly inhibit the response, Interestingly, when ICAM-1 and anti-CD3 are immobilized on separate beads and presented to the CTL, no ICAM-1-enhanced degranulation is observed. The ICAM-1 and anti-CD3 must be immobilized on the same surface to augment the response, suggesting that ICAM-1 either does not transmit signals into the cell or it transmits a very localized signal, since the ICAM-1 and anti-CD3 must be juxtaposed. Consistent with this finding, we demonstrate that ICAM-1 does not induce tyrosine phosphorylation or a Ca(2+)-flux in the CTL clone, but does potentiate these responses when co-immobilized with substimulatory anti-CD3. Finally ICAM-1 and anti-CD3 must be immobilized on the same bead for stable adhesion of CTL to ICAM-1. When ICAM-1 and anti-CD3 are immobilized on separate beads, there is only a transient, low level of adhesion to the ICAM-1 beads. Taken together, these results suggest that LFA-1 is acting principally as an adhesion molecule, with respect to ICAM-1, in CTL and that this adhesion is regulated through the TCR complex. |
