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

Hibi, Masahiko, Murakami, Masaaki, Saito, Mikiyoshi, Hirano, Toshio, Taga, Tetsuya, Kishimoto, Tadamitsu·1990·Cell
DOI 10.1016/0092-8674(90)90411-7
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Abstract

Interleukin-6 (IL-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 918 amino acids with a single transmembrane domain. The extracellular region comprises six units of a fibronectin type III module, and part of this region of approximately 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 gp130 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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  • IL-6R exists in an 80 kDa transmembrane form and a 50-55 kDa soluble form (sIL-6R).

    “Unlike gp130, IL-6R exists in an 80 kDa transmembrane form and a 50–55 kDa soluble form (sIL-6R) (Hibi et al., 1990”

    From Targeting Interleukin-6 Signaling in Clinic (2019) · cites this paper as Hibi et al., 1990

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Metadata

Authors
Hibi, M., Murakami, M., Saito, M., Hirano, T., Taga, T., & Kishimoto, T.
Venue
Cell
Publisher
Elsevier BV
Published
1990-12
Volume
63
Issue
6
Pages
1149-1157
ISSN
0092-8674
DOI
10.1016/0092-8674(90)90411-7
Cited by
1,039
References
0
Language
en
Licence
Funders
Ministry of Education, Culture, Sports, Science and Technology

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