ArticleThe Biochemical journal2006
NF-Y and Sp1/Sp3 are involved in the transcriptional regulation of the peptidylarginine deiminase type III gene (PADI3) in human keratinocytes.
Article in The Biochemical journal, 2006. The graph could read no effect estimate from its abstract, so it casts no vote on the map. Cited by 14 papers, 1 of them a synthesis that pooled it.
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Who cites it
14 citing papers in PubMed, 1 synthesis or guideline pooled it, 39 citations in OpenAlex.
- Role of the PADI family in inflammatory autoimmune diseases and cancers: A systematic review.Frontiers in immunology · 2023Pooled it
- Unveiling nuclear localization signals in human arginine deiminase proteins.Protein science : a publication of the Protein Society · 2026Article
- Review
- Deimination in epidermal barrier and hair formation.Philosophical transactions of the Royal Society of London. Series B, Biological sciences · 2023Review
- Article
- Structural characterization of human peptidyl-arginine deiminase type III by X-ray crystallography.Acta crystallographica. Section F, Structural biology communications · 2021Article
- PADI3 induces cell cycle arrestCancer biology & medicine · 2019Article
- Marine biogenics in sea spray aerosols interact with the mTOR signaling pathway.Scientific reports · 2019Article
- Article
- Transcriptome analysis of psoriasis in a large case-control sample: RNA-seq provides insights into disease mechanisms.The Journal of investigative dermatology · 2014Article
- Modulation of calcium-induced cell death in human neural stem cells by the novel peptidylarginine deiminase-AIF pathway.Biochimica et biophysica acta · 2014Article
- Bleomycin hydrolase is regulated biphasically in a differentiation- and cytokine-dependent manner: relevance to atopic dermatitis.The Journal of biological chemistry · 2011Article
- Deimination is regulated at multiple levels including auto-deimination of peptidylarginine deiminases.Cellular and molecular life sciences : CMLS · 2010Article
- Article
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Authors and funding
11 authors at 4 institutions in 2 countries.
Funding
No grant is acknowledged in the PubMed record.
Abstract
Human peptidylarginine deiminase type III gene (PADI3) encodes a crucial post-translational modification enzyme that converts protein-bound arginine residues into citrulline residues. Its expression is restricted to a few cell types, including keratinocytes in the granular layer of the epidermis and in the inner root sheath of hair follicles. In these cells, the enzyme is involved in terminal processing of intermediate filament-binding proteins such as filaggrin and trichohyalin. To study the molecular mechanisms that control the expression of PADI3 in human keratinocytes at the transcriptional level, we characterized its promoter region using human keratinocytes transfected with variously deleted fragments of the 5'-upstream region of PADI3 coupled to the luciferase gene. We found that as few as 129 bp upstream from the transcription initiation site were sufficient to direct transcription of the reporter gene. Electrophoretic mobility-shift and chromatin immunoprecipitation assays revealed that NF-Y (nuclear factor Y) and Sp1/Sp3 (specificity protein 1/3) bind to this region in vitro and in vivo. Moreover, mutation of the Sp1- or NF-Y-binding motif markedly reduced PADI3 promoter activity. Furthermore, Sp1 or NF-YA (NF-Y subunit) small interfering RNAs effectively diminished PADI3 expression in keratinocytes cultured in both low- and high-calcium medium. These data indicate that PADI3 expression is driven by Sp1/Sp3 and NF-Y binding to the promoter region.
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