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A soluble form of the interleukin‐1 receptor produced by a human B cell line
Author(s) -
Symons J.A.,
Duff G.W.
Publication year - 1990
Publication title -
febs letters
Language(s) - English
Resource type - Journals
SCImago Journal Rank - 1.593
H-Index - 257
eISSN - 1873-3468
pISSN - 0014-5793
DOI - 10.1016/0014-5793(90)80466-v
Subject(s) - chemistry , receptor , cell culture , microbiology and biotechnology , biochemistry , biology , genetics
A soluble protein that binds specifically to interleukin‐1 (IL‐1)β was released from a B cell line (Raji). The covalently cross‐linked binding protein/ [ 125 I]IL‐1β migrated at 60 kDa by SDS‐PAGE. The IL‐1 receptor (IL‐1R) on Raji cells had the same ligand specificity. Stimulation of Raji with dexamethasone increased surface expression of the IL‐1R and the rate of release of soluble binding protein. A serine protease inhibitor prevented release of the binding protein and increased IL‐1R expression on the cells. These results suggest that the soluble IL‐1β binding protein is a proteolytically cleaved form of the novel B cell IL‐1R.