Binding Interactions of Leukemia Inhibitory Factor and Ciliary Neurotrophic Factor with the Different Subunits of Their High Affinity Receptors

@article{Robledo1996BindingIO,
  title={Binding Interactions of Leukemia Inhibitory Factor and Ciliary Neurotrophic Factor with the Different Subunits of Their High Affinity Receptors},
  author={Olivier Robledo and Patrick Auguste and L Coupey and Vincent Praloran and Sylvie Chevalier and Annick Pouplard and Hugues Gascan},
  journal={Journal of Neurochemistry},
  year={1996},
  volume={66}
}
Abstract: Leukemia inhibitory factor (LIF) and ciliary neurotrophic factor (CNTF) share common components in their multimeric receptors. Both cytokine receptors contain gp130/interleukin‐6‐receptor transducer as well as gp190/low‐affinity LIF receptor. For CNTF, addition of a third subunit, or α subunit, defines the high‐affinity CNTF receptor. In the present study, we analyzed the binding interactions of LIF and CNTF in human cell lines and showed a mutual displacement for LIF and CNTF toward… 
The ciliary neurotrophic factor receptor α component induces the secretion of and is required for functional responses to cardiotrophin‐like cytokine
TLDR
It is demonstrated that CNTFR induces the secretion of CLC, as well as mediating the functional responses of C LC, which enhances motor neuron survival.
Alanine Substitution for Thr268 and Asp269 of Soluble Ciliary Neurotrophic Factor (CNTF) Receptor α Component Defines a Specific Antagonist for the CNTF Response*
TLDR
CNTFR3α specifically antagonizes the induction of gp130 and LIFRβ tyrosine phosphorylation observed in response to CNTF and wild type soluble CNTFRα in the HepG2 hepatoma cell line, as well as the subsequent events leading to haptoglobin synthesis.
Leukemia Inhibitory Factor (LIF), Cardiotrophin-1, and Oncostatin M Share Structural Binding Determinants in the Immunoglobulin-like Domain of LIF Receptor*
TLDR
It is indicated that LIF, CT-1, and OSM share an overlapping binding site located in the Ig-like domain of LIFR, which can be related to the different affinity of their site III for LifR.
LIF receptor‐gp130 interaction investigated by homology modeling: Implications for LIF binding
TLDR
Electrostatic isopotential surfaces of the CBD models suggest that gp130 and the membrane‐proximal CBD of LIFR hetero‐dimerize and bind LIF through contacts similar to those seen in the growth hormone receptor dimer.
Ciliary Neurotrophic Factor, Cardiotrophin-like Cytokine, and Neuropoietin Share a Conserved Binding Site on the Ciliary Neurotrophic Factor Receptor α Chain*
TLDR
Biochemical, cell proliferation, and cell signaling analyses showed that Phe172 and Glu286 of ciliary neurotrophic factor receptor α are key interaction residues.
Identification of a gp130 Cytokine Receptor Critical Site Involved in Oncostatin M Response*
TLDR
It is demonstrated that positions 189–192 of gp130 cytokine binding domain are essential for OSM binding to both gp130/LIF receptor β and gp130 /OSM receptor β heterocomplexes.
CLF associates with CLC to form a functional heteromeric ligand for the CNTF receptor complex
TLDR
This work has identified this factor as a stable secreted complex of cardiotrophin-like cytokine (CLC) and the soluble receptor cytokine-like factor-1 (CLF).
Functionally active fusion protein of the novel composite cytokine CLC/soluble CNTF receptor.
TLDR
It is demonstrated that a fusion protein comprising CLC covalently coupled through a glycine/serine linker to sCNTFR (CC-FP) is efficiently secreted from transfected mammalian cells and is a powerful tool to study the biological role of the recently described cytokine CLC.
Signaling of the Cardiotrophin-1 Receptor
TLDR
The results provide evidence that the CT-1 receptor is composed of a tripartite complex, a situation similar to the high affinity receptor for ciliary neurotrophic factor.
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TLDR
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