0000000000305594

AUTHOR

Hildegard Schmitz-van De Leur

showing 2 related works from this author

The membrane distal half of gp130 is responsible for the formation of a ternary complex with IL-6 and the IL-6 receptor

1995

AbstractGp130 is the signal transducing subunit of the interleukin-6 receptor. Signaling is initiated by the complex formation of gp130 with IL-6 bound to the IL-6 receptor (IL-6R). We have subdivided the extracellular domain of gp130 in two parts and expressed the mutant proteins as soluble IgG fusion proteins in COS-7 cells. By studying the formation of the ternary complex we show that the membrane distal half of gp130 which contains a cytokine receptor domain is responsible for the interaction with the IL-6/IL-6R complex. Interestingly this is the same region which is believed to be involved in specific recognition of the related cytokines LIF, OM, and probably also of CNTF and IL-11.

Molecular Sequence DataBiophysicsBiologyBiochemistryCytokine receptor domainCell Linegp130Structure-function analysisAntigens CDStructural BiologyCytokine Receptor gp130GeneticsAnimals5-HT5A receptorReceptorMolecular BiologyTernary complexMembrane GlycoproteinsBase SequenceInterleukin-6digestive oral and skin physiologyHaplorhiniReceptors InterleukinCell BiologyGlycoprotein 130Receptors Interleukin-6Fusion proteinbiological factorsCell biologyOligodeoxyribonucleotidesInterleukin-6 receptorCancer researchSignal transductionCytokine receptorProtein BindingSignal TransductionFEBS Letters
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Combining two mutations of human interleukin-6 that affect gp130 activation results in a potent interleukin-6 receptor antagonist on human myeloma ce…

1995

The pleiotropic cytokine interleukin-6 (IL-6) interacts with the specific ligand binding subunit (IL-6R alpha) of the IL-6 receptor, and this complex associates with the signal-transducing subunit gp130 (IL-6R beta). Human IL-6 acts on human and murine cells, whereas murine IL-6 is only active on murine cells. The construction of a set of chimeric human/murine IL-6 proteins has recently allowed us to define a region (residues 43-55) within the human IL-6 protein, which is important for the interaction with gp130. Subdividing this region shows that mainly residues 50-55 of the human IL-6 are necessary for this interaction. Recently, another human IL-6 double mutant (Q159E and T162P) showed r…

Protein ConformationProtein subunitmedicine.medical_treatmentMutantMolecular Sequence DataBiologyBiochemistryMiceAntigenAntigens CDmedicineCytokine Receptor gp130Tumor Cells CulturedAnimalsHumansPoint MutationInterleukin 6ReceptorMolecular BiologyMembrane GlycoproteinsBase SequenceInterleukin-6Wild typeCell BiologyReceptors InterleukinGlycoprotein 130Molecular biologyReceptors Interleukin-6CytokineOligodeoxyribonucleotidesbiology.proteinMultiple MyelomaThe Journal of biological chemistry
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