Inhibition of interleukin4

IL-4 signals through an heterodimeric receptor composed of the IL-4Ra and the IL-2 Ryc chain. Il.-4Ra exists in soluble form and protects IL-4 from proteolytic degradation. Because IL-4 soluble receptor has a lower affinity for IL-4 than the cell-bound receptors it seems likely that the soluble form serves as a carrier of IL-4, facilitating its presentation to cell-bound receptors. In addition, an alternative splice variant of human IL-4, called IL-4 8-2, inhibits in vitro IL-4-stimulated T cell proliferation. This splice variant seems to be preferentially expressed in the thymus and bronchoalveolar lavage cells. This finding suggests that the generation of cytokine variants by alternative RNA splicing due to exon-deletion mechanism might give rise to receptor antagonists and may be an important mechanism for the regulation of cytokine activity.

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