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A Convenient and General Expression Platform for the Production of Secreted Proteins from Human Cells
Published on: July 31, 2012
A soluble form of the interleukin-1 receptor produced by a human B cell line
1University of Edinburgh, Department of Medicine, Northern General Hospital, UK.
Insights
Researchers identified a soluble protein binding interleukin-1 beta (IL-1β) released from B cells. This protein appears to be a cleaved form of the B cell
Area of Science:
- Immunology
- Cell Biology
- Biochemistry
Background:
- Interleukin-1 beta (IL-1β) is a key inflammatory cytokine.
- B cells express receptors for IL-1.
- Soluble factors regulating IL-1β activity are of significant interest.
Purpose of the Study:
- To characterize a soluble protein released from B cells that binds IL-1β.
- To investigate the relationship between this soluble binding protein and the B cell IL-1 receptor (IL-1R).
Main Methods:
- Utilized a B cell line (Raji) for protein release studies.
- Employed SDS-PAGE and covalent cross-linking to analyze the binding protein.
- Investigated the effect of dexamethasone and serine protease inhibitors on protein release and receptor expression.
Main Results:
- A 60 kDa soluble protein specifically binding IL-1β was isolated from Raji cells.
- Raji cells possess an IL-1R with identical ligand specificity.
- Dexamethasone increased IL-1R expression and soluble binding protein release; protease inhibitors blocked release and increased receptor expression.
Conclusions:
- The soluble IL-1β binding protein is likely a proteolytically cleaved form of the B cell IL-1R.
- This finding suggests a novel mechanism for regulating IL-1β activity via B cell-derived soluble receptors.
Abstract:
A soluble protein that binds specifically to interleukin-1 (IL-1)beta was released from a B cell line (Raji). The covalently cross-linked binding protein/[125I]IL-1 beta 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-1 beta binding protein is a proteolytically cleaved form of the novel B cell IL-1R.
