Abstract

Macrophage-chemotactic factor (MChF)-producing T cell hybridomas were established. These hybridomas produced MChF upon the specific antigenic stimulation with phosphorylcholine (PC)-conjugated protein in the presence of I-Ed-positive antigen-presenting cells. The hybridomas also secreted MChF after co-culture with concanavalin A in the absence of antigen-presenting cells. The MChF-secreting hybridomas were positive for Kd, Dd, Lyt-1.2 but negative for I-Ad, Lyt-2.2. The molecular weight of MChF produced by the hybridomas was 43000 and the factor was focused at pH 6.6-6.8 in the chromatofocusing procedure. The MChF was protease sensitive but resistant to neuraminidase treatment, and it was stable by heating at 80 degrees C for 15 min. The MChF-producing hybridomas established in this stud did not produce macrophage migration inhibitory factor (MIF), macrophage-activating factor (MAF) or interleukin 2, suggesting molecular nonidentity between MChF and these lymphokines. The MChF-producing T cell hybridomas reactive to specific antigens (PC) will be promising tools for analysis of molecular nature of MChF as well as molecular aspects of antigen recognition mechanism of T cells.

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