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Research Article Free access | 10.1172/JCI113301

Dexamethasone inhibition of interleukin 1 beta production by human monocytes. Posttranscriptional mechanisms.

J A Kern, R J Lamb, J C Reed, R P Daniele, and P C Nowell

Department of Medicine, Hospital of the University of Pennsylvania, Philadelphia 19104-4283.

Find articles by Kern, J. in: PubMed | Google Scholar

Department of Medicine, Hospital of the University of Pennsylvania, Philadelphia 19104-4283.

Find articles by Lamb, R. in: PubMed | Google Scholar

Department of Medicine, Hospital of the University of Pennsylvania, Philadelphia 19104-4283.

Find articles by Reed, J. in: PubMed | Google Scholar

Department of Medicine, Hospital of the University of Pennsylvania, Philadelphia 19104-4283.

Find articles by Daniele, R. in: PubMed | Google Scholar

Department of Medicine, Hospital of the University of Pennsylvania, Philadelphia 19104-4283.

Find articles by Nowell, P. in: PubMed | Google Scholar

Published January 1, 1988 - More info

Published in Volume 81, Issue 1 on January 1, 1988
J Clin Invest. 1988;81(1):237–244. https://doi.org/10.1172/JCI113301.
© 1988 The American Society for Clinical Investigation
Published January 1, 1988 - Version history
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Abstract

Dexamethasone is known to have an inhibitory effect on IL-1 production. To determine the mechanism(s) of this inhibition, adherent human blood monocytes were stimulated with Escherichia coli lipopolysaccharide (LPS) (10 micrograms/ml) in the presence of dexamethasone. Nuclear transcription run-off assays showed that LPS induced IL-1 beta gene transcription two- to fourfold and that this induction was unaffected by dexamethasone exposure (10(-5) M). The lack of dexamethasone's transcriptional effects was further supported by the absence of any significant change in IL-1 beta mRNA accumulation between LPS-stimulated monocytes exposed or unexposed to dexamethasone, as determined by Northern blot analysis. Posttranscriptionally, dexamethasone was found to have multiple effects: slight prolongation of IL-1 beta mRNA half-life, moderate inhibition of translation of the IL-1 beta precursor, and profound inhibition of the release of IL-1 beta into the extracellular fluid. The data indicate that IL-1 beta is first translated as the 33,000-D pro-IL-1 beta protein, the predominant intracellular form, and the processed to a 17,500-D IL-1 beta protein before or during extracellular transport. The major inhibitory effects of dexamethasone appear to be directed at the translational and posttranslational steps involved in these events.

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