ArticleProceedings of the National Academy of Sciences of the United States of America1998
Identification of hepatic nuclear factor 1 binding sites in the 5' flanking region of the human phenylalanine hydroxylase gene: implication of a dual function of phenylalanine hydroxylase stimulator in the phenylalanine hydroxylation system.
Article in Proceedings of the National Academy of Sciences of the United States of America, 1998. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 8 papers.
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8 citing papers in PubMed, 29 citations in OpenAlex.
- Article
- New PAH gene promoter KLF1 and 3'-region C/EBPalpha motifs influence transcription in vitro.Journal of applied genetics · 2017Article
- Metabolomics identifies novel Hnf1alpha-dependent physiological pathways in vivo.Molecular endocrinology (Baltimore, Md.) · 2010Article
- Effects of dietary glycerol on the expression of pterin carbinolamine dehydratase in the rat.The Biochemical journal · 2003Article
- Definition and prediction of the full range of transcription factor binding sites--the hepatocyte nuclear factor 1 dimeric site.Nucleic acids research · 2002Article
- Dimerization co-factor of hepatocyte nuclear factor 1/pterin-4alpha-carbinolamine dehydratase is necessary for pigmentation in Xenopus and overexpressed in primary human melanoma lesions.The American journal of pathology · 2001Article
- Differential expression of chicken dimerization cofactor of hepatocyte nuclear factor-1 (DcoH) and its novel counterpart, DcoHalpha.The Biochemical journal · 2001Article
- Tetrahydrobiopterin biosynthesis, regeneration and functions.The Biochemical journal · 2000Review
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2 authors at 1 institution in 1 country.
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No grant is acknowledged in the PubMed record.
Abstract
Phenylalanine hydroxylase stimulator (PHS) is a component of the phenylalanine hydroxylation system that is involved in the regeneration of the cofactor tetrahydrobiopterin. It is also identical to the dimerization cofactor of hepatocyte nuclear factor 1 (HNF1) (DCoH) that is able to enhance the transcriptional activity of HNF1. Moreover, it has the structural potential for binding macromolecules such as proteins and nucleic acids, consistent with its involvement in gene expression. We investigated whether PHS/DCoH could enhance the expression of phenylalanine hydroxylase (PAH). Cotransfection assays showed that DCoH itself could not transactivate the 9-kb human PAH 5' flanking fragment. However, this 9-kb fragment was transactivated by HNF1 in a dose-dependent manner with a maximum of nearly 8-fold activation; DCoH potentiated this transactivation by another 1.6-fold. The HNF1 binding sites were located at -3.5 kb in a region that is 77.5% identical to the mouse liver-specific hormone-inducible PAH gene enhancer. This study suggests a possible dual function of PHS in vivo in the human phenylalanine hydroxylation system: it is involved in the regeneration of the cofactor tetrahydrobiopterin and can also enhance the expression of the human PAH gene.
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