Shedding of Endogenous Interleukin-6 Receptor (IL-6R) Is Governed by A Disintegrin and Metalloproteinase (ADAM) Proteases while a Full-length IL-6R Isoform Localizes to Circulating Microvesicles.

@article{Schumacher2015SheddingOE,
  title={Shedding of Endogenous Interleukin-6 Receptor (IL-6R) Is Governed by A Disintegrin and Metalloproteinase (ADAM) Proteases while a Full-length IL-6R Isoform Localizes to Circulating Microvesicles.},
  author={Neele Schumacher and D{\"o}rte Meyer and Andr{\'e} Mauermann and Jan von der Heyde and Janina Wolf and Jeanette Schwarz and Katharina Knittler and Gillian Murphy and Matthias Michalek and Christoph Garbers and J{\"o}rg W Bartsch and Songbo Guo and Beate Schacher and Peter Eickholz and Athena Chalaris and Stefan Rose-John and B. Khadem Rabe},
  journal={The Journal of biological chemistry},
  year={2015},
  volume={290 43},
  pages={26059-71}
}
Generation of the soluble interleukin-6 receptor (sIL-6R) is a prerequisite for pathogenic IL-6 trans-signaling, which constitutes a distinct signaling pathway of the pleiotropic cytokine interleukin-6 (IL-6). Although in vitro experiments using ectopically overexpressed IL-6R and candidate proteases revealed major roles for the metalloproteinases ADAM10 and ADAM17 in IL-6R shedding, the identity of the protease(s) cleaving IL-6R in more physiological settings, or even in vivo, remains unknown… CONTINUE READING
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