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Despite the existence of tumor-infiltrating T lymphocytes (TILs), the tumor manages to grow. The host laboratory has found that these TILs have dysfunctional cytokine secretion and lytic capacities. Treating TIL with a galectin antagonist can partially correct these defects. Galectins are lectins secreted in the tumor environment by tumor cells and macrophages. They bind to polysaccharide motifs that decorate the cell surface receptors. They can form galectin-glycoprotein lattices, wich decrease the mobility of these receptors. The host laboratory thought that TIL covered galectins had a poor ability to be activated. The Lck kinase is known to interact with both glycoproteins CD45 and LFA-1 expressed at the T cell surface. LFA-1 is an adhesion molecule involved in stabilizing intercellular interactions and the CD45 phosphatase is involved in the regulation of intracellular signaling. The host laboratory observed a lack of motility of these two receptors at the contact area between a TIL and its target, lack of motility that could be corrected by a treatment with galectin antagonists. We made preliminary experiments to trap CD45 and LFA-1 in artificial lattices by capturing these surface receptors with cross-linked anti-FLA-1 and anti-CD45 antibodies. These artificial lattices should reduce the motility of these receptors and mimic galectin- glycoprotein lattices. It will then be possible to examine whether this lack of receptor motility disrupt the secretion of cytokines by T lymphocytes as do galectins in TILs.

Lymphocyte Specific Protein Tyrosine Kinase p56(lck) --- CD8-Positive T-Lymphocytes --- Neoplasms --- Immunological Synapses