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- W972283446 abstract "The hormone gastrin helps maintain gastric mucosal integrity by regulating expression of genes such as plasminogen activator inhibitor 2 (PAI-2) and Regenerating protein 1 (Reg1) , but the mechanisms involved are incompletely understood. We hypothesized that the proteasome beta subunit PSMB1, recently implicated in the gastrin responsiveness of vesicular monoamine transporter 2, may be required for gastrin-mediated upregulation of PAI-2 and Reg1. PSMB1 was knocked down by siRNA in the gastric cancer cell line AGS-GR, which expresses the cholecystokinin 2 receptor, and the gastrin response to PAI-2 (1.6kb) and Reg1 (2.1kb) promoter-luciferase reporter constructs determined. In control cells (scrambled RNA) gastrin (2nM G17 for 6h) increased PAI-2 transcription by 9.2±1.5 fold (n=6), but in cells with PSMB1 knocked down (69.5±5.5% protein reduction), this was significantly reduced to 2.1±0.2 fold (p,0.001, ANOVA). In control cells, gastrin increased Reg1 transcription by 2.4±0.9 fold (n=9), but with PSMB1 knocked down, the response was abolished (1.2±0.1 fold, p,0.03). To investigate PSMB1 binding to the promoters, ChIP assays were performed using an anti-PSMB1 antibody for immunoprecipitation, or IgG control. In anti-PSMB1 precipitated chromatin from cells treated with gastrin (2nM G17 for 2h), there was a 7.9±2.5 (n=3) fold enrichment of DNA compared to control, determined by real time PCR using primers that generated a 250bp amplicon incorporating the region of the PAI-2 promoter known to respond to gastrin. Using primers generating a 218bp amplicon including the gastrin responsive region of the Reg1 promoter we observed 10.0±4.6 fold enrichment. Immunocytochemistry of unstimulated AGS-GR cells revealed distribution of PSMB1 throughout the cytoplasm and nucleus. After 2h stimulation with 2nM G17, cytoplasmic PSMB1 was barely detectable and nuclear staining was intensified; after 6h stimulation, PSMB1 was again visible in cytoplasm. Western blotting of nuclear and cytoplasmic extracts showed that the nuclear:cytoplasmic ratio of PSMB1 changed from 1.7±0.4 in untreated cells to 10.6±2.6 (n=7, p,0.01) after 2h stimulation with G17. This subcellular redistribution was not seen with alpha (PSMA5) or regulatory (PSMC1) proteasome subunits. PSMB1 distribution was unaffected by activation of other receptors expressed by AGS-GR cells, including histamine, epidermal growth factor, PGE2, or IL-8. The response to G17 was however mimicked by phorbol 12-myristate 13-acetate (0.1μM), and prevented by the protein kinase C (PKC) antagonist Ro-32-0432 (1μM). We conclude that proteasome beta subunits bind to the PAI-2 and Reg1 promoters in response to gastrin stimulation of AGSGR cells and are required for transcription. Gastrin induces a PKC-dependent subcellular redistribution of beta proteasome subunits that may be linked to their transcriptional functions." @default.
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- W972283446 date "2013-05-01" @default.
- W972283446 modified "2023-09-27" @default.
- W972283446 title "Sa1738 Crosstalk Between PKD1 and β-Catenin Signaling Pathways in Intestinal Epithelial Cells" @default.
- W972283446 doi "https://doi.org/10.1016/s0016-5085(13)61050-1" @default.
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