Interaction of IL-15 with the shared IL-2 receptor beta and gamma c subunits. The IL-15/beta/gamma c receptor-ligand complex is less stable than the IL-2/beta/gamma c receptor-ligand complex.

作者: P. M. Sondel , J. L. O. De Jong , J. G. Giri , M. B. Widmer , N. L. Farner

DOI:

关键词: Beta (finance)Interleukin 15Alpha chainIL-2 receptorAffinity labelG alpha subunitReceptorBiologyAlpha (ethology)Molecular biology

摘要: This study was designed to compare the interactions of IL-2 and IL-15 with IL-2R beta gamma c subunits, as differences in receptor between might contribute functional these two cytokines. The results suggest existence a human IL-15R alpha subunit, although physical evidence this molecule not obtained. Proliferation anti-CD3 (OKT3)-stimulated PBL compared for responsiveness IL-2, IL-15, F42K, mutant that does bind chain. F42K more potent than activating dose-dependent response. fact, along Scatchard binding analyses on OKT3 blasts YT cells revealing both high intermediate affinity receptors, supports cells. Additional characterization utilized covalent cross-linking label blasts. Consistent previously reported data, co-precipitated from [125I]IL-15 receptor-ligand complex, demonstrating interact physically subunit. While did co-precipitate presence beta/gamma complex. Finally, equilibrated then precipitated through showed 1:1 ratio, while only found immunoprecipitates IL-15. indicates creates less stable bridge chains result identical surface-iodinated were probed Western blots.

参考文章(0)