Interleukin-6 is a cytokine synthesized by many cells in the human body. IL-6 binds to a membrane bound IL-6R, which is only present on hepatocytes, some epithelial cells and some leukocytes. The complex of IL-6 and IL-6R binds to the ubiquitously expressed receptor subunit gp130, which forms a homodimer and thereby initiates intracellular signaling via the JAK/STAT and the MAPK pathways. IL-6R expressing cells can cleave the receptor protein to generate a soluble IL-6R (sIL-6R), which can still bind IL-6 and can associate with gp130 and induce signaling even on cells, which do not express IL-6R. This paradigm has been called IL-6 trans-signaling whereas signaling via the membrane bound IL-6R is referred to as classic signaling. We have generated several molecular tools to differentiate between IL-6 classic- and trans-signaling and to analyze the consequence of cellular IL-6 signaling in vivo.
CITATION STYLE
Garbers, C., & Rose-John, S. (2018). Dissecting interleukin-6 classic- and trans-signaling in inflammation and cancer. In Methods in Molecular Biology (Vol. 1725, pp. 127–140). Humana Press Inc. https://doi.org/10.1007/978-1-4939-7568-6_11
Mendeley helps you to discover research relevant for your work.