| Literature DB >> 1699802 |
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.Entities:
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Year: 1990 PMID: 1699802 DOI: 10.1016/0014-5793(90)80466-v
Source DB: PubMed Journal: FEBS Lett ISSN: 0014-5793 Impact factor: 4.124