Enhancement of LFA-1-mediated cell adhesion by triggering through CD2 or CD3 on T lymphocytes
Authors:
- P. van de Wiel-Van KemenadePKP. van de Wiel-Van Kemenade
- P. WederPWP. Weder
- T. W. KuijpersTKT. W. Kuijpers
- C. G. FigdorCFC. G. Figdor
- 1 December 1989
- journal article
- Published by Springer Nature in Nature
- Vol. 342 (6251) , 811-813
Abstract
The lymphocyte function-associated molecule LFA-1 (CD11a/CD18) plays a key part in lymphocyte adhesion. Lymphocytes do not adhere spontaneously; activation of protein kinase C (PKC) by phorbol esters, however, gives rise to strong LFA-1-dependent adhesion, indicating that activation of LFA-1 is required to induce cell adhesion. We have now investigated whether the functionally important CD2 and CD3 surface structures on T lymphocytes are involved in the activation of LFA-1. The stimulation of these molecules, which causes activation of PKC, strongly promoted LFA-1-dependent adhesion. Furthermore, we demonstrate by using cells from an LFA-1-deficient patient that this enhanced lymphocyte adhesion is caused by activation of the LFA-1 molecule and not by activation of its ligands. LFA-1 was persistently activated by triggering through CD2 but only transiently by triggering through CD3. We postulate that CD2 and CD3 can differentially regulate the affinity of LFA-1 for its ligands by modulating its molecular conformation through PKC-dependent mechanisms.Keywords
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