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Biosynthetic and glycosylation events of the IL‐6 receptor β‐Subunit, gp130
Author(s) -
Wang Yang,
Fuller Gerald M.
Publication year - 1995
Publication title -
journal of cellular biochemistry
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.028
H-Index - 165
eISSN - 1097-4644
pISSN - 0730-2312
DOI - 10.1002/jcb.240570405
Subject(s) - oncostatin m , glycoprotein 130 , glycosylation , biology , immunoprecipitation , microbiology and biotechnology , leukemia inhibitory factor , biochemistry , population , protein subunit , chemistry , signal transduction , cytokine , interleukin 6 , immunology , gene , demography , stat3 , sociology
It is now recognized that the β‐subunit of the interleukin‐6 (IL‐6) receptor, also known as gp130, is a common signal transducer shared by other cytokines, including ciliary neurotrophic factor, leukemia inhibitor factor, oncostatin M, and IL‐11. In this study, the biosynthesis and glycosylation of hepatic gp130 were investigated using a specific polyclonal antibody to the 287 amino acid cytoplasmic domain of gp130. Immunoprecipitation and metabolic labeling experiments demonstrate, in addition to a mature surface expressed gp130, the presence of a major immature form of the molecule within the cell. The immature form can shift to become a functional gp130 only after being terminally glycosylated. The kinetics of gp130 maturation and surface expression were determined. When both forms of gp130 are deglycosylated the resulting core peptides migrate to identical positions in a denatured protein gel, indicating that the principal difference between the two forms resides in the extent of their glycosylation. IL‐6 and other members of this cytokine family activate only the mature form, demonstrating its location at the membrane surface. Protein and mRNA turnover studies reveal gp130 to be a stable, slowly renewing population under nonstimulated conditions. These findings provide novel information on the intracellular events leading to the expression of this critically important signal transducing protein.