Cytotoxic T lymphocyte (CTL)-mediated cytotoxicity constitutes an important component of specific effector mechanisms in immuno-surveillance against virus-infected or transformed cells. Two mechanisms appear to account for this activity, one of which is the perforin-based process. Independently, a FAS-based mechanism involves the transducing molecule FAS (also designated APO-1) and its ligand (FAS-L). The human FAS protein is a cell surface glycoprotein that belongs to a family of receptors that includes CD40, nerve growth factor receptors and tumor necrosis factor receptors. The FAS antigen is expressed on a broad range of lymphoid cell lines, certain of which undergo apoptosis in response to treatment with antibody to FAS. These findings strongly imply that targeted cell death is potentially mediated by the intercellular interactions of FAS with its ligand or effectors, and that FAS may be critically involved in CTL-mediated cytotoxicity.
