The adhesion of human T lymphoblasts to ICAM-1-expressing normal dermal fibroblasts has been assessed as a sensitive model system for the analysis of the interaction of the leucocyte integrin LFA-1 with its counter-receptor ICAM-1. Using this model system, the effects of factors known to regulate the activity of LFA-1 have been quantitated: temperature; concentration of divalent cations; and exposure to phorbol esters. We show here that under the appropriate assay conditions, this model system represents a useful and simple alternative to the detection of leucocyte binding to purified ICAM-1 and also has the additional advantage of permitting more sensitive quantification than is possible using the homotypic adhesion assay.