Eukaryotic translation initiation factor 4E binding protein 1, or 4EBP1, is an mRNA translational repressor protein that negatively regulates eukaryotic translation initiation factor 4E, or EIF4E. EIF4E is a protein that forms a complex necessary to block the 5’ ends of mRNA with a 7-methyl-guanosine five-prime cap structure, which is important for normal translation of mRNA. Specifically, the EIF4E complex recruits 40s ribosome subunits to scan mRNA in order to regulate protein synthesis. When EIF4E is bound to 4EBP1, it is held in an inactive state, however phosphorylation of 4EBP1 will cause its release. While 4EBP1 has broad implications in translational research, the following articles hone in on how a 4EBP1 antibody plays a role in the regulation of skeletal muscle protein synthesis.
4EBP1 Antibody [NB200-157] - Human breast carcinoma. Antibody used at a dilution of 1:20,000 (0.05ug/ml).
Norton et al used a 4EBP1 antibody in their research of how leucine content in a meal directs peak activation of skeletal muscle protein synthesis in rats. To start, leucine had already been established as a regulator of muscle protein synthesis by activating mRNA translation factors through the mTOR pathway. With this in mind, time course changes in 4EBP1 were measured using a 4EBP1 antibody in western blot to show that phosphorylation of 4EBP1 increased after meal intake. However, 4EBP1 activity did not slow down 180 minutes post meal intake, leading these researchers to believe that a specific threshold of Leucine concentration is required in order to see its full effect on skeletal muscle mRNA.
Next, Wilson et al also used a 4EBP1 antibody in research surround feeding and skeletal muscle protein synthesis in neonatal pigs. First, the 4EBP1 antibody was used in immunoblot to demonstrate that phosphorylation of 4EBP1 increased 30 minutes post feeding and maintained its high expression until 60 minutes thereafter. However, similar to the prior study, the rates of protein synthesis were only increased for a limited time after a feeding, and while they were associated with EIF4E and 4EBP1 correlation, frequent feeding remains the preferred method to increase muscle mass.
Finally, Lang et al used a 4EBP1 antibody to investigate delayed recovery of skeletal muscle mass after hind limb immobilization. It has already been established that the impairment of muscle protein synthesis is due to a reduction in the phosphorylation of 4EBP1 and S6K1. Therefore, a total 4EBP1 antibody and a phospho-4EBP1 antibody were used in western blot on hind limb immobilized mice to measure 4EBP1 activity. As expected, the immobilization did in fact decrease the phosphorylation of 4EBP1 as compared to total 4EBP1 levels. The 4EBP1 antibody was also used in an immunoprecipitation assay to examine the interaction between raptor and 4EBP1, as well as S6K1, PRAS40 and Deptor. These results concluded that a decrease in raptor and 4EBP1 was correlated with decreased protein synthesis.
View all 4EBP1 antibodies for your research.
