Endotoxin (LPS) stimulates 4E-BP1/PHAS-I phosphorylation in macrophages

The Journal of Surgical Research
M W PotterM P Callery

Abstract

Translational control of cytokine production in endotoxin (LPS)-stimulated macrophages is poorly characterized but likely important. An early step in protein translation is engagement of mRNA by eukaryotic initiation factor 4E (eIF-4E). Translation initiation can be prevented by small 4E-binding proteins (4E-BP1 or PHAS-I) which must be phosphorylated in order to disengage eIF-4E. We examined whether LPS alters 4E-BP1 phosphorylation in macrophages. Elicited rat peritoneal macrophages and Raw 264.7 macrophages were treated with signal transduction inhibitors and then LPS. Cells were harvested and equal protein amounts were electrophoresed (SDS-PAGE). Western blots (WB) were developed with 4E-BP1 antibody. Alternatively cell lysates were exposed to 7-methyl GTP Sepharose beads in order to isolate the cap-binding protein eIF-4E. The relative amounts of 4E-BP1 associated with eIF-4E were then determined by WB. Macrophage 4E-BP1 is phosphorylated upon stimulation by LPS as evidenced by the appearance of a more slowly migrating gamma (hyperphosphorylated) band on gel electrophoresis. Inhibition of both the p42/p44 MAPK pathway (PD 98059) and the p38 MAPK pathway (SB 203580) failed to alter LPS-induced 4E-BP1 phosphorylation. Rapamyc...Continue Reading

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Citations

Apr 16, 2008·Neuropathology : Official Journal of the Japanese Society of Neuropathology·Karin BoerEleonora Aronica
Feb 13, 2014·Immunology and Cell Biology·Mena Abdel-NourStephen E Girardin
Jun 17, 2009·Toxicology in Vitro : an International Journal Published in Association with BIBRA·Sandra VerstraelenRosette Van Den Heuvel
Sep 11, 2010·The Journal of Surgical Research·Valérie SchaefferRonald V Maier
Aug 3, 2013·Journal of Neuroimmunology·Jiao-Jiang HeHui Yang
Oct 20, 2007·The Journal of Immunology : Official Journal of the American Association of Immunologists·Mei-Jen WangWu-Fu Chen

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