Molecular cloning and expression of an IL-6 signal transducer, gp130

M Hibi, M Murakami, M Saito, T Hirano, T Taga… - Cell, 1990 - cell.com
M Hibi, M Murakami, M Saito, T Hirano, T Taga, T Kishimoto
Cell, 1990cell.com
Summary Interleukind(11-6) signal is transduced through a membrane glycoprotein, gp130,
which associates with IL-6 receptor (IL-6-R). A cDNA encoding human gp130 has been
cloned, revealing that it consists of 916 amino acids with a single transmembrane domain.
The extracellular region comprises six units of a fibronectin type Ill module, and part of this
region of~ 200 amino acids has features typical of a cytokine receptor family. A cDNA-
expressed gp130 showed no binding property to IL-6 or several other cytokines. Although a …
Summary
Interleukind(11-6) signal is transduced through a membrane glycoprotein, gp130, which associates with IL-6 receptor (IL-6-R). A cDNA encoding human gp130 has been cloned, revealing that it consists of 916 amino acids with a single transmembrane domain. The extracellular region comprises six units of a fibronectin type Ill module, and part of this region of~ 200 amino acids has features typical of a cytokine receptor family. A cDNA-expressed gp130 showed no binding property to IL-6 or several other cytokines. Although a transfectant with an IL-6-R cDNA expressed mainly low affinity IL-6 binding sites, an increase in high affinity binding sites was observed after cotransfection with a gp130 cDNA. This confirmed that a gpl30 is involved in the formation of high affinity IL-6 binding sites. A cloned gp130 could associate with a complex of IL-6 and soluble IL-6-R and transduce the growth signal when expressed in a murine IL-3-dependent cell line.
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