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Cited by 1,461

The DOI matches its Crossref record; 10 of the 10 references it cites were found in a registry or an index.

gp 130 AND THE INTERLEUKIN-6 FAMILY OF CYTOKINES

Taga, Tetsuya, Kishimoto, Tadamitsu·1997·Annual Review of Immunology

Abstract

▪ Abstract Receptors for most interleukins and cytokines that regulate immune and hematopoietic systems belong to the class I cytokine receptor family. These molecules form multichain receptor complexes in order to exhibit high-affinity binding to, and mediate biological functions of, their respective cytokines. In most cases, these functional receptor complexes share common signal transducing receptor components that are also in the class I cytokine receptor family, i.e. gp130, common β, and common γ molecules. Interleukin-6 and related cytokines, interleukin-11, leukemia inhibitory factor, oncostatin M, ciliary neurotrophic factor, and cardiotrophin-1 are all pleiotropic and exhibit overlapping biological functions. Functional receptor complexes for this interleukin-6 family of cytokines share gp130 as a component critical for signal transduction. Unlike cytokines sharing common β and common γ chains that mainly function in hematopoietic and lymphoid cell systems, the interleukin-6 family of cytokines function extensively outside these systems as well, e.g. from the cardiovascular to the nervous system, owing to ubiquitously expressed gp130. Stimulation of cells with the interleukin-6 family of cytokines triggers homo- or hetero-dimerization of gp130. Although gp130 and its dimer partners possess no intrinsic tyrosine kinase domain, the dimerization of gp130 leads to activation of associated cytoplasmic tyrosine kinases and subsequent modification of transcription factors. This paper reviews recent progress in the study of the interleukin-6 family of cytokines and gp130.

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Metadata

Authors
Taga, T., & Kishimoto, T.
Venue
Annual Review of Immunology
Published
1997-04
Volume
15
Issue
1
Pages
797-819
ISSN
  • 0732-0582 (ISSN-L)
  • 1545-3278
OpenAlex
W2119120508
Cited by
1,461
References
10
FWCI
4.64
Type
journal article
Language
en
Open access
closed

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