Short communicationIsolation and characterization of a third isoform of human hepatocyte nuclear factor 4
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Constitutive expression of cytochrome P450 in foetal and adult porcine livers—Effects of body weight
2016, Toxicology LettersCitation Excerpt :Interestingly, two additionally bands of a lower molecular weight were detected in the adult pigs as well. These band could be due to truncated versions of HNF4 (Navas et al., 1999; Kritis et al., 1996). During the development of the liver from the foetal stage into adulthood a large number of adaptations occur.
Proteomic analysis of native hepatocyte nuclear factor-4α (HNF4α) isoforms, phosphorylation status, and interactive cofactors
2011, Journal of Biological ChemistryCitation Excerpt :The phosphorylation of HNF4α regulates specific genes by affecting DNA binding and/or cofactor recruitment (15–18). The HNF4α isoforms are generated by alternative promoters together with alternative splicing of the corresponding exons (19–21). Although partially redundant, specific isoforms modulate transcriptional activity, cofactor recruitment, and specific gene regulation (22–25).
Novel P2 promoter-derived HNF4α isoforms with different N-terminus generated by alternate exon insertion
2009, Experimental Cell ResearchStructural basis of natural promoter recognition by a unique nuclear receptor, HNF4α: Diabetes gene product
2008, Journal of Biological ChemistryCitation Excerpt :However, the same vector constructs were used, either performing or skipping a tobacco etch virus (TEV) protease digestion to remove or retain the MBP tag. The cDNA harboring the full-length human HNF-4αB splice variant (35) was a kind gift from Dr. Steve Shoelson from Joslin Diabetes Center. A modified MBP fusion expression vector, pET41a MBP, was used for our studies.
Hepatic scavenger receptor class B, type I is stimulated by peroxisome proliferator-activated receptor γ and hepatocyte nuclear factor 4α
2003, Biochemical and Biophysical Research CommunicationsCitation Excerpt :Furthermore, LXRα/RXR stimulated SR-BI promoter activity approximately equally in both Hepa 1c1c-7 cells and COS-7 cells [34]. We found that the liver-enriched factor HNF4α [44–46], not found endogenously in COS-7 cells [47], is able to induce SR-BI promoter activity. The weaker transactivation of SR-BI mediated by HNF4α in COS-7 cells compared to Hepa 1c1c-7 cells further indicates that HNF4α acts in concert with a liver-enriched transcription factor.