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Murine interleukin-1 receptor: differences in binding properties between fibroblastic and thymoma cells and evidence
T A Bird1, A J Gearing, J Saklatvala
1Strangeways Research Laboratory, Cambridge, England.
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.
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.