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Keywords :
Animals; Phosphorylation; Protein Tyrosine Phosphatase, Non-Receptor Type 11; Protein Tyrosine Phosphatase, Non-Receptor Type 6; Protein Tyrosine Phosphatases; Receptors, Interleukin-6; STAT1 Transcription Factor; STAT3 Transcription Factor; Trans-Activators; Mice; Membrane Glycoproteins; Intracellular Signaling Peptides and Proteins; Antigens, CD; Cell Line; Cytokine Receptor gp130; DNA-Binding Proteins; Endocytosis; Erythropoietin; Humans; Interleukin-6; Tumor Cells, Cultured
Abstract :
[en] The interleukin-6 (IL-6) receptor complex comprises the IL-6 receptor (IL-6R, gp80) and the signal transducer gp130. Binding of IL-6 to its receptor results in dimerization of gp130, activation of the Jak/STAT pathway, and in a down-regulation of IL-6 binding sites by endocytosis. The STAT activation after stimulation is transient, being maximal after 15-30 min and disappearing after 60-90 min. The mechanism which leads to the termination of the signal is still unknown.In this paper we have studied whether the down-modulation of the STAT signal requires the endocytosis of the receptor complex. Our results suggest that the desensitization of the IL-6 signal is not due to internalization of the receptor complex but requires de novo protein synthesis.
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