RGD Reference Report - Lipopolysaccharide stimulates phosphorylation of eukaryotic initiation factor-4F in macrophages and tumor necrosis factor participates in this event. - Rat Genome Database

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Lipopolysaccharide stimulates phosphorylation of eukaryotic initiation factor-4F in macrophages and tumor necrosis factor participates in this event.

Authors: Haas, DW  Shepherd, VL  Hagedorn, CH 
Citation: Haas DW, etal., Second Messengers Phosphoproteins. 1992-1993;14(3):163-71.
RGD ID: 10045884
Pubmed: PMID:1345341   (View Abstract at PubMed)

Bacterial lipopolysaccharide (LPS) produces rapid changes in macrophage protein synthesis and function. Phosphorylation of the 25 kDa mRNA cap-binding protein (eIF-4E) in model systems regulates the efficiency of protein synthesis. We report that both LPS and tumor necrosis factor-alpha (TNF-alpha) stimulate phosphorylation of eIF-4E and the p220 component of eIF-4F in bone marrow-derived macrophages. Moreover, anti-TNF-alpha antibodies inhibit LPS-stimulated phosphorylation of eIF-4E and p220 by 43% (+/- 6%) and 50% (+/- 5%), respectively. Our results indicate that LPS stimulates eIF-4F phosphorylation by a TNF-alpha-dependent mechanism, and suggest that phosphorylation of eIF-4F might play a role in the post-transcriptional regulation of gene expression in macrophages exposed to LPS.

Gene Ontology Annotations    Click to see Annotation Detail View

Biological Process
TermQualifierEvidenceWithReferenceNotesSourceOriginal Reference(s)
cellular response to lipopolysaccharide  IDA 10045884 RGD 
cellular response to tumor necrosis factor  IDA 10045884 RGD 

Objects Annotated

Genes (Rattus norvegicus)
Prpf8  (pre-mRNA processing factor 8)


Additional Information