Purification and characterization of TNP-specific immunoregulatory molecules produced by T cells sensitized by picrylchloride (PC1F).

ABSTRACT

T cell-derived TNP-specific factors associated with immunoregulatory activity were obtained by culture of T cells obtained from mice sensitized by skin-painting with picrylchloride. Culture medium was absorbed to TNP-Sepharose and TNP binding proteins were prepared by elution with TNP. The hapten affinity-purified proteins were characterized by size and charge and were found to be acidic 70,000 m.w. polypeptides that occur as monomers or oligomers. Oligomeric proteins interact with factors produced by mice injected with trinitrobenzenesulfonic acid to form factors that suppress specifically the ability of TNP-sensitized T cells to transfer contact sensitivity to TNP. Monomeric (no more than 70,000 m.w.) molecules do not form suppressor factors but can transfer contact sensitivity to TNP. Moreover, reduction and alkylation of oligomeric molecules inactivates their suppressor activity but causes them to be able to transfer contact sensitivity. The results suggest that T cell-derived antigen-specific molecules may have different effector functions dependent on their oligomeric state.