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- W2470293589 abstract "Interleukin-6 (IL-6) has been linked to numerous inflammatory diseases and is therefore an attractive therapeutic target in the clinic. Soluble and membrane-bound forms of the Interleukin-6 Receptor (IL-6R) are responsible for its pro- and anti-inflammatory properties via the membrane-bound β-receptor gp130. Formation of the signaling complex results in activation of the JAK/STAT signaling pathway. In addition, soluble forms of the IL-6R (sIL-6R) have been identified in several body fluids. Interestingly, a coding nonsynonymous single nucleotide polymorphism (SNP) within the IL-6R (rs2228145, Asp358Ala) results in a 2-fold increase in soluble IL-6R (sIL-6R) serum levels and a reduced risk for coronary heart disease. In vitro data show that the sIL-6R is generated either via limited proteolysis of the membrane-bound precursor or via alternative splicing of the IL-6R mRNA, and the latter has been shown to occur also in vivo. In order to identify and analyze sIL-6R that was generated by proteolysis we combined a “bottom-up” proteomics approach with LC-MS. We could determine the cleavage site used in vitro and in vivo, identify novel glycan motifs, and show for the first time that proteolysis contributes to sIL-6R serum levels in humans. Further analysis of N- and O-linked glycosylation revealed different functions in terms of signaling and proteolysis. Mutation of the identified cleavage site resulted in an IL-6R that was resistant towards shedding by ADAM10 and ADAM17. In summary, our data show that limited proteolysis contributes to sIL-6R serum levels in humans, and that glycosylation is an important regulatory modification of the IL-6R." @default.
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- W2470293589 date "2015-11-01" @default.
- W2470293589 modified "2023-10-18" @default.
- W2470293589 title "ID: 196" @default.
- W2470293589 doi "https://doi.org/10.1016/j.cyto.2015.08.200" @default.
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