ArticleBiochemical and biophysical research communications2012
Mdm2 is a novel activator of ApoCIII promoter which is antagonized by p53 and SHP inhibition.
Article in Biochemical and biophysical research communications, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 7 papers.
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The abstract states no effect estimate the extractor could read, or names no intervention and outcome on the map, so this paper lights no cell and moves no belief. It is still indexed, cited and linked below.
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Who cites it
7 citing papers in PubMed, 9 citations in OpenAlex.
- A Novel Role for RARα Agonists as Apolipoprotein CIII Inhibitors Identified from High Throughput Screening.Scientific reports · 2017Article
- Nuclear Receptors as Therapeutic Targets in Liver Disease: Are We There Yet?Annual review of pharmacology and toxicology · 2016Review
- Serum differential protein identification of Xinjiang Kazakh esophageal cancer patients based on the two-dimensional liquid-phase chromatography and LTQ MS.Molecular biology reports · 2014Article
- MicroRNA-433 inhibits liver cancer cell migration by repressing the protein expression and function of cAMP response element-binding protein.The Journal of biological chemistry · 2013Article
- A feedback inhibition between miRNA-127 and TGFβ/c-Jun cascade in HCC cell migration via MMP13.PloS one · 2013Article
- An autoregulatory feedback loop between Mdm2 and SHP that fine tunes Mdm2 and SHP stability.FEBS letters · 2012Article
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Authors and funding
3 authors at 2 institutions in 1 country.
Funding
Abstract
We examined the effect of Mdm2 on regulation of the ApoCIII promoter and its cross-talk with p53 and nuclear receptor SHP. Overexpression of Mdm2 markedly enhanced ApoCIII promoter activity by HNF4α. A direct association of Mdm2 protein with the HNF4α protein was observed by co-immunoprecipitation. Ectopic expression of p53 decreased HNF4α activation of the ApoCIII promoter and antagonized the effect of Mdm2. Co-expression of SHP further strengthened p53 inhibition and abolished Mdm2 activation of the ApoCIII promoter. Mdm2 inhibited p53-mediated enrichment of HNF4α to the ApoCIII promoter while simultaneously reducing p53 binding and increasing recruitment of SHP to the ApoCIII promoter. The results from this study implicate a potentially important function of Mdm2 in regulation of lipoprotein metabolism.
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