COMPOSITION OF TCR-CD3 COMPLEX IN HUMAN INTESTINAL INTRAEPITHELIAL LYMPHOCYTES - LACK OF FC-EPSILON-RI-GAMMA CHAIN

Human intestinal intraepithelial lymphocytes (iIEL) are a unique population of predominantly CD8 alpha beta(+), TCR alpha beta(+) lymphocytes and, to a lesser extent, TCR gamma delta(+) lymphocytes that proliferate poorly to anti-CD3 mitogenic signals but display significant cytolytic activity. Studies in mouse model systems have shown that the gamma chain of the high-affinity receptor for IgE (Fc epsilon Rly) may substitute for the zeta chain in the TCR-CD3 complex of iIEL. This has suggested that the functional properties of these cells may be associated with an altered composition of the TCR-CD3 complex. We therefore analyzed the TCR-CD3 complex of normal human iIEL. One- and two-dimensional non-reducing/reducing SDS-PAGE analysis of CD3 gamma, CD3 delta, CD3 epsilon, zeta and Fc epsilon Rly chain immuno-precipitates of cell surface radiolabeled proteins with subunit-specific antibodies revealed a TCR-CD3 complex without associated Fc epsilon Rly chains. Thus, normal human iIEL contain a TCR-CDS complex that consists predominantly of zeta homodimers in association with the alpha beta TCR and CD3 gamma, delta and epsilon. Similar to the majority of peripheral lymphocytes. This indicates that the distinct properties of human ilEL are not associated with substitutions of the Fc epsilon Rly chain in the TCR-CD3 complex.