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Separate regulation of a membrane protein, gp130, present in receptor complex specific for interleukin‐6 and other functionally related cytokines
Author(s) -
Falus András,
Biró Judit,
Rákász Éva,
Brunner Thomas,
Bischoff Stephan
Publication year - 1994
Publication title -
journal of molecular recognition
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 0.401
H-Index - 79
eISSN - 1099-1352
pISSN - 0952-3499
DOI - 10.1002/jmr.300070407
Subject(s) - glycoprotein 130 , oncostatin m , receptor , interleukin 6 receptor , ciliary neurotrophic factor , cell surface receptor , chemistry , microbiology and biotechnology , biology , interleukin , cytokine , biochemistry , interleukin 6 , immunology , neurotrophic factors
In addition to specific ligand binding elements, receptor assembly for interleukin(IL)‐6, oncostatin‐M, leukaemia inhibitory factor, ciliary neurotrophic factor and IL‐11 includes and additional unit, gp130. This molecule is a transmembrane glycoprotein of 130 kDa. In this paper, reviewing molecular, biochemical and functional data on gp130, we describe the dissimilar action of IL‐3 on the expression of the binding unit of the IL‐6 receptor and that of gp130. According to FACS studies, resting basophils express only IL‐6 receptors and no gp130 molecules on the plasma membranes. After incubation with IL‐3, the surface appearance and de novo transcription of gp130 was shown by FACS and mRNA polymerase chain reaction analysis.