ArticleMolecular and cellular endocrinology2012
Phorbol esters enhance 1α,25-dihydroxyvitamin D3-regulated 25-hydroxyvitamin D-24-hydroxylase (CYP24A1) gene expression through ERK-mediated phosphorylation of specific protein 3 (Sp3) in Caco-2 cells.
Article in Molecular and cellular endocrinology, 2012. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 9 papers.
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Who cites it
9 citing papers in PubMed, 11 citations in OpenAlex.
- Activation of Genes by Nuclear Receptor/Specificity Protein (Sp) Interactions in Cancer.Cancers · 2025Review
- Vitamin D regulation of HAS2, hyaluronan synthesis and metabolism in triple negative breast cancer cells.The Journal of steroid biochemistry and molecular biology · 2020Article
- 1,25-dihydroxyvitamin DBMC oral health · 2019Article
- Physiological TLR5 expression in the intestine is regulated by differential DNA binding of Sp1/Sp3 through simultaneous Sp1 dephosphorylation and Sp3 phosphorylation by two different PKC isoforms.Nucleic acids research · 2016Article
- The Non-Genomic Actions of Vitamin D.Nutrients · 2016Review
- The effect of 1,25 dihydroxyvitamin D3 treatment on the mRNA levels of β catenin target genes in mice with colonic inactivation of both APC alleles.The Journal of steroid biochemistry and molecular biology · 2015Review
- Role of proinflammatory cytokines on expression of vitamin D metabolism and target genes in colon cancer cells.The Journal of steroid biochemistry and molecular biology · 2014Review
- VDR activity is differentially affected by Hic-5 in prostate cancer and stromal cells.Molecular cancer research : MCR · 2014Article
- Nuclear receptors and epigenetic regulation: opportunities for nutritional targeting and disease prevention.Advances in nutrition (Bethesda, Md.) · 2014Review
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Authors and funding
2 authors at 1 institution in 1 country.
Funding
Abstract
Phorbol 12-myristate 13-acetate (PMA) increased 1,25(OH)(2)D(3)-induced human 25 hydroxyvitamin d-24 hydroxylase (hCYP24A1) gene expression and vitamin D receptor (VDR) binding to the hCYP24A1 promoter. It did not alter transient receptor potential cation channel, subfamily V, member 6 (TRPV6) expression, VDR binding to the TRPV6 promoter, or VDR binding to a crude chromatin preparation. PMA activated Extracellular signal-Regulated Kinases (ERK) 1/2 and p38 mitogen activated protein kinases (MAPK) and inhibiting these kinases reduced 1,25(OH)(2)D(3)-induced and PMA-enhanced hCYP24A1 promoter activity. Mithramycin A inhibits Specific Protein (Sp) family member binding to DNA and reduced 1,25(OH)(2)D(3)-induced and PMA-enhanced hCYP24A1 promoter activity. Sp1 or Sp3 siRNA knockdown reduced 1,25(OH)(2)D(3)-regulated hCYP24A1 promoter activity but only Sp3 siRNA reduced PMA-enhanced hCYP24A1 promoter activity. PMA increased MAPK-dependent Sp3 phosphorylation, Sp3-VDR interactions, and Sp3 binding to the hCYP24A1 promoter. These data suggest that MAPK signaling contributes to 1,25(OH)(2)D(3)-induced and PMA-enhanced CYP24A1 gene transcription by modulating Sp3 function.
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Registered trials
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