Functional Interactions of LFA-1, T8 and Alloantigen Surface Structures in T-Cell Mediated Cytotoxicity
Monoclonal antibodies (MAb) have provided powerful tools for dissecting the complex cellular interactions involved in the lysis of target cells by immune cytotoxic T lymphocytes (CTL). Seven distinct surface-membrane structures have been implicated to function in the cytolytic process mediated by human effector cells by virtue of the ability of their MAb to inhibit cytolysis in the absence of complement (Table 1). All of these inhibitory MAb recognize cell surface structures present on nonimmune mature lymphoid cells. The Ti, T3, T8 and T4 structures are unique to T cells and in the case for T8 and T4 define T-cell subpopulations that recognize antigen associated with Class I or Class II MHC glycoproteins, respectively (1–3). The clonotypic (Ti) surface structure and T3 appear to form the antigen binding recognition complex on the CTL surface (4) whereas the Lymphocyte Function Associated Antigen-2 (LFA-2) has been identified as the sheep red blood cell rosette receptor (5). In contrast, the LFA-1 molecule is present on both T and B lymphocytes and is structurally related to the OKM1/MAC-1 macrophage surface glycoprotein which is associated with complement receptor activity (CR3) (6,7). In contrast, the tissue distribution of LFA-3 is very broad including nonlymphoid cells (5).
KeywordsSurface Antigen Expression Simple Additive Effect Human Effector Cell Cytolytic Process Mature Lymphoid Cell
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