Regulation of Peroxisome Proliferator-Activated Receptors by E6-Associated Protein
2008
How E6-Associated Protein Affects PPARs
Sample size: 10
publication
10 minutes
Evidence: moderate
Author Information
Author(s): Gopinathan Lakshmi, Hannon Daniel B., Smith III Russell W., Peters Jeffrey M., Vanden Heuvel John P.
Primary Institution: The Pennsylvania State University
Hypothesis
E6-AP regulates the activity of peroxisome proliferator-activated receptors (PPARs).
Conclusion
E6-AP inhibits the transcriptional activity of PPARα and decreases the basal mRNA levels of its target genes.
Supporting Evidence
- E6-AP inhibited the ligand-independent transcriptional activity of PPARα and PPARβ.
- Inhibition of PPARα activity required the ubiquitin ligase function of E6-AP.
- E6-AP mRNA and protein levels were significantly increased in wildtype mice in response to clofibrate.
Takeaway
E6-AP is a protein that can stop other proteins called PPARs from working properly, which helps control how our bodies use fats and sugars.
Methodology
The study involved transfecting cells with E6-AP and measuring the effects on PPAR activity and target gene expression.
Participant Demographics
8-week old male wild-type and PPARα-null mice were used.
Statistical Information
P-Value
p<0.05
Statistical Significance
p<0.05
Digital Object Identifier (DOI)
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