Literature DB >> 8980136

A complex of the soluble interleukin-6 receptor and interleukin-6 is internalized via the signal transducer gp130.

L Graeve1, T A Korolenko, U Hemmann, O Weiergräber, E Dittrich, P C Heinrich.   

Abstract

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 125I-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/sIL-6R complex, thereby removing both from the circulation.

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Year:  1996        PMID： 8980136     DOI： 10.1016/s0014-5793(96)01305-1

Source DB:  PubMed          Journal:  FEBS Lett        ISSN： 0014-5793            Impact factor:   4.124


  8 in total

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2.  Internalization of the interleukin 6 signal transducer gp130 does not require activation of the Jak/STAT pathway.

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Review 3.  Interleukin-6-type cytokine signalling through the gp130/Jak/STAT pathway.

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7.  Intragenic regulation of SOCS3 isoforms.

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  8 in total

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