tailieunhanh - Báo cáo khoa học: Functionally active fusion protein of the novel composite cytokine CLC/soluble CNTF receptor

The heterodimeric cytokine composed of the soluble ciliary neurotrophic factor receptor (sCNTFR) and the IL-6 family member cardiotrophin-like cytokine (CLC) was recently identi®ed as a new ligand for gp130±leukemia inhibitory factor receptor (LIFR) complex [Plun-Favreau, H., Elson, G., Chabbert, M., Froger, J., deLapeyriere, O., Lelievre, E., Guillet, C., Hermann, J., Gauchat, J. F., Gascan, H. & Chevalier, S. (2001)EMBO , 1692± 1703]. This heterodimer shows overlapping biological properties with LIF | Eur. J. Biochem. 269 1932-1941 2002 FEBS 2002 doi Functionally active fusion protein of the novel composite cytokine CLC soluble CNTF receptor Catherine Guillet1 Eric Lelièvre1 Helene Plun-Favreau1. Josv Froger1. Marie Chabbert1 Jacaues Hermann1 Amelie Benoit de Coignac2 Jean-Yves Bonnefoy2 Hugues Gascan1 Jean-Francois Gauchat2 and Greg Elson2 1INSERM U564 CHU d Angers Angers France 2Centre diĩmmunologie Pierre Fabre St-Julien-en-Genevois France The heterodimeric cytokine composed of the soluble ciliary neurotrophic factor receptor sCNTFR and the IL-6 family member cardiotrophin-like cytokine CLC was recently identihed as a new ligand for gp130-leukemia inhibitory factor receptor LIFR complex Plun-Favreau H. Elson G. Chabbert M. Froger J. deLapeyriere O. Lelievre E. Guillet C. Hermann J. Gauchat J. F. Gascan H. Chevalier S. 2001 EMBO J. 20 16921703 . This heterodimer shows overlapping biological properties with LIF. Although CLC contains a putative signal peptide and therefore should enter into the classical secretory pathway the protein has been shown to be retained within transfected mammalian cells unless coexpressed with either sCNTFR or cytokine like factor CLF Elson G. C. Lelievre E. Guillet C. Chevalier S. Plun-Favreau H. Froger J. Suard I. de Coignac A. B. Delneste Y. Bonnefoy J. Y. Gauchat J. F. Gascan H. 2000 Nat. Neurosci. 3 867-872 . In the present study we demonstrate that a fusion protein comprising CLC covalently coupled through a glycine serine linker to sCNTFR CC-FP is efficiently secreted from transfected mammalian cells. CC-FP shows enhanced activities in respect to the CLC sCNTFR native complex on a number of cells expressing gp130 and LIFR on their surface. In addition CC-FP is able to compete with CNTF for cell binding indicating that both cytokines share binding epitope s expressed by their receptor complex. Analysis of the downstream signaling events revealed the recruitment by CC-FP of the signal transducer

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