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A complex of the soluble interleukin‐6 receptor and interleukin‐6 is internalized via the signal transducer gp130
Author(s) -
Graeve Lutz,
Korolenko Tatjana A.,
Hemmann Ulrike,
Weiergräber Oliver,
Dittrich Elke,
Heinrich Peter C.
Publication year - 1996
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/s0014-5793(96)01305-1
Subject(s) - glycoprotein 130 , transducer , receptor , signal (programming language) , interleukin , interleukin 2 , chemistry , interleukin 6 , microbiology and biotechnology , immunology , medicine , biology , cytokine , biochemistry , computer science , physics , acoustics , programming language
In human body fluids a soluble form of the interleukin‐6 receptor (sIL‐6R) has been found which together with interleukin‐6 (IL‐6) acts agonistically on cells expressing the signal transducer gp130. The means by which the sIL‐6R is removed from the circulation is unknown. Here, we show that a complex of 125 I‐labelled recombinant sIL‐6R and IL‐6 is internalized by MDCK cells stably transfected with gp130 and by human hepatoma cells HepG2 that endogenously express the IL‐6R and gp130. We further show that most of the internalized sIL‐6R is degraded within lysosomes. Our studies suggest that cells expressing gp130 are capable of endocytosing an IL‐6/sIL6R complex, thereby removing both from the circulation.