HIGH-AFFINITY INTERLEUKIN-6 RECEPTOR IS A HEXAMERIC COMPLEX CONSISTING OF 2 MOLECULES EACH OF INTERLEUKIN-6, INTERLEUKIN-6 RECEPTOR, AND GP-130
- Author(s)
- Ward, LD; Howlett, GJ; DISCOLO, G; Yasukawa, K; Hammacher, A; Moritz, RL; Simpson, RJ;
- Details
- Publication Year 1994-09-16,Volume 269,Issue #37,Page 23286-23289
- Journal Title
- JOURNAL OF BIOLOGICAL CHEMISTRY
- Publication Type
- Journal Article
- Abstract
- The high affinity human interleukin-6 (IL-6) receptor complex consists of IL-6 and two membrane-associated receptor components, the IL-6 receptor (alpha-subunit) and the high affinity converter and signal transducing molecule, gp-130 (beta-subunit). Recombinant IL-6 and the extracellular (''soluble'') components of the IL-6 receptor (sIL-6R) and gp-130 (sgp-130) have been prepared in order to investigate the stoichiometry and binding of these components in the low affinity (IL-6.sIL-6R) and high affinity (IL-6 sIL-6R.sgp-130) IL-6 receptor complexes. Using a combination of size-exclusion chromatography and analytical ultracentrifugation analysis, in the low affinity receptor complex, IL-6 was shown to bind sIL-6R in a stoichiometric ratio of 1:1, whereas the high affinity ternary complex is hexameric consisting of two molecules each of IL-6, sIL-6R, and sgp-130. This is the first direct demonstration of a higher order arrangement for receptor cytokine interactions that exhibit both high and low affinity complexes.
- Publisher
- AMER SOC BIOCHEMISTRY MOLECULAR BIOLOGY INC
- Keywords
- HUMAN GROWTH-HORMONE; MONOCLONAL-ANTIBODIES; EXTRACELLULAR DOMAIN; HUMAN IL-6; PURIFICATION; EXPRESSION; TRANSDUCER; CLONING; BINDING; GP130
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Creation Date: 1994-09-16 12:00:00