Murine interleukin-1 receptor: differences in binding properties between fibroblastic and thymoma cells and evidence for a two-chain receptor model.

The concentration of porcine interleukin-1 beta (pIL1 beta) required to elicit half-maximal IL2 production from NOB-1, a subline of murine thymoma EL4, was 100-fold greater than for p1L alpha. In contrast, similar doses of each type of IL1 stimulated increased lactate production by Balb/C 3T3 fibroblasts. Receptor-bound 125I-IL 1 alpha was displaced with equal efficiency by both unlabelled forms from 3T3 cells, but a 20-fold lower affinity for p1L1 beta was observed using NOB-1. Crosslinking experiments suggested that the IL1 receptors on each line consisted of two polypeptides of 80 and 100 kDa. The results provide the first evidence for a multiple-component IL1 receptor within which IL1 alpha and IL1 beta may bind at different loci, and suggest the receptors may have evolved differently in the two lines.